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Information on EC 3.4.16.5 - carboxypeptidase C and Organism(s) Mus musculus and UniProt Accession P16675

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.16 Serine-type carboxypeptidases
                3.4.16.5 carboxypeptidase C
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This record set is specific for:
Mus musculus
UNIPROT: P16675 not found.
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
release of a C-terminal amino acid with broad specificity
Synonyms
carboxypeptidase y, cathepsin a, catha, deamidase, serine carboxypeptidase, protective protein/cathepsin a, scpep1, procpy, carboxypeptidase yscy, carboxypeptidase-y, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
protective protein/cathepsin A
-
carboxypeptidase Y
-
-
-
-
carboxypeptidase YSCY
-
-
-
-
cathepsin A
-
-
-
-
CP-MI
-
-
-
-
CP-MIII
-
-
-
-
CP-WIII
-
-
-
-
CPY
-
-
-
-
deamidase
-
-
-
-
lysosomal carboxypeptidase A
-
-
-
-
lysosomal protective protein
-
-
-
-
MO54
-
-
-
-
Phaseolin
-
-
-
-
PpcA
-
-
protective protein cathepsin A
-
-
retinoid-inducible serine carboxypeptidase
-
-
Scpep1
serine carboxypeptidase
-
-
serine carboxypeptidase 1
-
serine carboxypeptidase I
-
-
-
-
serine carboxypeptidase Scpep1
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
9046-67-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
Scpep1 has carboxypeptidase activity against endothelin ET-1
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
a cDNA of bone marrow-derived monocyte/macrophage osteoclast progenitors is used
Manually annotated by BRENDA team
-
nerve fiber
Manually annotated by BRENDA team
-
embryonic
Manually annotated by BRENDA team
-
of digestive tract
Manually annotated by BRENDA team
-
nerve fiber
Manually annotated by BRENDA team
-
embryonic
Manually annotated by BRENDA team
-
of testis
Manually annotated by BRENDA team
-
macrophage-like cells
Manually annotated by BRENDA team
-
of lung
Manually annotated by BRENDA team
-
macrophage-like cells
Manually annotated by BRENDA team
-
Leydig cells
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
small amount also present in cytosolic fraction of transfected HEK-293 cells
Manually annotated by BRENDA team
in transfected HEK-293 cells
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
mice with a double CathA/Scpep1 deficiency (DD mice) demonstrate hypertension, increased ET-1-induced vasoconstriction and prolonged half-life of circulating ET-1 as compared to both wild-type animals and those with single CathA or Scpep1 deficiencies
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PPGB_MOUSE
474
0
53844
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55000
SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
-
Scpep1 is proteolytically cleaved to a mature enzyme
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
a yeast two-hybrid screening using a cDNA library of osteoclast precursors discloses PPCA as a binding partner of NF-kappaB p50/p65. Forced expression of PPCA with p50/p65 in HEK293 cells decreases both the level of p50/p65 proteins and the transcriptional activity. Overexpression of PPCA causes the disappearance of p50/p65 in both the lysosomal and cytosolic fractions. PPCA is expressed throughout osteoclastogenesis,and the expression is slightly up-regulated by nuclear factor (NF)-kappaB ligand signaling. Knockdown of PPCA in osteoclast precursors with PPCA siRNA stimulates binding of nuclear proteins to oligonucleotides containing an NF-kappaB binding motif and increases osteoclastogenesis
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in HEK293 cells
expressed in HT-1080 cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lee, T.H.; Streb, J.W.; Georger, M.A.; Miano, J.M.
Tissue expression of the novel serine carboxypeptidase Scpep1
J. Histochem. Cytochem.
54
701-711
2006
Mus musculus
Manually annotated by BRENDA team
Hermo, L.; Korah, N.; Gregory, M.; Liu, L.Y.; Cyr, D.G.; DAzzo, A.; Smith, C.E.
Structural alterations of epididymal epithelial cells in cathepsin A-deficient mice affect the blood-epididymal barrier and lead to altered sperm motility
J. Androl.
28
784-797
2007
Mus musculus
Manually annotated by BRENDA team
Masuhara, M.; Sato, T.; Hada, N.; Hakeda, Y.
Protective protein/cathepsin A down-regulates osteoclastogenesis by associating with and degrading NF-kappaB p50/p65
J. Bone Miner. Metab.
27
46-56
2009
Mus musculus (P16675)
Manually annotated by BRENDA team
Kollmann, K.; Damme, M.; Deuschl, F.; Kahle, J.; DHooge, R.; Luellmann-Rauch, R.; Luebke, T.
Molecular characterization and gene disruption of mouse lysosomal putative serine carboxypeptidase 1
FEBS J.
276
1356-1369
2009
Mus musculus (Q920A5), Mus musculus
Manually annotated by BRENDA team
Pan, X.; Grigoryeva, L.; Seyrantepe, V.; Peng, J.; Kollmann, K.; Tremblay, J.; Lavoie, J.; Hinek, A.; Lbke, T.; Pshezhetsky, A.
Serine carboxypeptidase SCPEP1 and cathepsin A play complementary roles in regulation of vasoconstriction via inactivation of Endothelin-1
PLoS Genet.
10
e1004146
2014
Mus musculus
Manually annotated by BRENDA team