ID   E7END6_HUMAN            Unreviewed;       495 AA.
AC   E7END6;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   16-JAN-2019, entry version 71.
DE   SubName: Full=Vitamin K-dependent protein C {ECO:0000313|Ensembl:ENSP00000386679};
GN   Name=PROC {ECO:0000313|Ensembl:ENSP00000386679};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000386679, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000386679, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 4.";
RL   Nature 434:724-731(2005).
RN   [2] {ECO:0000313|Ensembl:ENSP00000386679}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2011) to UniProtKB.
RN   [3] {ECO:0000213|PubMed:24275569}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|SAAS:SAAS00748227}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000256|SAAS:SAAS00559343}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   EMBL; AC068282; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_016859995.1; XM_017004506.1.
DR   ProteinModelPortal; E7END6; -.
DR   jPOST; E7END6; -.
DR   MaxQB; E7END6; -.
DR   PRIDE; E7END6; -.
DR   Ensembl; ENST00000409048; ENSP00000386679; ENSG00000115718.
DR   UCSC; uc061nom.1; human.
DR   EuPathDB; HostDB:ENSG00000115718.17; -.
DR   HGNC; HGNC:9451; PROC.
DR   OpenTargets; ENSG00000115718; -.
DR   GeneTree; ENSGT00940000154505; -.
DR   OMA; LDWIHSH; -.
DR   ChiTaRS; PROC; human.
DR   GenomeRNAi; 5624; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   Bgee; ENSG00000115718; Expressed in 94 organ(s), highest expression level in right lobe of liver.
DR   ExpressionAtlas; E7END6; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; 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:InterPro.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 4.10.740.10; -; 1.
DR   InterPro; IPR017857; Coagulation_fac-like_Gla_dom.
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; IPR012224; Pept_S1A_FX.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   Pfam; PF00008; EGF; 1.
DR   Pfam; PF00594; Gla; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PIRSF; PIRSF001143; Factor_X; 2.
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; SSF50494; SSF50494; 1.
DR   SUPFAM; SSF57630; SSF57630; 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   1: Evidence at protein level;
KW   Complete proteome {ECO:0000313|Proteomes:UP000005640};
KW   Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00076,
KW   ECO:0000256|SAAS:SAAS00037407};
KW   EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076,
KW   ECO:0000256|SAAS:SAAS00032677};
KW   Hydrolase {ECO:0000256|RuleBase:RU363034};
KW   Protease {ECO:0000256|RuleBase:RU363034};
KW   Proteomics identification {ECO:0000213|MaxQB:E7END6,
KW   ECO:0000213|PeptideAtlas:E7END6};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   Secreted {ECO:0000256|SAAS:SAAS00749664};
KW   Serine protease {ECO:0000256|RuleBase:RU363034};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     18       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        19    495       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5003218964.
FT   DOMAIN       42     88       Gla. {ECO:0000259|PROSITE:PS50998}.
FT   DOMAIN       97    132       EGF-like. {ECO:0000259|PROSITE:PS50026}.
FT   DOMAIN      246    484       Peptidase S1.
FT                                {ECO:0000259|PROSITE:PS50240}.
FT   ACT_SITE    287    287       Charge relay system.
FT                                {ECO:0000256|PIRSR:PIRSR001143-1}.
FT   ACT_SITE    333    333       Charge relay system.
FT                                {ECO:0000256|PIRSR:PIRSR001143-1}.
FT   ACT_SITE    436    436       Charge relay system.
FT                                {ECO:0000256|PIRSR:PIRSR001143-1}.
FT   DISULFID    101    111       {ECO:0000256|PROSITE-ProRule:PRU00076}.
FT   DISULFID    122    131       {ECO:0000256|PROSITE-ProRule:PRU00076}.
SQ   SEQUENCE   495 AA;  55390 MW;  9607664277F6BB75 CRC64;
     MWQLTSLLLF VATWGISGTP APLDSVFSSS ERAHQVLRIR KRANSFLEEL RHSSLERECI
     EEICDFEEAK EIFQNVDDTL AFWSKHVDGD QCLVLPLEHP CASLCCGHGT CIDGIGSFSC
     DCRSGWEGRF CQRGEGERWM LAGGGAGLGP GWGRGTSTSC PRPPLPAEVS FLNCSLDNGG
     CTHYCLEEVG WRRCSCAPGY KLGDDLLQCH PAVKFPCGRP WKRMEKKRSH LKRDTEDQED
     QVDPRLIDGK MTRRGDSPWQ VVLLDSKKKL ACGAVLIHPS WVLTAAHCMD ESKKLLVRLG
     EYDLRRWEKW ELDLDIKEVF VHPNYSKSTT DNDIALLHLA QPATLSQTIV PICLPDSGLA
     ERELNQAGQE TLVTGWGYHS SREKEAKRNR TFVLNFIKIP VVPHNECSEV MSNMVSENML
     CAGILGDRQD ACEGDSGGPM VASFHGTWFL VGLVSWGEGC GLLHNYGVYT KVSRYLDWIH
     GHIRDKEAPQ KSWAP
//