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Information on EC 7.4.2.5 - bacterial ABC-type protein transporter and Organism(s) Homo sapiens and UniProt Accession Q03518
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7.4.2.5 bacterial ABC-type protein transporterIUBMB Comments
An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. This entry stands for a family of bacterial enzymes that are dedicated to the secretion of one or several closely related proteins belonging to the toxin, protease and lipase families. Examples from Gram-negative bacteria include alpha-hemolysin, cyclolysin, colicin V and siderophores, while examples from Gram-positive bacteria include bacteriocin, subtilin, competence factor and pediocin.
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Word Map
- 7.4.2.5
-
caco-2
- tripeptides
- jejunum
-
gly-sar
-
glycylsarcosine
-
secyeg
- xenopus
- oocyte
-
histocompatibility
-
multidrug
-
prodrugs
- p-glycoprotein
-
enterocytes
- duodenum
-
peptidomimetic
- beta-lactams
- preproteins
-
basolateral
- ileum
- cephalexin
- laevis
-
peptide-like
-
translocons
-
transepithelial
-
brush-border
-
carrier-mediated
-
h+-coupled
-
villus
-
electrogenic
-
pepts
-
proton-dependent
- valacyclovir
- acyclovir
-
transporter-mediated
-
tapasin
- carnosine
-
sec-dependent
-
paracellular
-
membrane-embedded
-
two-electrode
- bestatin
- oct1
-
oatp2b1
-
oatps
-
antigen-processing
- gly-gly
- cefixime
-
i-restricted
-
apical-to-basolateral
-
serine-rich
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
pept1, peptide transporter, pept2, seca2, abc transport, seca protein, peptide transporter 1, abcb10, seca1, seca atpase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ABCB8
ABCB9
peptide transporter
peptide-transporting ATPase
TAPL
peptide-transporting ATPase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
transmembrane transport
hydolysis of phosphoric ester
-
-
-
-
transmembrane transport
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (ABC-type, peptide-exporting)
An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. This entry stands for a family of bacterial enzymes that are dedicated to the secretion of one or several closely related proteins belonging to the toxin, protease and lipase families. Examples from Gram-negative bacteria include alpha-hemolysin, cyclolysin, colicin V and siderophores, while examples from Gram-positive bacteria include bacteriocin, subtilin, competence factor and pediocin.
CAS REGISTRY NUMBER
COMMENTARY
9000-83-3
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O + cefadroxil/in
ADP + phosphate + cefadroxil/out
-
preferable substrate
-
-
?
ATP + H2O + CRYQKSTEL/in
ADP + phosphate + CRYQKSTEL/out
-
peptide transport assay, fluorescein is coupled via the cysteine
-
-
?
ATP + H2O + D-phenylglycine-L-Dopa/in
ADP + phosphate + D-phenylglycine-L-Dopa/out
-
-
-
-
?
ATP + H2O + delta-aminolevulinic acid/in
ADP + phosphate + delta-aminolevulinic acid/out
-
-
-
-
?
ATP + H2O + formyl-methionyl-leucine-phenylalanine/in
ADP + phosphate + formyl-methionyl-leucine-phenylalanine/out
-
-
-
-
?
ATP + H2O + glycyl-sarcosine/in
ADP + phosphate + glycyl-sarcosine/out
-
-
-
-
?
ATP + H2O + guanidine oseltamivir carboxylate-L-Val/in
ADP + phosphate + guanidine oseltamivir carboxylate-L-Val/out
-
-
-
-
?
ATP + H2O + JBP485/in
ADP + phosphate + JBP485/out
-
JBP485 is cyclo-trans-4-L-hydroxyprolyl-L-serine
-
-
?
ATP + H2O + L-Ala-gamma-D-Glu-meso-diaminopimelic acid/in
ADP + phosphate + L-Ala-gamma-D-Glu-meso-diaminopimelic acid/out
-
-
-
-
?
ATP + H2O + L-Val-didanosine/in
ADP + phosphate + L-Val-didanosine/out
-
didanosine is also named Videx or 5'-O-2'-3'-dideoxydidanosine
-
-
?
ATP + H2O + major histocompatibility complex class I molecules/in
ADP + phosphate + major histocompatibility complex class I molecules/out
-
-
-
-
?
ATP + H2O + muramyl dipeptide/in
ADP + phosphate + muramyl dipeptide/out
-
-
-
-
?
