PROS_RAT
ID PROS_RAT Reviewed; 675 AA.
AC P53813;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 137.
DE RecName: Full=Vitamin K-dependent protein S;
DE Flags: Precursor;
GN Name=Pros1; Synonyms=Pros;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=7608128; DOI=10.1093/jb/117.2.374;
RA Yasuda F., Hayashi T., Tanitame K., Nishioka J., Suzuki K.;
RT "Molecular cloning and functional characterization of rat plasma protein
RT S.";
RL J. Biochem. 117:374-383(1995).
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; S78744; AAC60704.1; -; mRNA.
DR PIR; JC4180; KXRTS.
DR AlphaFoldDB; P53813; -.
DR SMR; P53813; -.
DR STRING; 10116.ENSRNOP00000064737; -.
DR GlyGen; P53813; 2 sites.
DR PaxDb; P53813; -.
DR RGD; 620971; Pros1.
DR eggNOG; ENOG502QSNF; Eukaryota.
DR InParanoid; P53813; -.
DR PhylomeDB; P53813; -.
DR Reactome; R-RNO-114608; Platelet degranulation.
DR Reactome; R-RNO-140837; Intrinsic Pathway of Fibrin Clot Formation.
DR Reactome; R-RNO-140875; Common Pathway of Fibrin Clot Formation.
DR Reactome; R-RNO-159740; Gamma-carboxylation of protein precursors.
DR Reactome; R-RNO-159763; Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
DR Reactome; R-RNO-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins.
DR Reactome; R-RNO-202733; Cell surface interactions at the vascular wall.
DR PRO; PR:P53813; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR GO; GO:0042730; P:fibrinolysis; IEA:UniProtKB-KW.
DR GO; GO:0001889; P:liver development; IEP:RGD.
DR GO; GO:0050819; P:negative regulation of coagulation; IDA:RGD.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IDA:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
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; 3.
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; 1.
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_0000022127"
FT CHAIN 42..675
FT /note="Vitamin K-dependent protein S"
FT /id="PRO_0000022128"
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"
SQ SEQUENCE 675 AA; 74627 MW; B4338F756B486075 CRC64;
MRVLSVRFRV LLACLALVLP NSETNFLSKE RASQVLVRKR RANTLLEETK KGNLERECIE
ELCNKEEARE VFENNPETDY FYPKYLGCLG AFRVGAFSAA RQSANAYPDL RSCVNAIPDQ
CDPMPCNEDG YLSCKDGQGA FTCICKPGWQ GDKCQFDINE CKDPSNINGG CSQTCDNTPG
SYHCSCKIGF AMLTNKKDCK DVDECSLKPS VCGTAVCKNI PGDFECECPN GYRYDPSSKS
CKDVDECSEN TCAQLCVNYP GGYSCYCDGK KGFKLAQDQR SCEGIPVCLS LDLDKNYELL
YLAEQFAGVV LYLKFRLPDI TRFSAEFDFR TYDSEGIILY AESLDHSNWL LIALREGKIE
VQFKNEFSTQ ITTGGNVINN GIWNMVSVEE LDDSVSIKIA KEAVMNINKL GSLFKPTDGF
LDTKIYFAGL PRKVESALIK PINPRLDGCI RGWNLMKQGA LGAKEIVEGK QNKHCFLTVE
KGSYYPGSGI AQFSIDYNNV TNAEGWQINV TLNIRPSTGT GVMLALVSGD TVPFALSLVD
SGSGTSQDIL VFVENSVAAH LEAITLCSEQ PSQLKCNINR NGLELWTPVR KDVIYSKDLQ
RQLAILDKTM KGTVATYLGG VPDISFSATP VNAFYSGCME VNINGVQLDL DEAISKHNDI
RAHSCPSVRK IQKNF
