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Information on EC 3.4.21.112 - site-1 protease and Organism(s) Cricetulus griseus and UniProt Accession Q9Z2A8

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.112 site-1 protease
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Cricetulus griseus
UNIPROT: Q9Z2A8 not found.
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Word Map
The taxonomic range for the selected organisms is: Cricetulus griseus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
processes precursors containing basic and hydrophobic/aliphatic residues at P4 and P2, respectively, with a relatively relaxed acceptance of amino acids at P1 and P3
Synonyms
ski-1, ski-1/s1p, site-1 protease, site 1 protease, pcsk8, convertase site 1 protease, hski-1, srebp site 1 protease, subtilisin kexin isozyme 1/site 1 protease, subtilisin-kexin isoenzyme-1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
convertase site 1 protease
-
SKI-1/S1P
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
cleavage of C-N-linkage
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
167140-48-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
glycoprotein precursor Gc + H2O
?
show the reaction diagram
-
-
-
?
(pro)renin receptor + H2O
soluble (pro)renin receptor + ?
show the reaction diagram
-
-
-
-
?
ATF6 + H2O
?
show the reaction diagram
-
i.e. activating transcription factor 6
-
-
?
sterol regulatory element-binding protein + H2O
?
show the reaction diagram
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
?
-
-
initiates a process by which the active fragments of the SREBPs translocate to the nucleus and activate genes controlling the synthesis and uptake of cholersterol and unsaturated fatty acids in animal cells
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
PF429242
-
inhibotor suppresses the formation of soluble (pro)renin receptor
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
cis-and medial-Golgi, but not in the trans-Golgi
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
in CHO cells deficient of S1P (termed SRD-12B cells) glycoprotein GP-C processing is abrogated after Lassa virus infection
physiological function
-
siRNA-mediated reduction of endogenous S1P in cChinese hamster ovary cells attenuates soluble (pro)renin receptor generation. Overexpression of S1P by transient transfection in this cell line increases s(P)RR generation. The S1P inhibitor PF429242 suppresses the generation of soluble (pro)renin receptor
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MBTP1_CRIGR
1052
1
117552
Swiss-Prot
Secretory Pathway (Reliability: 1)
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
six potential N-glycosylation sites
proteolytic modification
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S414A
-
inactive mutant, no autocatalytic processing to generate S1P-C
additional information
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
into pcMV-S1P-Myc
-
truncated from lacking the COOH-terminal membrane anchor, expressed in CHO cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
glycoprotein cleavage by S1P is a promising target for the development of novel anti-arenaviral strategies
additional information
-
S1P is required for the endoplasmic reticulum stress response as well as for lipid synthesis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
DeBose-Boyd, R.A.; Brown, M.S.; Li, W.P.; Nohturfft, A.; Goldstein, J.L.; Espenshade, P.J.
Transport-dependent proteolysis of SREBP: relocation of site-1 protease from Golgi to ER obviates the need for SREBP transport to Golgi
Cell
99
703-712
1999
Cricetulus griseus
Manually annotated by BRENDA team
Espenshade, P.J.; Cheng, D.; Goldstein, J.L.; Brown, M.S.
Autocatalytic processing of site-1 protease removes propeptide and permits cleavage of sterol regulatory element-binding proteins
J. Biol. Chem.
274
22795-22804
1999
Cricetulus griseus
Manually annotated by BRENDA team
Seidah, N.G.; Chretien, M.
Proprotein convertase SKI-1/SIP
Handbook of Proteolytic Enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , Eds. ) Academic Press
2
1845-1847
2004
Arabidopsis thaliana, Cricetulus griseus, Homo sapiens, Mus musculus, Oryza sativa, Rattus norvegicus
-
Manually annotated by BRENDA team
Ye, J.; Rawson, R.B.; Komuro, R.; Chen, X.; Dave, U.P.; Prywes, R.; Brown, M.S.; Goldstein, J.L.
ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs
Mol. Cell
6
1355-1364
2000
Cricetulus griseus
Manually annotated by BRENDA team
Maisa, A.; Stroeher, U.; Klenk, H.D.; Garten, W.; Strecker, T.
Inhibition of Lassa virus glycoprotein cleavage and multicycle replication by site 1 protease-adapted alpha(1)-antitrypsin variants
PLoS Negl. Trop. Dis.
3
e446
2009
Cricetulus griseus (Q9Z2A8)
Manually annotated by BRENDA team
Nakagawa, T.; Suzuki-Nakagawa, C.; Watanabe, A.; Asami, E.; Matsumoto, M.; Nakano, M.; Ebihara, A.; Uddin, M.N.; Suzuki, F.
Site-1 protease is required for the generation of soluble (pro)renin receptor
J. Biochem.
161
369-379
2017
Cricetulus griseus
Manually annotated by BRENDA team