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Membrane-bound transcription factor site-1 protease (EC 3.4.21.112) (Endopeptidase S1P) (Sterol-regulated luminal protease) (Subtilisin/kexin-isozyme 1) (SKI-1)

 MBTP1_CRIGR             Reviewed;        1052 AA.
Q9Z2A8; G3GRY2;
16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 2.
20-JUN-2018, entry version 95.
RecName: Full=Membrane-bound transcription factor site-1 protease;
EC=3.4.21.112;
AltName: Full=Endopeptidase S1P;
AltName: Full=Sterol-regulated luminal protease;
AltName: Full=Subtilisin/kexin-isozyme 1;
Short=SKI-1;
Flags: Precursor;
Name=MBTPS1; Synonyms=S1P, SKI1;
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Cricetidae; Cricetinae; Cricetulus.
NCBI_TaxID=10029;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS OF ASP-218; HIS-249 AND
SER-414.
TISSUE=Ovary;
PubMed=9809072; DOI=10.1016/S1097-2765(00)80150-1;
Sakai J., Rawson R.B., Espenshade P.J., Cheng D., Seegmiller A.C.,
Goldstein J.L., Brown M.S.;
"Molecular identification of the sterol-regulated luminal protease
that cleaves SREBPs and controls lipid composition of animal cells.";
Mol. Cell 2:505-514(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=21804562; DOI=10.1038/nbt.1932;
Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W.,
Xie M., Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B.,
Koh W., Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J.,
Quake S.R., Famili I., Palsson B.O., Wang J.;
"The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell
line.";
Nat. Biotechnol. 29:735-741(2011).
[3]
FUNCTION.
PubMed=11163209; DOI=10.1016/S1097-2765(00)00133-7;
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).
-!- FUNCTION: Serine protease that catalyzes the first step in the
proteolytic activation of the sterol regulatory element-binding
proteins (SREBPs). Other known substrates are BDNF, GNPTAB and
ATF6. Cleaves after hydrophobic or small residues, provided that
Arg or Lys is in position P4. Cleaves known substrates after Arg-
Ser-Val-Leu (SERBP-2), Arg-His-Leu-Leu (ATF6), Arg-Gly-Leu-Thr
(BDNF) and its own propeptide after Arg-Arg-Leu-Leu. Mediates the
protein cleavage of GNPTAB into subunit alpha and beta, thereby
participating in biogenesis of lysosomes.
{ECO:0000269|PubMed:11163209}.
-!- CATALYTIC ACTIVITY: 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.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
-!- ENZYME REGULATION: Inhibited by divalent copper and zinc ions, but
not by nickel or cobalt. Inhibited by its prosegment, but not
smaller fragments thereof (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Golgi apparatus membrane {ECO:0000250}; Single-pass type I
membrane protein {ECO:0000250}. Note=May sort to other organelles,
including lysosomal and/or endosomal compartments. {ECO:0000250}.
-!- INDUCTION: Down-regulated by sterols.
-!- PTM: The 148 kDa zymogen is processed progressively into two
membrane-bound 120 and 106 kDa forms in the endoplasmic reticulum,
and late into a secreted 98 kDa form. The propeptide is
autocatalytically removed through an intramolecular cleavage after
Leu-186. Further cleavage generates 14, 10, and 8 kDa
intermediates (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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EMBL; AF078105; AAC78321.1; -; mRNA.
EMBL; JH000004; EGV94126.1; -; Genomic_DNA.
PIR; T17093; T17093.
RefSeq; NP_001233611.1; NM_001246682.1.
ProteinModelPortal; Q9Z2A8; -.
SMR; Q9Z2A8; -.
MEROPS; S08.063; -.
PRIDE; Q9Z2A8; -.
GeneID; 100689417; -.
KEGG; cge:100689417; -.
CTD; 8720; -.
HOVERGEN; HBG052421; -.
KO; K08653; -.
BRENDA; 3.4.21.112; 1309.
Proteomes; UP000001075; Unassembled WGS sequence.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0005795; C:Golgi stack; IEA:Ensembl.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0004252; F:serine-type endopeptidase activity; ISS:UniProtKB.
GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
GO; GO:0007040; P:lysosome organization; ISS:UniProtKB.
GO; GO:0031293; P:membrane protein intracellular domain proteolysis; IMP:ParkinsonsUK-UCL.
GO; GO:0006606; P:protein import into nucleus; IEA:Ensembl.
GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:ParkinsonsUK-UCL.
CDD; cd07479; Peptidases_S8_SKI-1_like; 1.
Gene3D; 3.40.50.200; -; 1.
InterPro; IPR000209; Peptidase_S8/S53_dom.
InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
InterPro; IPR022398; Peptidase_S8_His-AS.
InterPro; IPR023828; Peptidase_S8_Ser-AS.
InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
InterPro; IPR034185; Site-1_peptidase_cat_dom.
Pfam; PF00082; Peptidase_S8; 1.