ATP + H2O + NP-647/in
ADP + phosphate + NP-647/out
-
NP-647 is L-pGlu-(2-propyl)-L-His-L-ProNH2
-
-
?
ATP + H2O + oseltamivir carboxylate/in
ADP + phosphate + oseltamivir carboxylate/out
-
the enzyme is not implicated in the oral absorption of oseltamivir carboxylate
-
-
?
ATP + H2O + oseltamivir/in
ADP + phosphate + oseltamivir/out
-
the enzyme is not implicated in the oral absorption of oseltamivir
-
-
?
ATP + H2O + RCYQKSTEL/in
ADP + phosphate + RCYQKSTEL/out
-
peptide transport assay, fluorescein is coupled via the cysteine
-
-
?
ATP + H2O + RRCQKSTEL/in
ADP + phosphate + RRCQKSTEL/out
-
peptide transport assay, fluorescein is coupled via the cysteine
-
-
?
ATP + H2O + RRYQCSTEL/in
ADP + phosphate + RRYQCSTEL/out
-
peptide transport assay, fluorescein is coupled via the cysteine
-
-
?
ATP + H2O + RRYQKCTEL/in
ADP + phosphate + RRYQKCTEL/out
-
peptide transport assay, fluorescein is coupled via the cysteine
-
-
?
ATP + H2O + RRYQKSCEL/in
ADP + phosphate + RRYQKSCEL/out
-
peptide transport assay, fluorescein is coupled via the cysteine
-
-
?
ATP + H2O + RRYQKSTCL/in
ADP + phosphate + RRYQKSTCL/out
-
peptide transport assay, fluorescein is coupled via the cysteine
-
-
?
ATP + H2O + RRYQKSTEC/in
ADP + phosphate + RRYQKSTEC/out
-
peptide transport assay, fluorescein is coupled via the cysteine
-
-
?
ATP + H2O + peptide/in
ADP + phosphate + peptide/out
-
-
-
-
?
ATP + H2O + peptide/in
ADP + phosphate + peptide/out
-
TAPL is a half-type ABC transporter that localizes in lysosome and putatively conveys peptides from cytosol to lysosome
-
-
?
ATP + H2O + peptide/in
ADP + phosphate + peptide/out
the enzyme translocates cytosolic peptides into the lumen of lysosomes driven by the hydrolysis of ATP
-
-
?
ATP + H2O + RRYCKSTEL/in
ADP + phosphate + RRYCKSTEL/out
-
peptide transport assay, fluorescein is coupled via the cysteine
-
-
?
ATP + H2O + RRYCKSTEL/in
ADP + phosphate + RRYCKSTEL/out
-
substrate in peptide transport assay, fluorescein coupled via a cyteine residue
-
-
?
ATP + H2O + RRYQNSTCL/in
ADP + phosphate + RRYQNSTCL/out
-
peptide transport assay, fluorescein is coupled via the cysteine
-
-
?
ATP + H2O + RRYQNSTCL/in
ADP + phosphate + RRYQNSTCL/out
-
substrate in peptide transport assay, fluorescein coupled via a cyteine residue
-
-
?
additional information
?
-
ABCB2 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB2 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB2 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB2 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB2 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
-
ABCB2 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
-
ATPase activity associated with transporter associated with antigen processing, TAP. Role of TAP in peptide loading of MHC molecules and the overall process of antigen presentation
-
-
?
additional information
?
-
-
coordinated dialogue between peptide binding site, nucleotide-binding domain, and the translocation site
-
-
?
additional information
?
-
ABCB10 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis. ABCB10 plays physiological role in antigen processing
-
-
?
additional information
?
-
ABCB10 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis. ABCB10 plays physiological role in antigen processing
-
-
?
additional information
?
-
ABCB10 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis. ABCB10 plays physiological role in antigen processing
-
-
?
additional information
?
-
ABCB10 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis. ABCB10 plays physiological role in antigen processing
-
-
?
additional information
?
-
ABCB10 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis. ABCB10 plays physiological role in antigen processing
-
-
?
additional information
?
-
-
ABCB10 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis. ABCB10 plays physiological role in antigen processing
-
-
?
additional information
?
-
ABCB3 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB3 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB3 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB3 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB3 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
-
ABCB3 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB8 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB8 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB8 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB8 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB8 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
-
ABCB8 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB9 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB9 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB9 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB9 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB9 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
-
ABCB9 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
-
the enzyme binds ATP, ADP, GTP, and dATP, UTP, and CTP to a lower extent, but not AMP
-
-
?
additional information
?
