ID A0A2K6GGP1_PROCO Unreviewed; 675 AA.
AC A0A2K6GGP1;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Vitamin K-dependent protein S {ECO:0000256|ARBA:ARBA00017875};
GN Name=PROS1 {ECO:0000313|Ensembl:ENSPCOP00000025410.1};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000025410.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000025410.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 {ECO:0000256|ARBA:ARBA00002240}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR AlphaFoldDB; A0A2K6GGP1; -.
DR STRING; 379532.ENSPCOP00000025410; -.
DR Ensembl; ENSPCOT00000036102.1; ENSPCOP00000025410.1; ENSPCOG00000024926.1.
DR GeneTree; ENSGT00940000154035; -.
DR OMA; GQAAFTC; -.
DR Proteomes; UP000233160; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0005796; C:Golgi lumen; IEA:UniProt.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0042730; P:fibrinolysis; IEA:UniProtKB-KW.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
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; 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 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; PF12661; hEGF; 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; 1.
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; 3.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS00011; GLA_1; 1.
DR PROSITE; PS50998; GLA_2; 1.
DR PROSITE; PS50025; LAM_G_DOMAIN; 1.
PE 4: Predicted;
KW Blood coagulation {ECO:0000256|ARBA:ARBA00023281};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Fibrinolysis {ECO:0000256|ARBA:ARBA00023281};
KW Gamma-carboxyglutamic acid {ECO:0000256|ARBA:ARBA00022479};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hemostasis {ECO:0000256|ARBA:ARBA00023281};
KW Reference proteome {ECO:0000313|Proteomes:UP000233160};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..675
FT /note="Vitamin K-dependent protein S"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014376822"
FT DOMAIN 41..87
FT /note="Gla"
FT /evidence="ECO:0000259|PROSITE:PS50998"
FT DOMAIN 117..155
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 201..242
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 299..475
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DISULFID 126..143
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 145..154
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 675 AA; 74812 MW; 0057D2F61B6FCF3C CRC64;
MRVLGGRCGA LLACVALVLS VAEANFLSKQ HASQVLVRKR RANTLLEETK QGNLERECIE
ELCNKEEARE IFENDPETDY FYPKYLGCLG SFRAGLFTAA RQSTNAHPDL RSCVNAIPDQ
CNPPPCNEDG YISCRDGQAT FTCICKSGWQ GERCEFDINE CKDPSNVNGG CSQICDNTPG
SYHCSCKSGF VMLSNKKDCK DMDECSMKPS ICGTAVCKNI PGDFECECPE GYRYDPKSKS
CEDVDECSEN MCAQLCVNYP GGYSCYCDGK KGFKLAHDQK SCEAVPVCLP LNLNKNYELL
YLAEQFIGVV LYLKFRLPEI TRFSAEFDFR THDSEGVLLY AESLDHSAWF LIALRDGKIE
IQFKNEYTAK ITTGGKVINN GLWNMVSVEE LEHSISVKIA KEAVMNINKP GSLFNPTNGF
LETKVYFAGF PRKVENALIK PINPRLDGCI RGWNLMNQGA SGVKEIIQEK QNKHCLVSVE
KGSYYPGSGV AQFSIDYNNV SSAEGWQVNV TLNIRPSTGT GVMLALVSGN TVPFALSLVD
STSEKFQDIL VSVEDTVISQ IEAMSLCSGQ QSFLEFRVDR NNLKVRTPLQ EDTISSEHFQ
RQFAILDKAM KGTVATYLGG IPDVPFNATP VNAFYNGCME TKINSVQLDL DEAISKHNDI
RAHSCPSVQK DTKNS
//
