ID E9PIT3_HUMAN Unreviewed; 583 AA. AC E9PIT3; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 16-JAN-2019, entry version 65. DE SubName: Full=Prothrombin {ECO:0000313|Ensembl:ENSP00000433907}; GN Name=F2 {ECO:0000313|Ensembl:ENSP00000433907}; 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:ENSP00000433907, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000433907, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [2] {ECO:0000313|Ensembl:ENSP00000433907} 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 -!- 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:PRU00121}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AC115088; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; E9PIT3; -. DR SMR; E9PIT3; -. DR jPOST; E9PIT3; -. DR MaxQB; E9PIT3; -. DR PeptideAtlas; E9PIT3; -. DR PRIDE; E9PIT3; -. DR Ensembl; ENST00000530231; ENSP00000433907; ENSG00000180210. DR UCSC; uc058aym.1; human. DR EuPathDB; HostDB:ENSG00000180210.14; -. DR HGNC; HGNC:3535; F2. DR OpenTargets; ENSG00000180210; -. DR GeneTree; ENSGT00940000154234; -. DR ChiTaRS; F2; human. DR Proteomes; UP000005640; Chromosome 11. DR Bgee; ENSG00000180210; Expressed in 66 organ(s), highest expression level in right lobe of liver. DR ExpressionAtlas; E9PIT3; baseline and differential. DR GO; GO:0005576; C:extracellular region; IEA:InterPro. 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; cd00108; KR; 2. DR CDD; cd00190; Tryp_SPc; 1. DR Gene3D; 2.40.20.10; -; 2. DR Gene3D; 4.10.140.10; -; 1. DR InterPro; IPR035972; GLA-like_dom_SF. DR InterPro; IPR000294; GLA_domain. DR InterPro; IPR000001; Kringle. DR InterPro; IPR013806; Kringle-like. DR InterPro; IPR018056; Kringle_CS. DR InterPro; IPR038178; Kringle_sf. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR001314; Peptidase_S1A. DR InterPro; IPR003966; Prothrombin/thrombin. DR InterPro; IPR018992; Thrombin_light_chain. DR InterPro; IPR037111; Thrombin_light_chain_sf. DR InterPro; IPR001254; Trypsin_dom. DR InterPro; IPR018114; TRYPSIN_HIS. DR InterPro; IPR033116; TRYPSIN_SER. DR PANTHER; PTHR24254:SF10; PTHR24254:SF10; 2. DR Pfam; PF00594; Gla; 1. DR Pfam; PF00051; Kringle; 2. DR Pfam; PF09396; Thrombin_light; 1. DR Pfam; PF00089; Trypsin; 2. DR PIRSF; PIRSF001149; Thrombin; 2. DR PRINTS; PR00722; CHYMOTRYPSIN. DR PRINTS; PR00001; GLABLOOD. DR PRINTS; PR01505; PROTHROMBIN. DR SMART; SM00069; GLA; 1. DR SMART; SM00130; KR; 2. DR SMART; SM00020; Tryp_SPc; 1. DR SUPFAM; SSF50494; SSF50494; 1. DR SUPFAM; SSF57440; SSF57440; 2. DR SUPFAM; SSF57630; SSF57630; 1. DR PROSITE; PS00011; GLA_1; 1. DR PROSITE; PS50998; GLA_2; 1. DR PROSITE; PS00021; KRINGLE_1; 2. DR PROSITE; PS50070; KRINGLE_2; 2. 