-
-
permeation of cationic antimicrobial di- and tripeptides derived from lactoferricin and test for interaction with PEPT1, none serves as a substrate
-
-
?
additional information
?
-
-
using the two-electrode, voltage-clamp technique at Xenopus laevis oocytes, strong hPEPT1-specific inward transport currents are recorded for glycylsarcosine, anserine and carnosine, but not for glycine
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O + formyl-methionyl-leucine-phenylalanine/in
ADP + phosphate + formyl-methionyl-leucine-phenylalanine/out
-
-
-
-
?
ATP + H2O + L-Ala-gamma-D-Glu-meso-diaminopimelic acid/in
ADP + phosphate + L-Ala-gamma-D-Glu-meso-diaminopimelic acid/out
-
-
-
-
?
ATP + H2O + major histocompatibility complex class I molecules/in
ADP + phosphate + major histocompatibility complex class I molecules/out
-
-
-
-
?
ATP + H2O + muramyl dipeptide/in
ADP + phosphate + muramyl dipeptide/out
-
-
-
-
?
ATP + H2O + peptide/in
ADP + phosphate + peptide/out
-
-
-
-
?
ATP + H2O + peptide/in
ADP + phosphate + peptide/out
-
TAPL is a half-type ABC transporter that localizes in lysosome and putatively conveys peptides from cytosol to lysosome
-
-
?
ATP + H2O + peptide/in
ADP + phosphate + peptide/out
the enzyme translocates cytosolic peptides into the lumen of lysosomes driven by the hydrolysis of ATP
-
-
?
additional information
?
-
ABCB2 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB2 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB2 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB2 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB2 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
-
ABCB2 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
-
ATPase activity associated with transporter associated with antigen processing, TAP. Role of TAP in peptide loading of MHC molecules and the overall process of antigen presentation
-
-
?
additional information
?
-
ABCB10 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis. ABCB10 plays physiological role in antigen processing
-
-
?
additional information
?
-
ABCB10 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis. ABCB10 plays physiological role in antigen processing
-
-
?
additional information
?
-
ABCB10 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis. ABCB10 plays physiological role in antigen processing
-
-
?
additional information
?
-
ABCB10 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis. ABCB10 plays physiological role in antigen processing
-
-
?
additional information
?
-
ABCB10 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis. ABCB10 plays physiological role in antigen processing
-
-
?
additional information
?
-
-
ABCB10 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis. ABCB10 plays physiological role in antigen processing
-
-
?
additional information
?
-
ABCB3 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB3 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB3 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB3 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB3 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
-
ABCB3 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB8 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB8 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB8 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB8 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB8 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
-
ABCB8 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB9 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB9 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB9 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB9 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB9 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
-
ABCB9 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-biphenyl-L-alanyl-L-arginine methyl ester
-
peptide derived from lactoferricin, at 1 mM, 10% inhibition of glycylsarcosine-induced current
cisplatin
-
IC50 value for growth inhibition of cell line PC-3 0.0033 mM, DU-145 0.0045 mM, 2008 0.0194 mM, C-13 0.117 mM, L-540 0.0025 mM
Fv fragment of the monoclonal antibody mAb148.3
-
Fv binding to the C terminus of TAP1
-
RWR-NH(benzyl)
-
peptide derived from lactoferricin, at 1 mM, 87% inhibition of glycylsarcosine-induced current, peptide can also impair membrane protein functions in an unspecific manner
RWR-NH2
