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Database: UniProt
Entry: P07224
LinkDB: P07224
Original site: P07224 
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   13-FEB-2019, entry version 162.
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;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; 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.,
RA   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
RP   AND ASN-258, GLYCOSYLATION AT ASN-499, DISULFIDE BONDS, AND
RP   GAMMA-CARBOXYGLUTAMATION AT GLU-47; GLU-48; GLU-55; GLU-57; GLU-60;
RP   GLU-61; GLU-66; GLU-67; GLU-70; GLU-73 AND GLU-77.
RX   PubMed=2937785;
RA   Dahlback B., Lundwall A., Stenflo J.;
RT   "Localization of thrombin cleavage sites in the amino-terminal region
RT   of bovine protein S.";
RL   J. Biol. Chem. 261:5111-5115(1986).
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:0000269|PubMed:2937785}.
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   UniGene; Bt.48894; -.
DR   ProteinModelPortal; P07224; -.
DR   SMR; P07224; -.
DR   STRING; 9913.ENSBTAP00000032310; -.
DR   iPTMnet; P07224; -.
DR   PaxDb; P07224; -.
DR   PRIDE; P07224; -.
DR   Ensembl; ENSBTAT00000032377; ENSBTAP00000032310; ENSBTAG00000023652.
DR   GeneID; 282006; -.
DR   KEGG; bta:282006; -.
DR   CTD; 5627; -.
DR   VGNC; VGNC:49565; PROS1.
DR   eggNOG; ENOG410IGF6; Eukaryota.
DR   eggNOG; ENOG410ZTGU; LUCA.
DR   GeneTree; ENSGT00940000154035; -.
DR   HOGENOM; HOG000065758; -.
DR   HOVERGEN; HBG051702; -.
DR   InParanoid; P07224; -.
DR   KO; K03908; -.
DR   OMA; YPKYLGC; -.
DR   OrthoDB; 317733at2759; -.
DR   TreeFam; TF352157; -.
DR   Reactome; R-BTA-114608; Platelet degranulation.
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   Reactome; R-BTA-977606; Regulation of Complement cascade.
DR   PMAP-CutDB; P07224; -.
DR   Proteomes; UP000009136; Chromosome 1.
DR   Bgee; ENSBTAG00000023652; Expressed in 10 organ(s), highest expression level in liver.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   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   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; 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; 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   Complete proteome; Direct protein sequencing; Disulfide bond;
KW   EGF-like domain; Fibrinolysis; Gamma-carboxyglutamic acid;
KW   Glycoprotein; Hemostasis; Hydroxylation; Reference proteome; Repeat;
KW   Secreted; Signal; Zymogen.
FT   SIGNAL        1     24
FT   PROPEP       25     41       {ECO:0000269|PubMed:2937785}.
FT                                /FTId=PRO_0000022117.
FT   CHAIN        42    675       Vitamin K-dependent protein S.
FT                                {ECO:0000269|PubMed:2940598}.
FT                                /FTId=PRO_0000022118.
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   SITE         93     94       Cleavage; by thrombin.
FT   SITE        111    112       Cleavage; by thrombin.
FT   MOD_RES      47     47       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:2937785}.
FT   MOD_RES      48     48       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:2937785}.
FT   MOD_RES      55     55       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:2937785}.
FT   MOD_RES      57     57       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:2937785}.
FT   MOD_RES      60     60       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:2937785}.
FT   MOD_RES      61     61       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:2937785}.
FT   MOD_RES      66     66       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:2937785}.
FT   MOD_RES      67     67       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:2937785}.
FT   MOD_RES      70     70       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:2937785}.
FT   MOD_RES      73     73       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:2937785}.
FT   MOD_RES      77     77       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:2937785}.
FT   MOD_RES     136    136       (3R)-3-hydroxyaspartate.
FT                                {ECO:0000269|PubMed:2937785}.
FT   MOD_RES     177    177       (3R)-3-hydroxyasparagine.
FT                                {ECO:0000269|PubMed:2937785}.
FT   MOD_RES     219    219       (3R)-3-hydroxyasparagine.
FT                                {ECO:0000269|PubMed:2937785}.
FT   MOD_RES     258    258       (3R)-3-hydroxyasparagine.
FT                                {ECO:0000269|PubMed:2937785}.
FT   CARBOHYD    499    499       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:2937785}.
FT   CARBOHYD    509    509       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     58     63       {ECO:0000250}.
FT   DISULFID     88    113       {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    288    567       {ECO:0000269|PubMed:2937785}.
FT   DISULFID    449    475       {ECO:0000269|PubMed:2937785}.
FT   DISULFID    638    665       {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
//
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