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   24-JAN-2024, entry version 195.
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; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   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-dependent
RT   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 DNA
RT   sequencing of cDNA.";
RL   Thromb. Res. Suppl. 74:135-142(1994).
CC   -!- FUNCTION: Anticoagulant plasma protein; it is a cofactor to activated
CC       protein C in the degradation of coagulation factors Va and VIIIa. It
CC       helps to prevent coagulation and stimulating fibrinolysis.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Plasma.
CC   -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate
CC       and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   AlphaFoldDB; Q08761; -.
DR   SMR; Q08761; -.
DR   STRING; 10090.ENSMUSP00000023629; -.
DR   GlyCosmos; Q08761; 2 sites, No reported glycans.
DR   GlyGen; Q08761; 2 sites.
DR   iPTMnet; Q08761; -.
DR   PhosphoSitePlus; Q08761; -.
DR   CPTAC; non-CPTAC-3543; -.
DR   CPTAC; non-CPTAC-3934; -.
DR   PaxDb; 10090-ENSMUSP00000023629; -.
DR   PeptideAtlas; Q08761; -.
DR   ProteomicsDB; 291603; -.
DR   Pumba; Q08761; -.
DR   Antibodypedia; 858; 496 antibodies from 39 providers.
DR   DNASU; 19128; -.
DR   Ensembl; ENSMUST00000023629.9; ENSMUSP00000023629.9; ENSMUSG00000022912.9.
DR   GeneID; 19128; -.
DR   KEGG; mmu:19128; -.
DR   UCSC; uc007zpx.1; mouse.
DR   AGR; MGI:1095733; -.
DR   CTD; 5627; -.
DR   MGI; MGI:1095733; Pros1.
DR   VEuPathDB; HostDB:ENSMUSG00000022912; -.
DR   eggNOG; ENOG502QSNF; Eukaryota.
DR   GeneTree; ENSGT00940000154035; -.
DR   HOGENOM; CLU_026236_0_0_1; -.
DR   InParanoid; Q08761; -.
DR   OMA; GQAAFTC; -.
DR   OrthoDB; 19806at2759; -.
DR   PhylomeDB; Q08761; -.
DR   TreeFam; TF352157; -.
DR   Reactome; R-MMU-114608; Platelet degranulation.
DR   Reactome; R-MMU-140837; Intrinsic Pathway of Fibrin Clot Formation.
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   BioGRID-ORCS; 19128; 0 hits in 78 CRISPR screens.
DR   ChiTaRS; Pros1; mouse.
DR   PRO; PR:Q08761; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; Q08761; Protein.
DR   Bgee; ENSMUSG00000022912; Expressed in cumulus cell and 259 other cell types or tissues.
DR   ExpressionAtlas; Q08761; baseline and differential.
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   CDD; cd00054; EGF_CA; 3.
DR   CDD; cd00110; LamG; 1.
DR   Gene3D; 2.60.120.200; -; 2.
DR   Gene3D; 4.10.740.10; Coagulation Factor IX; 1.
DR   Gene3D; 2.10.25.10; Laminin; 4.
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; 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   PANTHER; PTHR24040; LAMININ G-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR24040:SF0; VITAMIN K-DEPENDENT PROTEIN S; 1.
DR   Pfam; PF07645; EGF_CA; 2.
DR   Pfam; PF14670; FXa_inhibition; 1.
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; Concanavalin A-like lectins/glucanases; 2.
DR   SUPFAM; SSF57630; GLA-domain; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 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.
DR   Genevisible; Q08761; MM.
PE   2: Evidence at transcript level;
KW   Blood coagulation; Calcium; Cleavage on pair of basic residues;
KW   Disulfide bond; EGF-like domain; Fibrinolysis; Gamma-carboxyglutamic acid;
KW   Glycoprotein; Hemostasis; Hydroxylation; Reference proteome; Repeat;
KW   Secreted; Signal; Zymogen.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000250"
FT   PROPEP          25..41
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000022123"
FT   CHAIN           42..675
FT                   /note="Vitamin K-dependent protein S"
FT                   /id="PRO_0000022124"
FT   DOMAIN          42..87
FT                   /note="Gla"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT   DOMAIN          117..155
FT                   /note="EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          157..200
FT                   /note="EGF-like 2; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          201..242
FT                   /note="EGF-like 3; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          243..283
FT                   /note="EGF-like 4; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          299..475
FT                   /note="Laminin G-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          484..665
FT                   /note="Laminin G-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   REGION          88..116
FT                   /note="Thrombin-sensitive"
FT   MOD_RES         47
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P07224,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         48
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P07224,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         55
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P07224,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         57
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P07224,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         60
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P07224,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         61
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P07224,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         66
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P07224,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         67
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P07224,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         70
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P07224,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         73
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P07224,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         77
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P07224,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         136
FT                   /note="(3R)-3-hydroxyaspartate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        499
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        509
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        58..63
FT                   /evidence="ECO:0000250"
FT   DISULFID        121..134
FT                   /evidence="ECO:0000250"
FT   DISULFID        126..143
FT                   /evidence="ECO:0000250"
FT   DISULFID        145..154
FT                   /evidence="ECO:0000250"
FT   DISULFID        161..175
FT                   /evidence="ECO:0000250"
FT   DISULFID        171..184
FT                   /evidence="ECO:0000250"
FT   DISULFID        186..199
FT                   /evidence="ECO:0000250"
FT   DISULFID        205..217
FT                   /evidence="ECO:0000250"
FT   DISULFID        212..226
FT                   /evidence="ECO:0000250"
FT   DISULFID        228..241
FT                   /evidence="ECO:0000250"
FT   DISULFID        247..256
FT                   /evidence="ECO:0000250"
FT   DISULFID        252..265
FT                   /evidence="ECO:0000250"
FT   DISULFID        267..282
FT                   /evidence="ECO:0000250"
FT   DISULFID        449..475
FT                   /evidence="ECO:0000250"
FT   DISULFID        638..665
FT                   /evidence="ECO:0000250"
FT   CONFLICT        493
FT                   /note="F -> L (in Ref. 2; AAA40006)"
FT                   /evidence="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
//