ID G3V843_RAT Unreviewed; 617 AA. AC G3V843; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAR-2024, entry version 104. DE RecName: Full=Prothrombin {ECO:0000256|ARBA:ARBA00014840, ECO:0000256|PIRNR:PIRNR001149}; DE EC=3.4.21.5 {ECO:0000256|ARBA:ARBA00012174, ECO:0000256|PIRNR:PIRNR001149}; DE AltName: Full=Coagulation factor II {ECO:0000256|ARBA:ARBA00032835, ECO:0000256|PIRNR:PIRNR001149}; GN Name=F2 {ECO:0000313|Ensembl:ENSRNOP00000022233.3, GN ECO:0000313|RGD:61996}; 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|Ensembl:ENSRNOP00000022233.3, ECO:0000313|Proteomes:UP000002494}; RN [1] {ECO:0000313|Ensembl:ENSRNOP00000022233.3, ECO:0000313|Proteomes:UP000002494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000022233.3, RC ECO:0000313|Proteomes:UP000002494}; RX PubMed=15057822; DOI=10.1038/nature02426; RG Rat Genome Sequencing Project Consortium; RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., RA Mockrin S., Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into mammalian RT evolution."; RL Nature 428:493-521(2004). RN [2] {ECO:0000313|Ensembl:ENSRNOP00000022233.3} RP IDENTIFICATION. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000022233.3}; RG Ensembl; RL Submitted (NOV-2023) to UniProtKB. CC -!- FUNCTION: Thrombin, which cleaves bonds after Arg and Lys, converts CC fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in CC complex with thrombomodulin, protein C. Functions in blood homeostasis, CC inflammation and wound healing. {ECO:0000256|ARBA:ARBA00025390, CC ECO:0000256|PIRNR:PIRNR001149}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Selective cleavage of Arg-|-Gly bonds in fibrinogen to form CC fibrin and release fibrinopeptides A and B.; EC=3.4.21.5; CC Evidence={ECO:0000256|ARBA:ARBA00001621, CC ECO:0000256|PIRNR:PIRNR001149}; CC -!- SIMILARITY: Belongs to the peptidase S1 family. CC {ECO:0000256|PIRNR:PIRNR001149}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC 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 RefSeq; NP_075213.2; NM_022924.2. DR AlphaFoldDB; G3V843; -. DR SMR; G3V843; -. DR MEROPS; S01.217; -. DR Ensembl; ENSRNOT00000022233.6; ENSRNOP00000022233.3; ENSRNOG00000016325.6. DR GeneID; 29251; -. DR KEGG; rno:29251; -. DR CTD; 2147; -. DR RGD; 61996; F2. DR GeneTree; ENSGT00940000154234; -. DR HOGENOM; CLU_006842_19_4_1; -. DR OMA; VMIFRKS; -. DR OrthoDB; 211181at2759; -. DR TreeFam; TF327329; -. DR Proteomes; UP000002494; Chromosome 3. DR Bgee; ENSRNOG00000016325; Expressed in liver and 17 other cell types or tissues. DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl. DR GO; GO:0005615; C:extracellular space; IEA:Ensembl. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0008201; F:heparin binding; IEA:Ensembl. DR GO; GO:0001530; F:lipopolysaccharide binding; IEA:Ensembl. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC. DR GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl. DR GO; GO:0070053; F:thrombospondin receptor activity; IEA:Ensembl. DR GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW. DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IEA:Ensembl. DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:Ensembl. DR GO; GO:0051838; P:cytolysis by host of symbiont cells; IEA:Ensembl. DR GO; GO:0042730; P:fibrinolysis; IEA:Ensembl. