ID   PROS_RABIT              Reviewed;         646 AA.
AC   P98118;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Vitamin K-dependent protein S;
DE   Flags: Precursor; Fragment;
GN   Name=PROS1; Synonyms=PROS;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8223642; DOI=10.1111/j.1432-1033.1993.tb18314.x;
RA   He X., Dahlbaeck B.;
RT   "Molecular cloning, expression and functional characterization of rabbit
RT   anticoagulant vitamin-K-dependent protein S.";
RL   Eur. J. Biochem. 217:857-865(1993).
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   -!- SUBUNIT: Interacts with C4b-binding protein, a regulator of the complex
CC       system. In rabbit plasma however, protein S appears to be present only
CC       in free form.
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; Z26485; CAA81259.1; -; mRNA.
DR   PIR; S38819; S38819.
DR   AlphaFoldDB; P98118; -.
DR   SMR; P98118; -.
DR   STRING; 9986.ENSOCUP00000018723; -.
DR   PRIDE; P98118; -.
DR   eggNOG; ENOG502QSNF; Eukaryota.
DR   InParanoid; P98118; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProt.
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; 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   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   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; Zymogen.
FT   PROPEP          <1..12
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000022125"
FT   CHAIN           13..646
FT                   /note="Vitamin K-dependent protein S"
FT                   /id="PRO_0000022126"
FT   DOMAIN          13..58
FT                   /note="Gla"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT   DOMAIN          88..126
FT                   /note="EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          128..171
FT                   /note="EGF-like 2; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          172..213
FT                   /note="EGF-like 3; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          214..254
FT                   /note="EGF-like 4; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          270..446
FT                   /note="Laminin G-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          455..636
FT                   /note="Laminin G-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   REGION          59..87
FT                   /note="Thrombin-sensitive"
FT   MOD_RES         18
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P07224,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         19
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P07224,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         26
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P07224,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         28
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P07224,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         31
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P07224,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         32
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P07224,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         37
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P07224,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         38
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P07224,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         41
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P07224,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         44
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         107
FT                   /note="(3R)-3-hydroxyaspartate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        470
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        480
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        29..34
FT                   /evidence="ECO:0000250"
FT   DISULFID        92..105
FT                   /evidence="ECO:0000250"
FT   DISULFID        97..114
FT                   /evidence="ECO:0000250"
FT   DISULFID        116..125
FT                   /evidence="ECO:0000250"
FT   DISULFID        132..146
FT                   /evidence="ECO:0000250"
FT   DISULFID        142..155
FT                   /evidence="ECO:0000250"
FT   DISULFID        157..170
FT                   /evidence="ECO:0000250"
FT   DISULFID        176..188
FT                   /evidence="ECO:0000250"
FT   DISULFID        183..197
FT                   /evidence="ECO:0000250"
FT   DISULFID        199..212
FT                   /evidence="ECO:0000250"
FT   DISULFID        218..227
FT                   /evidence="ECO:0000250"
FT   DISULFID        223..236
FT                   /evidence="ECO:0000250"
FT   DISULFID        238..253
FT                   /evidence="ECO:0000250"
FT   DISULFID        420..446
FT                   /evidence="ECO:0000250"
FT   DISULFID        609..636
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   646 AA;  71969 MW;  131219C48891B2EC CRC64;
     GHASQVLVRK RRANSMLEET KKGNLERECI EELCNKEEAR EVFENDPETD YFYPKYLGCL
     GSFRAKLFTA TRRSANGYPD LRSCVNAIPD QCNPLPCSEE GYLNCKDGQA TFTCICKPGW
     QGEKCEIDIN ECKDPTNING GCSQICDNTA GSYHCSCKSG FVMLANEKDC KDMDECSVKP
     SVCGTAVCKN TPGDFECECS EGYRYNPTAK SCEDIDECSE NMCAQLCVNY PGGYSCYCDG
     KKGFKLAQDK KSCEAVPVCL PLDLDKNYQL LYLAEQFVGA VLYLKFHLPE ITRFSAEFDF
     RTYDSEGVIL YAESLDHSTW FLIALRQGKI EIQFKNDYAA QITTGGQVIN DGLWNMVSVE
     ELEHSVSIKI AQEPVMNINK PGSLFKPTNG FLETKVYFAG LPRKVENALI RPINPRLDGC
     MRGWNLMKQG ASGVKEIIQQ KQKKHCLVTV EKGSYYPGSG IAQFHIDYNN LSYVEDWQVN
     VTLNIRPSTG TGVMLTLVSG NTLPFALSLV QSTSETSQDI LVSVENRVIY QLESISLCSG
     QQSQLEFSVS RNHLELSTPL VKDVIYSEDL QRHLAVLDEA MKGTVTTYLG GLPEVPFNAT
     PVNAFYNGCM EVNINGVQLD LDEAISKHND IRAHSCPSVW NDKTNS