ID A0A383YMT8_BALAS Unreviewed; 675 AA.
AC A0A383YMT8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Vitamin K-dependent protein S {ECO:0000256|ARBA:ARBA00017875};
GN Name=PROS1 {ECO:0000313|RefSeq:XP_007164144.1};
OS Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS (Balaenoptera davidsoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC Balaenopteridae; Balaenoptera.
OX NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007164144.1};
RN [1] {ECO:0000313|RefSeq:XP_007164144.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007164144.1};
RG RefSeq;
RL Submitted (JAN-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 RefSeq; XP_007164144.1; XM_007164082.2.
DR AlphaFoldDB; A0A383YMT8; -.
DR STRING; 310752.A0A383YMT8; -.
DR GeneID; 103010877; -.
DR KEGG; bacu:103010877; -.
DR CTD; 5627; -.
DR InParanoid; A0A383YMT8; -.
DR OrthoDB; 19806at2759; -.
DR Proteomes; UP000261681; Unplaced.
DR GO; GO:0005615; C:extracellular space; 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; 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; 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; 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:UP000261681};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
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_5016946406"
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; 75037 MW; BC5A12A800B35EBD CRC64;
MRVLGGRSGA LLACLALVLP VLEANFLSKQ HASQVLVRKS RANSLIEETK KGNLERECIE
ELCNKEEARE VFENDPETEY FYPKYLGCLG SFRAGLFTTA RLSTNAYPDL RSCVNAISDQ
CNPLPCNEDG YMTCKDGQAT FTCICKSGWQ GEKCEFDINE CKDPSNVNGG CNQICDNTPG
SYHCSCKSGF VMLSNKKDCR DVDECSVKPS ICGTAVCKNI PGDFECECTE GYRYNPISKS
CEDVDECSEN ICAQLCVNHP GGYSCYCDGK KGFKLAQDQK SCEAVPVCLP LNLDKNYELL
YLAEQFVGVV LYLKFRLPEI TRFSAEFDFR TYDSEGVILY AESSDQSAWF LIALREGKIE
IQFKNEYTAK ITTGGKVIND GLWNMVSVEE LEQSISVKIA KEAVMNINKP ESLFKPTNGF
LETKVYFAAI PRKVENALIR PINPRLDGCI RGWNLMNQGA SGVKEIIQEK QNKHCLVTVE
KGSYYPGSGV AQFSIDYKNV SNPEAWQVNV SLNIRPSSGT GVMLALVSSN TVPFALSLVD
SATEELQDIL VSVENMVIAR IEALSLCSNQ QSLLEIRVNR NNVELLTQHR KDSFHSEDFQ
RQFAILDKAM KETVATYLGG LPDVPFSATP VNAFYNGCME VNINGVQLDL DEAISKHNDI
RAHSCPSVWK KTKNT
//
