PROS_MACMU
ID PROS_MACMU Reviewed; 649 AA.
AC Q28520;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Vitamin K-dependent protein S;
DE Flags: Precursor; Fragment;
GN Name=PROS1; Synonyms=PROS;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=7832752; DOI=10.1042/bj3050397;
RA Greengard J.S., Fernandez J.A., Radtke K.P., Griffin J.H.;
RT "Identification of candidate residues for interaction of protein S with C4b
RT binding protein and activated protein C.";
RL Biochem. J. 305:397-403(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA70376.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L31380; AAA70376.1; ALT_INIT; mRNA.
DR PIR; S53434; S53434.
DR RefSeq; NP_001038191.1; NM_001044726.1.
DR AlphaFoldDB; Q28520; -.
DR SMR; Q28520; -.
DR STRING; 9544.ENSMMUP00000026760; -.
DR GeneID; 694845; -.
DR KEGG; mcc:694845; -.
DR CTD; 5627; -.
DR eggNOG; ENOG502QSNF; Eukaryota.
DR InParanoid; Q28520; -.
DR Proteomes; UP000006718; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProt.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005796; C:Golgi lumen; 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:SF10; PTHR24040:SF10; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF07645; EGF_CA; 2.
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; 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; 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..14
FT /evidence="ECO:0000250"
FT /id="PRO_0000022121"
FT CHAIN 15..649
FT /note="Vitamin K-dependent protein S"
FT /id="PRO_0000022122"
FT DOMAIN 15..60
FT /note="Gla"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT DOMAIN 90..128
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 130..173
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 174..215
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 216..256
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 272..448
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 457..639
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT REGION 61..89
FT /note="Thrombin-sensitive"
FT MOD_RES 20
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P07224,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 21
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 30
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P07224,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 33
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P07224,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 34
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P07224,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 39
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P07224,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 40
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P07224,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 43
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P07224,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 46
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P07224,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 50
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P07224,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 109
FT /note="(3R)-3-hydroxyaspartate"
FT /evidence="ECO:0000250"
FT CARBOHYD 472
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 482
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 503
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..36
FT /evidence="ECO:0000250"
FT DISULFID 94..107
FT /evidence="ECO:0000250"
FT DISULFID 99..116
FT /evidence="ECO:0000250"
FT DISULFID 118..127
FT /evidence="ECO:0000250"
FT DISULFID 134..148
FT /evidence="ECO:0000250"
FT DISULFID 144..157
FT /evidence="ECO:0000250"
FT DISULFID 159..172
FT /evidence="ECO:0000250"
FT DISULFID 178..190
FT /evidence="ECO:0000250"
FT DISULFID 185..199
FT /evidence="ECO:0000250"
FT DISULFID 201..214
FT /evidence="ECO:0000250"
FT DISULFID 220..229
FT /evidence="ECO:0000250"
FT DISULFID 225..238
FT /evidence="ECO:0000250"
FT DISULFID 240..255
FT /evidence="ECO:0000250"
FT DISULFID 422..448
FT /evidence="ECO:0000250"
FT DISULFID 612..639
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 649 AA; 72402 MW; 5C7C13D31CD7EB6B CRC64;
SKQQASQVLV RKRRANSMLE ETKQGNLERE CIEELCNKEE AREVFENDPE TDYFYPKYLV
CLRSFQSGLF TAARQSTDAY PDLRSCVNAI PDQCSPLPCN EDGYMSCKDG KASFTCTCKP
GWQGERCEFD INECKDPSNI NGGCSQICDN TPGSYHCSCK SGFVMLSNKK DCKDVDECSL
KPNMCGTAVC KNIPGDFECE CPEGYRYNLK SKSCEDVDEC SENMCAQLCV NYPGGYTCYC
DGKKGFKLAQ DQKSCEAVSV CLPLNLDTKY ELLYLAEQFA GVVLYLKFRL PEISRFSAEF
DFRTYDSQGV ILYAESIDHS AWLLIALRGG KIEVQLKNEH TSKITTGGDI INNGLWNMVS
VEELEHSISI KIAKEAVMDI NKPGPLFKPE NGLLETKVYF AGFPRKVESE LIKPINPRLD
GCIRSWNLMK QGASGIKEII QEKQNKHCLV TVEKGSYYPG SGIAEFHIDY NNGSNAEGWH
INVTLNIRPS TGTGVMLALV SSNNTVPFAV SLVDSTSEKS QDIVISVENT VIYRIQALSL
CSYQRSHLEF RVNRNNLELL TPLKIETISQ EELQTQLAIL DKAMKGKVAT YLGGLPDVPF
SATPVNAFYN GCMEVNINGV ELDLDEAISK HNDIRAHSCP SVWKKTKNS
