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Database: UniProt
Entry: Q08761
LinkDB: Q08761
Original site: Q08761 
ID   PROS_MOUSE              Reviewed;         675 AA.
AC   Q08761; P43483;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   13-FEB-2019, entry version 171.
DE   RecName: Full=Vitamin K-dependent protein S;
DE   Flags: Precursor;
GN   Name=Pros1; Synonyms=Pros;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8148380; DOI=10.1016/0167-4781(94)90294-1;
RA   Chu M.D., Sun J., Bird P.I.;
RT   "Cloning and sequencing of a cDNA encoding the murine vitamin K-
RT   dependent protein S.";
RL   Biochim. Biophys. Acta 1217:325-328(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 33-675.
RX   PubMed=8029814; DOI=10.1016/0049-3848(94)90006-X;
RA   Lu D., Schmidel D.K., Long G.L.;
RT   "Structure of mouse protein S as determined by PCR amplification and
RT   DNA sequencing of cDNA.";
RL   Thromb. Res. Suppl. 74:135-142(1994).
CC   -!- FUNCTION: Anticoagulant plasma protein; it is a cofactor to
CC       activated protein C in the degradation of coagulation factors Va
CC       and VIIIa. It helps to prevent coagulation and stimulating
CC       fibrinolysis.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Plasma.
CC   -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
CC       aspartate and asparagine is (R) stereospecific within EGF domains.
CC       {ECO:0000250}.
DR   EMBL; Z25469; CAA80961.1; -; mRNA.
DR   EMBL; L27439; AAA40006.1; -; mRNA.
DR   CCDS; CCDS28263.1; -.
DR   PIR; S43504; KXMSS.
DR   RefSeq; NP_035303.1; NM_011173.3.
DR   UniGene; Mm.127156; -.
DR   ProteinModelPortal; Q08761; -.
DR   SMR; Q08761; -.
DR   STRING; 10090.ENSMUSP00000023629; -.
DR   iPTMnet; Q08761; -.
DR   PhosphoSitePlus; Q08761; -.
DR   PaxDb; Q08761; -.
DR   PeptideAtlas; Q08761; -.
DR   PRIDE; Q08761; -.
DR   Ensembl; ENSMUST00000023629; ENSMUSP00000023629; ENSMUSG00000022912.
DR   GeneID; 19128; -.
DR   KEGG; mmu:19128; -.
DR   UCSC; uc007zpx.1; mouse.
DR   CTD; 5627; -.
DR   MGI; MGI:1095733; Pros1.
DR   eggNOG; ENOG410IGF6; Eukaryota.
DR   eggNOG; ENOG410ZTGU; LUCA.
DR   GeneTree; ENSGT00940000154035; -.
DR   HOGENOM; HOG000065758; -.
DR   HOVERGEN; HBG051702; -.
DR   InParanoid; Q08761; -.
DR   KO; K03908; -.
DR   OMA; YPKYLGC; -.
DR   OrthoDB; 317733at2759; -.
DR   PhylomeDB; Q08761; -.
DR   TreeFam; TF352157; -.
DR   Reactome; R-MMU-114608; Platelet degranulation.
DR   Reactome; R-MMU-140875; Common Pathway of Fibrin Clot Formation.
DR   Reactome; R-MMU-159740; Gamma-carboxylation of protein precursors.
DR   Reactome; R-MMU-159763; Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
DR   Reactome; R-MMU-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins.
DR   Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
DR   ChiTaRS; Pros1; mouse.
DR   PRO; PR:Q08761; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   Bgee; ENSMUSG00000022912; Expressed in 278 organ(s), highest expression level in blood.
DR   ExpressionAtlas; Q08761; baseline and differential.
DR   Genevisible; Q08761; MM.
DR   GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR   GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR   GO; GO:0042730; P:fibrinolysis; IEA:UniProtKB-KW.
DR   GO; GO:0050819; P:negative regulation of coagulation; ISO:MGI.
DR   GO; GO:0050766; P:positive regulation of phagocytosis; ISO:MGI.
DR   Gene3D; 4.10.740.10; -; 1.
DR   InterPro; IPR017857; Coagulation_fac-like_Gla_dom.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR035972; GLA-like_dom_SF.
DR   InterPro; IPR000294; GLA_domain.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR033189; PROS1.
DR   PANTHER; PTHR24040:SF0; PTHR24040:SF0; 1.
DR   Pfam; PF00008; EGF; 1.
DR   Pfam; PF07645; EGF_CA; 2.
DR   Pfam; PF00594; Gla; 1.
DR   Pfam; PF00054; Laminin_G_1; 1.
DR   PRINTS; PR00001; GLABLOOD.
DR   SMART; SM00181; EGF; 4.
DR   SMART; SM00179; EGF_CA; 4.