PRINTS; PR00723; SUBTILISIN.
SUPFAM; SSF52743; SSF52743; 2.
PROSITE; PS00137; SUBTILASE_HIS; 1.
PROSITE; PS00138; SUBTILASE_SER; 1.
1: Evidence at protein level;
Autocatalytic cleavage; Calcium; Cholesterol metabolism;
Complete proteome; Endoplasmic reticulum; Glycoprotein;
Golgi apparatus; Hydrolase; Lipid metabolism; Membrane;
Phosphoprotein; Protease; Reference proteome; Serine protease; Signal;
Steroid metabolism; Sterol metabolism; Transmembrane;
Transmembrane helix; Zymogen.
SIGNAL 1 17 {ECO:0000255}.
PROPEP 18 186 {ECO:0000255}.
/FTId=PRO_0000027049.
CHAIN 187 1052 Membrane-bound transcription factor site-
1 protease.
/FTId=PRO_0000027050.
TOPO_DOM 187 999 Lumenal. {ECO:0000255}.
TRANSMEM 1000 1022 Helical. {ECO:0000255}.
TOPO_DOM 1023 1052 Cytoplasmic. {ECO:0000255}.
DOMAIN 214 472 Peptidase S8.
COMPBIAS 1023 1050 Arg/Lys/Pro-rich (basic).
ACT_SITE 218 218 Charge relay system. {ECO:0000250}.
ACT_SITE 249 249 Charge relay system. {ECO:0000250}.
ACT_SITE 414 414 Charge relay system. {ECO:0000250}.
SITE 186 187 Cleavage; by autolysis. {ECO:0000250}.
MOD_RES 168 168 Phosphoserine.
{ECO:0000250|UniProtKB:Q14703}.
CARBOHYD 148 148 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 236 236 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 305 305 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 515 515 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 728 728 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 939 939 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
MUTAGEN 218 218 D->N: Loss of activity.
{ECO:0000269|PubMed:9809072}.
MUTAGEN 249 249 H->F: Loss of activity.
{ECO:0000269|PubMed:9809072}.
MUTAGEN 414 414 S->A: Loss of activity.
{ECO:0000269|PubMed:9809072}.
CONFLICT 875 875 T -> N (in Ref. 1; AAC78321).
{ECO:0000305}.
SEQUENCE 1052 AA; 117552 MW; 7DD079393815BAED CRC64;
MKLINIWLLL LVVLLCGKKH LGDRLGKKAF EKASCPSCSH LTLKVEFSST VVEYEYIVAF
NGYFTAKARN SFISSALKSS EVDNWRIIPR NNPSSDYPSD FEVIQIKEKQ KAGLLTLEDH
PNIKRVTPQR KVFRSLKFAE SDPIVPCNET RWSQKWQSSR PLRRASLSLG SGFWHATGRH
SSRRLLRAIP RQVAQTLQAD VLWQMGYTGA NVRVAVFDTG LSEKHPHFKN VKERTNWTNE
RTLDDGLGHG TFVAGVIASM RECQGFAPDA ELHIFRVFTN NQVSYTSWFL DAFNYAILKK
IDVLNLSIGG PDFMDHPFVD KVWELTANNV IMVSAIGNDG PLYGTLNNPA DQMDVIGVGG
IDFEDNIARF SSRGMTTWEL PGGYGRVKPD IVTYGAGVRG SGVKGGCRAL SGTSVASPVV
AGAVTLLVST VQKRELVNPA SVKQALIASA RRLPGVNMFE QGHGKLDLLR AYQILSSYKP
QASLSPSYID LTECPYMWPY CSQPIYYGGM PTIVNVTILN GMGVTGRIVD KPEWRPYLPQ
NGDNIEVAFS YSSVLWPWSG YLAISISVTK KAASWEGIAQ GHIMITVASP AETEAKNGAE
HTSTVKLPIK VKIIPTPPRS KRVLWDQYHN LRYPPGYFPR DNLRMKNDPL DWNGDHVHTN
FRDMYQHLRS MGYFVEVLGA PFTCFDATQY GTLLMVDSEE EYFPEEIAKL RRDVDNGLSL
VIFSDWYNTS VMRKVKFYDE NTRQWWMPDT GGANIPALNE LLSVWNMGFS DGLYEGEFAL
ANHDMYYASG CSIAKFPEDG VVITQTFKDQ GLEVLKQETA VVENVPILGL YQIPAEGGGR
IVLYGDSNCL DDSHRQKDCF WLLDALLQYT SYGVTPPSLS HSGNRQRPPS GAGLAPPERM
EGNHLHRYSK VLEAHLGDPK PRPLPACPHL SWAKPQPLNE TAPSNLWKHQ KLLSIDLDKV
VLPNFRSNRP QVRPLSPGES GAWDIPGGIM PGRYNQEVGQ TIPVFAFLGA MVALAFFVVQ
ISKAKSRPKR RRPRAKRPQL TQQTHPPRTP SV


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