-
peptide derived from lactoferricin, at 1 mM, 15% inhibition of glycylsarcosine-induced current
[AuIIIBr2(dtc-Sar-Aib-O(t-Bu))]
-
IC50 value for growth inhibition of cell line PC-3 0.0008 mM, DU-145 0.0014 mM, 2008 0.0045 mM, C-13 0.0037 mM, L-540 0.0015 mM
[AuIIICl2(dtc-Sar-Aib-O(t-Bu))]
-
IC50 value for growth inhibition of cell line PC-3 0.0011 mM, DU-145 0.0022 mM, 2008 0.0047 mM, C-13 0.0051 mM, L-540 0.0017 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00000022
0.00000026
0.0000003
-
peptide transport rate, K545A/H699A mutant, in the presence of 3 mM ATP and 1 mM orthovanadate
0.00000035
-
peptide transport rate, wild type, in the presence of 3 mM ATP and 500 microM competitor peptide RRYQKSTEL
0.00000039
-
peptide transport rate, K545A/H699A mutant, in the presence of 3 mM AMP
0.000003
-
peptide transport rate, TAPL reconstitution in liposomes of defined lipid composition, DOPC-eggPG, 9 to 1
0.000004
-
peptide transport rate, TAPL reconstitution in liposomes of defined lipid composition, DOPC-DOPE, 9 to 1
0.000006
-
peptide transport rate, TAPL reconstituted in liposomes prepared from bovine heart lipids
0.000011
-
peptide transport rate, TAPL reconstituted in liposomes prepared from bovine brain lipids
0.000023
-
peptide transport rate, TAPL reconstituted in liposomes prepared from bovine liver lipids
0.000045
-
peptide transport rate, TAPL reconstituted in liposomes prepared from Escherichia coli lipids, 100% phosphatidylcholine
0.00007
-
peptide transport rate, TAPL reconstitution in liposomes composed of DOPC and 90% DOPS
0.000075
-
peptide transport rate, TAPL reconstitution in liposomes of defined lipid composition, DOPC-DOPA, 9 to 1
0.000095
-
peptide transport rate, TAPL reconstitution in liposomes composed of DOPC and 10% DOPS
0.000115
-
peptide transport rate, TAPL reconstituted in liposomes prepared from Escherichia coli lipids, 70% phosphatidylcholine
0.000135
-
peptide transport rate, TAPL reconstitution in liposomes of defined lipid composition, DOPC-DOPS, 9 to 1
0.000245
-
peptide transport rate, TAPL reconstitution in liposomes composed of DOPC and 70% DOPS
0.00026
-
peptide transport rate, TAPL reconstitution in liposomes composed of DOPC and 30% DOPS
0.00042
-
peptide transport rate, TAPL reconstituted in liposomes prepared from Escherichia coli lipids
0.000423
-
peptide transport rate, TAPL reconstitution in liposomes composed of DOPC and 50% DOPS
0.000505
-
peptide transport rate, TAPL reconstitution in Eschericha coli liposomes, for comparison
0.000535
-
peptide transport rate, TAPL reconstitution in liposomes of defined lipid composition, for comparison in Eschericha coli liposomes
0.00055
-
peptide transport rate, TAPL reconstituted in liposomes prepared from Escherichia coli lipids, no phosphatidylcholine
0.00127
-
peptide transport rate, TAPL reconstituted in liposomes prepared from Escherichia coli lipids, 50% phosphatidylcholine
0.00132
-
peptide transport rate, TAPL reconstituted in liposomes prepared from Escherichia coli lipids, 10% phosphatidylcholine
0.00168
-
peptide transport rate, TAPL reconstituted in liposomes prepared from Escherichia coli lipids, 30% phosphatidylcholine
0.00000022
-
peptide transport rate, K545A/H699A mutant, in the presence of 3 mM ATP
0.00000022
-
peptide transport rate, wild type, in the presence of 3 mM ATP and 1 mM orthovanadate
0.00000026
-
peptide transport rate, K545A/H699A mutant, in the presence of 3 mM ATP and 500 microM competitor peptide RRYQKSTEL
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
TAPL expression is strongly induced during differentiation of monocytes to dendritic cells and to macrophages
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
the enzyme contributes to water absorption in the colon
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
homodimer
-
TAPL forms a homodimer in the membrane and under the solubilized conditions
homodimer
-
dissected in TMD0 (residues 1-142), containing a C-terminal myc-tag, and the core complex (residues 143-766), which consists of the cytosolic linker L0. Core-TAPL is essential and sufficient for peptide transport
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
EPR spectroscopy using covalently attached 2,2,5,5-tetramethylpyrrolidine-1-oxyl spin probes, and 2,2,6,6-tetramethylpiperidine-1-oxyl-4-amino-4-carboxylic acid spin-labeled peptides. The side-chains' mobility is strongly restricted at the ends of the peptide, whereas the central region is flexible, suggesting a central peptide bulge. Peptides bind to TAP in an extended kinked structure, analogous to those bound to MHC class I proteins
