PROS_MOUSE
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 03-AUG-2022, entry version 188.
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}.
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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 GlyGen; Q08761; 2 sites.
DR iPTMnet; Q08761; -.
DR PhosphoSitePlus; Q08761; -.
DR CPTAC; non-CPTAC-3543; -.
DR CPTAC; non-CPTAC-3934; -.
DR PaxDb; Q08761; -.
DR PeptideAtlas; Q08761; -.
DR PRIDE; Q08761; -.
DR ProteomicsDB; 291603; -.
DR Antibodypedia; 858; 460 antibodies from 39 providers.
DR DNASU; 19128; -.
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 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; 317733at2759; -.
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 73 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 256 other tissues.
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 CDD; cd00110; LamG; 1.
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; 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 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
