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Database: UniProt
Entry: P98118
LinkDB: P98118
Original site: P98118 
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   28-MAR-2018, entry version 124.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
OC   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
RT   rabbit anticoagulant vitamin-K-dependent protein S.";
RL   Eur. J. Biochem. 217:857-865(1993).
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   -!- SUBUNIT: Interacts with C4b-binding protein, a regulator of the
CC       complex system. In rabbit plasma however, protein S appears to be
CC       present only in free form.
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:0000250}.
DR   EMBL; Z26485; CAA81259.1; -; mRNA.
DR   PIR; S38819; S38819.
DR   UniGene; Ocu.6257; -.
DR   ProteinModelPortal; P98118; -.
DR   SMR; P98118; -.
DR   STRING; 9986.ENSOCUP00000018723; -.
DR   PRIDE; P98118; -.
DR   eggNOG; ENOG410IGF6; Eukaryota.
DR   eggNOG; ENOG410ZTGU; LUCA.
DR   HOGENOM; HOG000065758; -.
DR   HOVERGEN; HBG051702; -.
DR   InParanoid; P98118; -.
DR   Proteomes; UP000001811; Unplaced.
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; 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   Complete proteome; Disulfide bond; EGF-like domain; Fibrinolysis;
KW   Gamma-carboxyglutamic acid; Glycoprotein; Hemostasis; Hydroxylation;
KW   Reference proteome; Repeat; Secreted; Zymogen.
FT   PROPEP       <1     12       {ECO:0000255}.
FT                                /FTId=PRO_0000022125.
FT   CHAIN        13    646       Vitamin K-dependent protein S.
FT                                /FTId=PRO_0000022126.
FT   DOMAIN       13     58       Gla. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   DOMAIN       88    126       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      128    171       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      172    213       EGF-like 3; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      214    254       EGF-like 4; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      270    446       Laminin G-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN      455    636       Laminin G-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   REGION       59     87       Thrombin-sensitive.
FT   MOD_RES      18     18       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P07224,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      19     19       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P07224,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      26     26       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P07224,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      28     28       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P07224,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      31     31       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P07224,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      32     32       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P07224,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      37     37       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P07224,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      38     38       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P07224,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      41     41       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P07224,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      44     44       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P07224,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      48     48       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P07224,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES     107    107       (3R)-3-hydroxyaspartate. {ECO:0000250}.
FT   CARBOHYD    470    470       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    480    480       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     29     34       {ECO:0000250}.
FT   DISULFID     92    105       {ECO:0000250}.
FT   DISULFID     97    114       {ECO:0000250}.
FT   DISULFID    116    125       {ECO:0000250}.
FT   DISULFID    132    146       {ECO:0000250}.
FT   DISULFID    142    155       {ECO:0000250}.
FT   DISULFID    157    170       {ECO:0000250}.
FT   DISULFID    176    188       {ECO:0000250}.
FT   DISULFID    183    197       {ECO:0000250}.
FT   DISULFID    199    212       {ECO:0000250}.
FT   DISULFID    218    227       {ECO:0000250}.
FT   DISULFID    223    236       {ECO:0000250}.
FT   DISULFID    238    253       {ECO:0000250}.
FT   DISULFID    420    446       {ECO:0000250}.
FT   DISULFID    609    636       {ECO:0000250}.
FT   NON_TER       1      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
//
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