ID PROS_BOVIN Reviewed; 675 AA.
AC P07224;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 24-JAN-2024, entry version 184.
DE RecName: Full=Vitamin K-dependent protein S;
DE Flags: Precursor;
GN Name=PROS1; Synonyms=PROS;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2940598; DOI=10.1073/pnas.83.12.4199;
RA Dahlback B., Lundwall A., Stenflo J.;
RT "Primary structure of bovine vitamin K-dependent protein S.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:4199-4203(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wydro R., Cohen E., Dackowski W., Stenflo J., Lundwall A., Dahlback B.;
RL Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 42-141, HYDROXYLATION AT ASP-136; ASN-177; ASN-219 AND
RP ASN-258, GLYCOSYLATION AT ASN-499, DISULFIDE BONDS, AND
RP GAMMA-CARBOXYGLUTAMATION AT GLU-47; GLU-48; GLU-55; GLU-57; GLU-60; GLU-61;
RP GLU-66; GLU-67; GLU-70; GLU-73 AND GLU-77.
RX PubMed=2937785; DOI=10.1016/s0021-9258(19)89221-9;
RA Dahlback B., Lundwall A., Stenflo J.;
RT "Localization of thrombin cleavage sites in the amino-terminal region of
RT bovine protein S.";
RL J. Biol. Chem. 261:5111-5115(1986).
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.
CC {ECO:0000269|PubMed:2937785}.
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DR EMBL; M13044; AAA30757.1; -; mRNA.
DR EMBL; X12891; CAA31382.1; -; mRNA.
DR PIR; A24759; KXBOS.
DR RefSeq; NP_776863.1; NM_174438.1.
DR AlphaFoldDB; P07224; -.
DR SMR; P07224; -.
DR STRING; 9913.ENSBTAP00000069933; -.
DR GlyCosmos; P07224; 2 sites, No reported glycans.
DR iPTMnet; P07224; -.
DR PaxDb; 9913-ENSBTAP00000032310; -.
DR Ensembl; ENSBTAT00000032377.4; ENSBTAP00000032310.3; ENSBTAG00000023652.4.
DR GeneID; 282006; -.
DR KEGG; bta:282006; -.
DR CTD; 5627; -.
DR VEuPathDB; HostDB:ENSBTAG00000023652; -.
DR VGNC; VGNC:49565; PROS1.
DR eggNOG; ENOG502QSNF; Eukaryota.
DR GeneTree; ENSGT00940000154035; -.
DR HOGENOM; CLU_026236_0_0_1; -.
DR InParanoid; P07224; -.
DR OrthoDB; 19806at2759; -.
DR TreeFam; TF352157; -.
DR Reactome; R-BTA-114608; Platelet degranulation.
DR Reactome; R-BTA-140837; Intrinsic Pathway of Fibrin Clot Formation.
DR Reactome; R-BTA-140875; Common Pathway of Fibrin Clot Formation.
DR Reactome; R-BTA-159740; Gamma-carboxylation of protein precursors.
DR Reactome; R-BTA-159763; Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
DR Reactome; R-BTA-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins.
DR Reactome; R-BTA-202733; Cell surface interactions at the vascular wall.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000023652; Expressed in liver and 103 other cell types or tissues.
DR ExpressionAtlas; P07224; baseline and differential.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR GO; GO:0042730; P:fibrinolysis; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 2.
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; PF00008; EGF; 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 Pfam; PF02210; Laminin_G_2; 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; 3.
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 1: Evidence at protein level;
KW Blood coagulation; Calcium; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; EGF-like domain; Fibrinolysis;
KW Gamma-carboxyglutamic acid; Glycoprotein; Hemostasis; Hydroxylation;
KW Reference proteome; Repeat; Secreted; Signal; Zymogen.
FT SIGNAL 1..24
FT PROPEP 25..41
FT /evidence="ECO:0000269|PubMed:2937785"
FT /id="PRO_0000022117"
FT CHAIN 42..675
FT /note="Vitamin K-dependent protein S"
FT /evidence="ECO:0000269|PubMed:2940598"
FT /id="PRO_0000022118"
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 SITE 93..94
FT /note="Cleavage; by thrombin"
FT SITE 111..112
FT /note="Cleavage; by thrombin"
FT MOD_RES 47
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:2937785"
FT MOD_RES 48
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:2937785"
FT MOD_RES 55
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:2937785"
FT MOD_RES 57
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:2937785"
FT MOD_RES 60
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:2937785"
FT MOD_RES 61
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:2937785"
FT MOD_RES 66
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:2937785"
FT MOD_RES 67
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:2937785"
FT MOD_RES 70
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:2937785"
FT MOD_RES 73
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:2937785"
FT MOD_RES 77
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:2937785"
FT MOD_RES 136
FT /note="(3R)-3-hydroxyaspartate"
FT /evidence="ECO:0000269|PubMed:2937785"
FT MOD_RES 177
FT /note="(3R)-3-hydroxyasparagine"
FT /evidence="ECO:0000269|PubMed:2937785"
FT MOD_RES 219
FT /note="(3R)-3-hydroxyasparagine"
FT /evidence="ECO:0000269|PubMed:2937785"
FT MOD_RES 258
FT /note="(3R)-3-hydroxyasparagine"
FT /evidence="ECO:0000269|PubMed:2937785"
FT CARBOHYD 499
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:2937785"
FT CARBOHYD 509
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 58..63
FT /evidence="ECO:0000250"
FT DISULFID 88..113
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 288..567
FT /evidence="ECO:0000269|PubMed:2937785"
FT DISULFID 449..475
FT /evidence="ECO:0000269|PubMed:2937785"
FT DISULFID 638..665
FT /evidence="ECO:0000269|PubMed:2937785"
SQ SEQUENCE 675 AA; 75133 MW; CF7EC5BC1C318DEE CRC64;
MRVLGGRTGT LLACLALVLP VLEANFLSRQ HASQVLIRRR RANTLLEETK KGNLERECIE
ELCNKEEARE IFENNPETEY FYPKYLGCLG SFRAGLFTAA RLSTNAYPDL RSCVNAISDQ
CNPLPCNEDG FMTCKDGQAT FTCICKSGWQ GEKCESDINE CKDPVNINGG CSQICENTPG
SYHCSCKNGF VMLSNKKDCK DVDECVLKPS ICGTAVCKNI PGDFECECAE GYKYNPVSKS
CDDVDECAEN LCAQLCVNYP GGYSCYCDGK KGFKLAQDQK SCEAVPVCLP LDLDKNYELL
YLAEQFVGVV LYLKFRLPET TRFSAEFDFR TYDSEGVILY AESSDHSAWF LIALREGKIE
IQFKNEKTTK MTTGGKVIND GLWHMVSVEE LEQSISVKIA KEAVMNINKP GSLFKPTNGF
LETKVYFAGV PRKMENALIR PINPRLDGCI RGWNLMNQGT SGVKEIIQEK QNKHCLVNVE
KGSYYPGTGV AQFSINYKNE SNPEAWQINV SLNIRPSAGT GVMLALVSDN TVPFALSLVD
SATEKLQDIL VSVESMVIGR IEAISLCSDQ QTFLEIRVNR NNLELSTQLR KDSFHSEDFQ
RQFAILDEAM KGTVVTYLGG LPDVPFSATP VNAFYQGCME VNINGVQVDL DEAISKHNDI
RAHSCPSVWQ KTKHT
//
