ID Q68FY8_RAT Unreviewed; 461 AA.
AC Q68FY8;
DT 11-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 11-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 170.
DE RecName: Full=Vitamin K-dependent protein C {ECO:0000256|ARBA:ARBA00040219};
DE EC=3.4.21.69 {ECO:0000256|ARBA:ARBA00038995};
DE AltName: Full=Anticoagulant protein C {ECO:0000256|ARBA:ARBA00042906};
DE AltName: Full=Autoprothrombin IIA {ECO:0000256|ARBA:ARBA00041306};
DE AltName: Full=Blood coagulation factor XIV {ECO:0000256|ARBA:ARBA00042403};
GN Name=Proc {ECO:0000313|EMBL:AAH78879.1, ECO:0000313|RGD:3411};
GN ORFNames=rCG_49213 {ECO:0000313|EMBL:EDL76183.1};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000313|EMBL:AAH78879.1};
RN [1] {ECO:0000313|EMBL:AAH78879.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung {ECO:0000313|EMBL:AAH78879.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2] {ECO:0000313|EMBL:EDL76183.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BN {ECO:0000313|EMBL:EDL76183.1};
RX PubMed=15632090; DOI=10.1101/gr.2889405;
RA Florea L., Di Francesco V., Miller J., Turner R., Yao A., Harris M.,
RA Walenz B., Mobarry C., Merkulov G.V., Charlab R., Dew I., Deng Z.,
RA Istrail S., Li P., Sutton G.;
RT "Gene and alternative splicing annotation with AIR.";
RL Genome Res. 15:54-66(2005).
RN [3] {ECO:0000313|EMBL:EDL76183.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BN {ECO:0000313|EMBL:EDL76183.1};
RA Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H.,
RA Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M.,
RA Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L., Lu F.,
RA Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C., Sutton G.G.,
RA Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Degradation of blood coagulation factors Va and VIIIa.;
CC EC=3.4.21.69; Evidence={ECO:0000256|ARBA:ARBA00036045};
CC -!- SUBUNIT: Synthesized as a single chain precursor, which is cleaved into
CC a light chain and a heavy chain held together by a disulfide bond. The
CC enzyme is then activated by thrombin, which cleaves a tetradecapeptide
CC from the amino end of the heavy chain; this reaction, which occurs at
CC the surface of endothelial cells, is strongly promoted by
CC thrombomodulin. {ECO:0000256|ARBA:ARBA00038638}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000256|ARBA:ARBA00004240}. Golgi apparatus
CC {ECO:0000256|ARBA:ARBA00004555}. Secreted
CC {ECO:0000256|ARBA:ARBA00004613}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; BC078879; AAH78879.1; -; mRNA.
DR EMBL; CH473974; EDL76183.1; -; Genomic_DNA.
DR RefSeq; XP_006254589.1; XM_006254527.2.
DR RefSeq; XP_008770240.2; XM_008772018.2.
DR AlphaFoldDB; Q68FY8; -.
DR SMR; Q68FY8; -.
DR MEROPS; S01.218; -.
DR GeneID; 25268; -.
DR CTD; 5624; -.
DR RGD; 3411; Proc.
DR HOGENOM; CLU_006842_19_5_1; -.
DR OrthoDB; 4629979at2759; -.
DR TreeFam; TF327329; -.
DR Proteomes; UP000234681; Chromosome 18.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IEA:UniProt.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 4.10.740.10; Coagulation Factor IX; 1.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR017857; Coagulation_fac-like_Gla_dom.
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; IPR012224; Pept_S1A_FX.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24278; COAGULATION FACTOR; 1.
DR PANTHER; PTHR24278:SF0; VITAMIN K-DEPENDENT PROTEIN C; 1.
DR Pfam; PF14670; FXa_inhibition; 1.
DR Pfam; PF00594; Gla; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF001143; Factor_X; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR PRINTS; PR00001; GLABLOOD.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 1.
DR SMART; SM00069; GLA; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF57630; GLA-domain; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS00011; GLA_1; 1.
DR PROSITE; PS50998; GLA_2; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 2: Evidence at transcript level;
KW Blood coagulation {ECO:0000256|ARBA:ARBA00023084};
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}; Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Gamma-carboxyglutamic acid {ECO:0000256|ARBA:ARBA00022479};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Hemostasis {ECO:0000256|ARBA:ARBA00022696};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363034};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU363034};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU363034}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..461
FT /note="Vitamin K-dependent protein C"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014310301"
FT DOMAIN 41..87
FT /note="Gla"
FT /evidence="ECO:0000259|PROSITE:PS50998"
FT DOMAIN 96..131
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 213..450
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT ACT_SITE 254
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001143-1"
FT ACT_SITE 300
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001143-1"
FT ACT_SITE 402
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001143-1"
FT DISULFID 100..110
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 121..130
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 461 AA; 51827 MW; C0181CED046B584B CRC64;
MWQFRIFLLF ASTWGISGVS AHPDPVFSSS EGAHQVLRVR RANSFLEEVR AGSLERECME
EICDFEEAQE IFQNVEDTLA FWIKYFDGDQ CSTPPLDHQC DSPCCGHGTC IDGLGGFSCS
CDKGWEGRFC QQEMGFQDCR VKNGGCYHYC LEETRGRRCA CAPGYELADD HMHCRPTVNF
PCGKLWKRTD KKRKNFKRDI DPEDEELELG PRIVNGTLTK QGDSPWQAIL LDSKKKLACG
GVLIHTSWVL TAAHCLESSK KLTVRLGEYD LRRRDPWELD LDIKEVLVHP NYTRSNSDND
IALLRLSQPA TLSKTIVPIC LPNSGLAQEL SQAGQETVVT GWGYQSDKVK DGRRNRTFIL
TFIRIPLAAR NDCMQVMNNV VSENMLCAGI IGDTRDACDG DSGGPMVVFF RGTWFLVGLV
SWGEGCGHLN NYGVYTKVGS YLKWIHSYIG ERDVSLKSPK L
//