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
mutant pairs of TAP1/TAP2 with mutation in ABC signature motif, C-loop. Chimera with two canonical C-loops show highest transport activity, chimera with two degenerate C-loops have lowest transport rates. All single mutants and chimera show similar activities in peptide or ATP binding
additional information
-
knockdown of the ABC transporter enzyme in WM793B cells by shRNA leads to increases the sensitivity of cells to doxorubicin and reduces the cell survival, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crude membranes containing TAPL are prepared from Sf9 insect cells, furthermore a SP Sepharose Fast Low column and a Zn2+-iminodiacetate column are used
-
recombinant TAPL from membranes of Drosophila melanogaster S2 cells by detergent solubilization, and ADP or ATP affinity chromatography, not by AMP affinity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a set of N-terminally truncated human TAP variants are generated, PCR products are cloned into the vector pFASTBac Dual for expression in the Baculovirus system
-
baculoviruses encoding a histidine-tagged and a green fluorescent protein tagged version of TAP1, and a yellow fluorescent protein-tagged version of TAP2 are obtained
-
human TAPL is cloned into pEGFP-N3 and pIRES2-EGFP resulting in TAPL with a C-terminal EGFP and TAPL co-translated EGFP, respectively, TAPL containing a C-terminal myc-tag is cloned into pcDNA3.1+, and into the retroviral vector pLPCX
-
isozyme 12A, expression of TAPL in membranes of Drosophila melanogaster S2 cells
-
recombinant baculovirus, encoding human TAP1 and TAP2, is used for infection of Sf9 cells, used for the peptide transport assay
-
TAPL containing a C-terminal His10 tag or a Strep-tag II is cloned for expression in Sf9 insect cells infected with recombinant baculovirus
-
the coding sequence of the nucleotide-binding domain of TAP1, amino acids 489-748, is cloned into the pET21a+ vector
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wandersman, C.
Protein and peptide secretion by ABC exporters
Res. Microbiol.
149
163-170
1998
Escherichia coli, Enterococcus faecalis, Gram-negative bacteria, Homo sapiens, Mus sp., Rattus norvegicus
Momburg, F.; Roelse, J.; Howard, J.C.; Butcher, G.W.; Hammerling, G.J.; Neefjes, J.J.
Selectivity of MHC-encoded peptide transporters from human, mouse and rat
Nature
367
648-651
1994
Homo sapiens, Mus sp., Rattus norvegicus
Chen, M.; Abele, R.; Tampe, R.
Functional non-equivalence of ATP-binding cassette signature motifs in the transporter associated with antigen processing (TAP)
J. Biol. Chem.
279
46073-46081
2004
Homo sapiens
Gorbulev, S.; Abele, R.; Tampe, R.
Allosteric crosstalk between peptide-binding, transport, and ATP hydrolysis of the ABC transporter TAP
Proc. Natl. Acad. Sci. USA
98
3732-3737
2001
Homo sapiens
Herget, M.; Tampe, R.
Intracellular peptide transporters in human - compartmentalization of the "peptidome"
Pflugers Arch.
453
591-600
2006
Homo sapiens (Q03518), Homo sapiens (Q03519), Homo sapiens (Q9NP78), Homo sapiens (Q9NRK6), Homo sapiens (Q9NUT2), Homo sapiens
Koch, J.; Guntrum, R.; Tampe, R.
The first N-terminal transmembrane helix of each subunit of the antigenic peptide transporter TAP is essential for independent tapasin binding
FEBS Lett.
580
4091-4096
2006
Homo sapiens
Ernst, R.; Koch, J.; Horn, C.; Tampe, R.; Schmitt, L.
Engineering ATPase activity in the isolated ABC cassette of human TAP1
J. Biol. Chem.
281
27471-27480
2006
Homo sapiens
Perria, C.L.; Rajamanickam, V.; Lapinski, P.E.; Raghavan, M.
Catalytic site modifications of TAP1 and TAP2 and their functional consequences
J. Biol. Chem.
281
39839-39851
2006
Homo sapiens
Demirel, O.; Waibler, Z.; Kalinke, U.; Gruenebach, F.; Appel, S.; Brossart, P.; Hasilik, A.; Tampe, R.; Abele, R.
Identification of a lysosomal peptide transport system induced during dendritic cell development
J. Biol. Chem.
282
37836-37843
2007
Homo sapiens
Zhao, C.; Haase, W.; Tampe, R.; Abele, R.
Peptide specificity and lipid activation of the lysosomal transport complex ABCB9 (TAPL)
J. Biol. Chem.
283
17083-17091
2008
Homo sapiens
Plewnia, G.; Schulze, K.; Hunte, C.; Tampe, R.; Koch, J.