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:Ensembl. DR GO; GO:1990806; P:ligand-gated ion channel signaling pathway; IEA:Ensembl. DR GO; GO:0048712; P:negative regulation of astrocyte differentiation; IEA:Ensembl. DR GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; IEA:Ensembl. DR GO; GO:0045861; P:negative regulation of proteolysis; IEA:Ensembl. DR GO; GO:0070945; P:neutrophil-mediated killing of gram-negative bacterium; IEA:Ensembl. DR GO; GO:0030168; P:platelet activation; IEA:Ensembl. DR GO; GO:0030194; P:positive regulation of blood coagulation; IEA:Ensembl. DR GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl. DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IEA:Ensembl. DR GO; GO:0032024; P:positive regulation of insulin secretion; IEA:Ensembl. DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl. DR GO; GO:1900738; P:positive regulation of phospholipase C-activating G protein-coupled receptor signaling pathway; IEA:Ensembl. DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; IEA:Ensembl. DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl. DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IEA:Ensembl. DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IEA:Ensembl. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl. DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IEA:Ensembl. DR CDD; cd00108; KR; 2. DR CDD; cd00190; Tryp_SPc; 1. DR Gene3D; 2.40.20.10; Plasminogen Kringle 4; 2. DR Gene3D; 4.10.140.10; Thrombin light chain domain; 1. DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2. 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; IPR043504; Peptidase_S1_PA_chymotrypsin. 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; PROTHROMBIN; 1. DR PANTHER; PTHR24254:SF10; PROTHROMBIN; 1. DR Pfam; PF00594; Gla; 1. DR Pfam; PF00051; Kringle; 2. DR Pfam; PF09396; Thrombin_light; 1. DR Pfam; PF00089; Trypsin; 1. DR PIRSF; PIRSF001149; Thrombin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR PRINTS; PR00001; GLABLOOD. DR PRINTS; PR00018; KRINGLE. DR PRINTS; PR01505; PROTHROMBIN. DR SMART; SM00069; GLA; 1. DR SMART; SM00130; KR; 2. DR SMART; SM00020; Tryp_SPc; 1. DR SUPFAM; SSF57630; GLA-domain; 1. DR SUPFAM; SSF57440; Kringle-like; 2. DR SUPFAM; SSF50494; Trypsin-like serine proteases; 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 3: Inferred from homology; KW Acute phase {ECO:0000256|ARBA:ARBA00022486, ECO:0000256|PIRNR:PIRNR001149}; KW Blood coagulation {ECO:0000256|ARBA:ARBA00023084, KW ECO:0000256|PIRNR:PIRNR001149}; Calcium {ECO:0000256|ARBA:ARBA00022837}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE- KW ProRule:PRU00121}; KW Gamma-carboxyglutamic acid {ECO:0000256|ARBA:ARBA00022479}; KW Hemostasis {ECO:0000256|ARBA:ARBA00022696, ECO:0000256|PIRNR:PIRNR001149}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR001149}; KW Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE- KW ProRule:PRU00121}; KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PIRNR:PIRNR001149}; KW Reference proteome {ECO:0000313|Proteomes:UP000002494}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Serine protease {ECO:0000256|PIRNR:PIRNR001149}; KW Signal {ECO:0000256|ARBA:ARBA00022729}. FT DISULFID 215..292 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121" FT DISULFID 264..287 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121" SQ SEQUENCE 617 AA; 70386 MW; 8C11117828B20AC0 CRC64; MSHVRGLGLP GCLALAALAS LVHSQHVFLA PQQALSLLQR VRRANSGFLE ELRKGNLERE CVEEQCSYEE AFEALESPQD TDVFWAKYTV CDSVRKPRET FMDCLEGRCA MDLGLNYHGN VSVTHTGIEC QLWRSRYPHR PDINSTTHPG ADLKENFCRN PDSSTSGPWC YTTDPTVRRE ECSIPVCGQE GRTTVKMTPR SRGSKENLSP PLGECLLERG RLYQGNLAVT TLGSPCLAWD SLPTKTLSKY QNFDPEVKLV QNFCRNPDRD EEGAWCFVAQ QPGFEYCSLN YCDEAVGEEN HDGDESIAGR TTDAEFHTFF DERTFGLGEA DCGLRPLFEK KSLTDKTEKE LLDSYIDGRI VEGWDAEKGI APWQVMLFRK SPQELLCGAS LISDRWVLTA AHCILYPPWD KNFTENDLLV RIGKHSRTRY ERNVEKISML EKIYIHPRYN WRENLDRDIA LLKLKKPVPF SDYIHPVCLP DKQTVTSLLQ AGYKGRVTGW GNLRETWTTN INEIQPSVLQ VVNLPIVERP VCKASTRIRI TDNMFCAGFK VNDTKRGDAC EGDSGGPFVM KSPYNHRWYQ MGIVSWGEGC DRNGKYGFYT HVFRLKRWMQ KVIDQHR //