DR   SMART; SM00069; GLA; 1.
DR   SMART; SM00282; LamG; 2.
DR   SUPFAM; SSF49899; SSF49899; 2.
DR   SUPFAM; SSF57184; SSF57184; 1.
DR   SUPFAM; SSF57630; SSF57630; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 4.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 3.
DR   PROSITE; PS50026; EGF_3; 4.
DR   PROSITE; PS01187; EGF_CA; 3.
DR   PROSITE; PS00011; GLA_1; 1.
DR   PROSITE; PS50998; GLA_2; 1.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 2.
PE   2: Evidence at transcript level;
KW   Blood coagulation; Calcium; Cleavage on pair of basic residues;
KW   Complete proteome; Disulfide bond; EGF-like domain; Fibrinolysis;
KW   Gamma-carboxyglutamic acid; Glycoprotein; Hemostasis; Hydroxylation;
KW   Reference proteome; Repeat; Secreted; Signal; Zymogen.
FT   SIGNAL        1     24       {ECO:0000250}.
FT   PROPEP       25     41       {ECO:0000250}.
FT                                /FTId=PRO_0000022123.
FT   CHAIN        42    675       Vitamin K-dependent protein S.
FT                                /FTId=PRO_0000022124.
FT   DOMAIN       42     87       Gla. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   DOMAIN      117    155       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      157    200       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      201    242       EGF-like 3; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      243    283       EGF-like 4; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      299    475       Laminin G-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN      484    665       Laminin G-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   REGION       88    116       Thrombin-sensitive.
FT   MOD_RES      47     47       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P07224,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      48     48       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P07224,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      55     55       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P07224,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      57     57       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P07224,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      60     60       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P07224,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      61     61       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P07224,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      66     66       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P07224,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      67     67       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P07224,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      70     70       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P07224,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      73     73       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P07224,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      77     77       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P07224,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES     136    136       (3R)-3-hydroxyaspartate. {ECO:0000250}.
FT   CARBOHYD    499    499       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    509    509       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     58     63       {ECO:0000250}.
FT   DISULFID    121    134       {ECO:0000250}.
FT   DISULFID    126    143       {ECO:0000250}.
FT   DISULFID    145    154       {ECO:0000250}.
FT   DISULFID    161    175       {ECO:0000250}.
FT   DISULFID    171    184       {ECO:0000250}.
FT   DISULFID    186    199       {ECO:0000250}.
FT   DISULFID    205    217       {ECO:0000250}.
FT   DISULFID    212    226       {ECO:0000250}.
FT   DISULFID    228    241       {ECO:0000250}.
FT   DISULFID    247    256       {ECO:0000250}.
FT   DISULFID    252    265       {ECO:0000250}.
FT   DISULFID    267    282       {ECO:0000250}.
FT   DISULFID    449    475       {ECO:0000250}.
FT   DISULFID    638    665       {ECO:0000250}.
FT   CONFLICT    493    493       F -> L (in Ref. 2; AAA40006).
FT                                {ECO:0000305}.
SQ   SEQUENCE   675 AA;  74934 MW;  79D51203E85AF31F CRC64;
     MRVLSARFRV LLACLALVIP VSETNFLSKE RASQVLVRKR RANTLFEETM KGNLERECIE
     ELCNKEEARE VFENNPETDY FYPKYLGCLG AFRVGSFHAA RQSANAYPDL RSCVKAISDQ
     CDPIPCNEDG YLACQDGQAA FTCFCKPGWQ GDRCQYDVNE CKDPSNVNGG CSQICDNTPG
     SYHCSCKRGF AMLPNKKDCK DLDECALKPS VCGTAVCKNI PGDFECECPD GYRYDPSSKS
     CKDVDECSEN MCAQLCVNFP GGYSCYCDGK KGFKLAQDQK SCEGIPVCLS LDLDKNYELL
     YLAEQFAGVV LYLKFRLPDI TRFSAEFDFR TYDSEGIILY AESLDHSNWL LIALRDGKIE
     VQFKNEFSTQ ITTGGNVINN GIWNMVSVEE LDDSVSIKIA KEAVMNINKL GSLFKPTDGF
     LDTKIYFAGL PRKVESALIK PINPRLDGCI RGWNLMKQGA LGAKEIIEGK QNKHCFLNVE
     KGSYYPGSGI AQFSIDYNNV TNAEGWQMNV TLNIRPSTGT GVMLALVSGG TVPFALSLVD
     SRSGTSQDIV VFVENSVVAR LEAVSLCSDQ QSQLKCNVNR NGLELWTPLR KDVIYSKDLQ
     RQLAVLDKAM KRTVATYLGG IPDISFSATP VNAFYSGCME VNINGVQLDL DEAISKHKDI
     RAHSCPSVRK IQKNF
//
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