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|PIRSR:PIRSR001149-4, KW ECO:0000256|SAAS:SAAS00037407}; KW Hydrolase {ECO:0000256|RuleBase:RU363034, KW ECO:0000256|SAAS:SAAS00745848}; KW Kringle {ECO:0000256|PROSITE-ProRule:PRU00121, KW ECO:0000256|SAAS:SAAS00045973}; KW Protease {ECO:0000256|RuleBase:RU363034, KW ECO:0000256|SAAS:SAAS00745848}; KW Proteomics identification {ECO:0000213|EPD:E9PIT3, KW ECO:0000213|MaxQB:E9PIT3, ECO:0000213|PeptideAtlas:E9PIT3}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Serine protease {ECO:0000256|RuleBase:RU363034, KW ECO:0000256|SAAS:SAAS00745848}; Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 24 {ECO:0000256|SAM:SignalP}. FT CHAIN 25 583 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003245057. FT DOMAIN 43 89 Gla. {ECO:0000259|PROSITE:PS50998}. FT DOMAIN 107 186 Kringle. {ECO:0000259|PROSITE:PS50070}. FT DOMAIN 212 291 Kringle. {ECO:0000259|PROSITE:PS50070}. FT DOMAIN 364 579 Peptidase S1. FT {ECO:0000259|PROSITE:PS50240}. FT SITE 198 199 Cleavage; by thrombin. FT {ECO:0000256|PIRSR:PIRSR001149-2}. FT SITE 327 328 Cleavage; by factor Xa. FT {ECO:0000256|PIRSR:PIRSR001149-2}. FT SITE 363 364 Cleavage; by factor Xa. FT {ECO:0000256|PIRSR:PIRSR001149-2}. FT CARBOHYD 121 121 N-linked (GlcNAc...) (complex) FT asparagine. FT {ECO:0000256|PIRSR:PIRSR001149-3}. FT CARBOHYD 143 143 N-linked (GlcNAc...) (complex) FT asparagine. FT {ECO:0000256|PIRSR:PIRSR001149-3}. FT CARBOHYD 416 416 N-linked (GlcNAc...) (complex) FT asparagine. FT {ECO:0000256|PIRSR:PIRSR001149-3}. FT DISULFID 60 65 {ECO:0000256|PIRSR:PIRSR001149-4}. FT DISULFID 90 103 {ECO:0000256|PIRSR:PIRSR001149-4}. FT DISULFID 108 186 {ECO:0000256|PIRSR:PIRSR001149-4}. FT DISULFID 129 169 {ECO:0000256|PIRSR:PIRSR001149-4}. FT DISULFID 157 181 {ECO:0000256|PIRSR:PIRSR001149-4}. FT DISULFID 213 291 {ECO:0000256|PIRSR:PIRSR001149-4}. FT DISULFID 234 274 {ECO:0000256|PIRSR:PIRSR001149-4}. FT DISULFID 262 286 {ECO:0000256|PIRSR:PIRSR001149-4}. FT DISULFID 391 407 {ECO:0000256|PIRSR:PIRSR001149-4}. FT DISULFID 497 511 {ECO:0000256|PIRSR:PIRSR001149-4}. FT DISULFID 525 555 {ECO:0000256|PIRSR:PIRSR001149-4}. SQ SEQUENCE 583 AA; 65409 MW; 9AA7C96D997C827C CRC64; MAHVRGLQLP GCLALAALCS LVHSQHVFLA PQQARSLLQR VRRANTFLEE VRKGNLEREC VEETCSYEEA FEALESSTAT DVFWAKYTAC ETARTPRDKL AACLEGNCAE GLGTNYRGHV NITRSGIECQ LWRSRYPHKP EINSTTHPGA DLQENFCRNP DSSTTGPWCY TTDPTVRRQE CSIPVCGQDQ VTVAMTPRSE GSSVNLSPPL EQCVPDRGQQ YQGRLAVTTH GLPCLAWASA QAKALSKHQD FNSAVQLVEN FCRNPDGDEE GVWCYVAGKP GDFGYCDLNY CEEAVEEETG DGLDEDSDRA IEGRTATSEY QTFFNPRTFG SGEADCGLRP LFEKKSLEDK TERELLESYI DGRIVEGSDA EIGMSPWQVM LFRKSPQELL CGASLISDRW VLTAAHCLLY PPWDKNFTEN DLLVRIGKHS RTRYERNIEK ISMLEKIYIH PSLLQAGYKG RVTGWGNLKE TWTANVGKGQ PSVLQVVNLP IVERPVCKDS TRIRITDNMF CAGYKPDEGK RGDACEGDSG GPFVMKSPFN NRWYQMGIVS WGEGCDRDGK YGFYTHVFRL KKWIQKVIDQ FGE //