Modulation of the antigenic peptide transporter TAP by recombinant antibodies binding to the last five residues of TAP1
J. Mol. Biol.
369
95-107
2007
Homo sapiens
Ohara, T.; Ohashi-Kobayashi, A.; Maeda, M.
Biochemical characterization of transporter associated with antigen processing (TAP)-like (ABCB9) expressed in insect cells
Biol. Pharm. Bull.
31
1-5
2008
Homo sapiens, Rattus norvegicus
Kawai, H.; Tanji, T.; Shiraishi, H.; Yamada, M.; Iijima, R.; Inoue, T.; Kezuka, Y.; Ohashi, K.; Yoshida, Y.; Tohyama, K.; Gengyo-Ando, K.; Mitani, S.; Arai, H.; Ohashi-Kobayashi, A.; Maeda, M.
Normal formation of a subset of intestinal granules in Caenorhabditis elegans requires ABC transporters HAF-4 and HAF-9, which are highly homologous to human lysosomal peptide transporter TAPL (TAP-like)
Mol. Biol. Cell
20
2979-2990
2009
Caenorhabditis elegans, Homo sapiens
Elliott, A.M.; Al-Hajj, M.
ABCB8 mediates doxorubicin resistance in melanoma cells by protecting the mitochondrial genome
Mol. Cancer Res.
7
79-87
2009
Homo sapiens
Demirel, O.; Bangert, I.; Tamp, R.; Abele, R.
Tuning the cellular trafficking of the lysosomal peptide transporter TAPL by its N-terminal domain
Traffic
11
383-393
2010
Homo sapiens
Geissler, S.; Zwarg, M.; Kntter, I.; Markwardt, F.; Brandsch, M.
The bioactive dipeptide anserine is transported by human proton-coupled peptide transporters
FEBS J.
277
790-795
2010
Homo sapiens, Rattus norvegicus
Flaten, G.; Kottra, G.; Stensen, W.; Isaksen, G.; Karstad, R.; Svendsen, J.; Daniel, H.; Svenson, J.
In vitro characterization of human peptide transporter hPEPT1 interactions and passive permeation studies of short cationic antimicrobial peptides
J. Med. Chem.
54
2422-2432
2011
Homo sapiens
Negom Kouodom, M.; Ronconi, L.; Celegato, M.; Nardon, C.; Marchiò, L.; Dou, Q.; Aldinucci, D.; Formaggio, F.; Fregona, D.
Toward the selective delivery of chemotherapeutics into tumor cells by targeting peptide transporters: Tailored gold-based anticancer peptidomimetics
J. Med. Chem.
55
2212-2226
2012
Homo sapiens
Herget, M.; Baldauf, C.; Schlz, C.; Parcej, D.; Wiesmller, K.; Tampe, R.; Abele, R.; Bordignon, E.
Conformation of peptides bound to the transporter associated with antigen processing (TAP)
Proc. Natl. Acad. Sci. USA
108
1349-1354
2011
Homo sapiens
Wuensch, T.; Schulz, S.; Ullrich, S.; Lill, N.; Stelzl, T.; Rubio-Aliaga, I.; Loh, G.; Chamaillard, M.; Haller, D.; Daniel, H.
The peptide transporter PEPT1 is expressed in distal colon in rodents and humans and contributes to water absorption
Am. J. Physiol. Gastrointest. Liver Physiol.
305
G66-G73
2013
Homo sapiens, Mus musculus, Rattus norvegicus
Brandsch, M.
Drug transport via the intestinal peptide transporter PepT1
Curr. Opin. Pharmacol.
13
881-887
2013
Homo sapiens, Mus musculus, Rattus norvegicus
Poirier, A.; Belli, S.; Funk, C.; Otteneder, M.B.; Portmann, R.; Heinig, K.; Prinssen, E.; Lazic, S.E.; Rayner, C.R.; Hoffmann, G.; Singer, T.; Smith, D.E.; Schuler, F.
Role of the intestinal peptide transporter PEPT1 in oseltamivir absorption: in vitro and in vivo studies
Drug Metab. Dispos.
40
1556-1565
2012
Homo sapiens, Rattus norvegicus
EXTERNAL LINKS (specific for EC-Number 7.4.2.5)
Transporter Classification Database (TCDB): 3.A.1.109.8
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