ID THRB_MOUSE Reviewed; 618 AA. AC P19221; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 1. DT 27-MAR-2024, entry version 224. DE RecName: Full=Prothrombin; DE EC=3.4.21.5; DE AltName: Full=Coagulation factor II; DE Contains: DE RecName: Full=Activation peptide fragment 1; DE Contains: DE RecName: Full=Activation peptide fragment 2; DE Contains: DE RecName: Full=Thrombin light chain; DE Contains: DE RecName: Full=Thrombin heavy chain; DE Flags: Precursor; GN Name=F2; Synonyms=Cf2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND GAMMA-CARBOXYGLUTAMATION AT GLU-50; GLU-51; RP GLU-58; GLU-60; GLU-63; GLU-64; GLU-69; GLU-70; GLU-73 AND GLU-76. RC STRAIN=C57BL/6J; TISSUE=Liver; RX PubMed=2222810; DOI=10.1089/dna.1990.9.487; RA Friezner Degen S.J., Schaffer L.A., Jamison C.S., Grant S.G., RA Fitzgibbon J.J., Pai J.-A., Chapman V.M., Elliott R.W.; RT "Characterization of the cDNA coding for mouse prothrombin and localization RT of the gene on mouse chromosome 2."; RL DNA Cell Biol. 9:487-498(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; 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 [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 384-618. RC TISSUE=Liver; RX PubMed=1557383; DOI=10.1073/pnas.89.7.2779; RA Banfield D.K., Macgillivray R.T.; RT "Partial characterization of vertebrate prothrombin cDNAs: amplification RT and sequence analysis of the B chain of thrombin from nine different RT species."; RL Proc. Natl. Acad. Sci. U.S.A. 89:2779-2783(1992). RN [4] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-122; ASN-413 AND ASN-553. RC STRAIN=C57BL/6J; TISSUE=Plasma; RX PubMed=17330941; DOI=10.1021/pr0604559; RA Bernhard O.K., Kapp E.A., Simpson R.J.; RT "Enhanced analysis of the mouse plasma proteome using cysteine-containing RT tryptic glycopeptides."; RL J. Proteome Res. 6:987-995(2007). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, RC Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 319-618, AND DISULFIDE BONDS. RX PubMed=17428793; DOI=10.1074/jbc.m701323200; RA Marino F., Chen Z.-W., Ergenekan C.E., Bush-Pelc L.A., Mathews F.S., RA Di Cera E.; RT "Structural basis of Na+ activation mimicry in murine thrombin."; RL J. Biol. Chem. 282:16355-16361(2007). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 317-618 OF MUTANT ALA-565 IN RP COMPLEXES WITH PAR3/F2RL2 AND PAR4/F2RL3, AND MUTAGENESIS OF SER-565. RX PubMed=17606903; DOI=10.1073/pnas.0704409104; RA Bah A., Chen Z.-W., Bush-Pelc L.A., Mathews F.S., Di Cera E.; RT "Crystal structures of murine thrombin in complex with the extracellular RT fragments of murine protease-activated receptors PAR3 and PAR4."; RL Proc. Natl. Acad. Sci. U.S.A. 104:11603-11608(2007). 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 (By similarity). {ECO:0000250}. 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 -!- ACTIVITY REGULATION: Inhibited by SERPINA5. {ECO:0000250}. CC -!- SUBUNIT: Heterodimer (named alpha-thrombin) of a light and a heavy CC chain; disulfide-linked. Forms a heterodimer with SERPINA5. In plasma, CC interacts (via N-terminus) with alpha-1-microglobulin; this interaction CC does not prevent the activation of prothrombin to thrombin. CC {ECO:0000250|UniProtKB:P00734}. CC -!- PTM: The gamma-carboxyglutamyl residues, which bind calcium ions, CC result from the carboxylation of glutamyl residues by a microsomal CC enzyme, the vitamin K-dependent carboxylase. The modified residues are CC necessary for the calcium-dependent interaction with a negatively CC charged phospholipid surface, which is essential for the conversion of CC prothrombin to thrombin. {ECO:0000269|PubMed:2222810}. CC -!- PTM: In the penultimate step of the coagulation cascade, prothrombin is CC converted to thrombin by the prothrombinase complex composed of factor CC Xa (F10), cofactor Va (F5), and phospholipids. This activation requires CC factor Xa-catalyzed sequential cleavage at 2 sites, Arg-311 and Arg- CC 360, along 2 possible pathways. In the first pathway, the first CC cleavage occurs at Arg-311, leading to the formation of the inactive CC intermediate prethrombin-2. This pathway preferentially occurs on CC platelets and in the absence of cofactor Va. In the second pathway, the CC first cleavage occurs at Arg-360, which separates protease domain into CC 2 chains that remain connected through a disulfide bond and generates CC the active intermediate meizothrombin. The presence of cofactor Va CC directs activation along the meizothrombin pathway and greatly CC accelerates the rate of cleavage at Arg-360, but has a smaller effect CC on the cleavage of meizothrombin at Arg-311. Meizothrombin accumulates CC as an intermediate when prothrombinase is assembled on the membrane of CC red blood cells. {ECO:0000250|UniProtKB:P00734}. CC -!- MISCELLANEOUS: Thrombin can itself cleave the N-terminal fragment CC (fragment 1) of the prothrombin, prior to its activation by factor Xa. CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE- CC ProRule:PRU00274}. 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; X52308; CAA36548.1; -; mRNA. DR EMBL; BC013662; AAH13662.1; -; mRNA. DR EMBL; M81394; AAA40435.1; -; mRNA. DR CCDS; CCDS16434.1; -. DR PIR; A35827; A35827. DR RefSeq; NP_034298.1; NM_010168.3. DR PDB; 2OCV; X-ray; 2.20 A; A=319-346, B=361-618. DR PDB; 2PUX; X-ray; 2.00 A; A=317-360, B=361-618. DR PDB; 2PV9; X-ray; 3.50 A; A=317-360, B=361-618. DR PDB; 3EDX; X-ray; 2.40 A; A/C/E=317-360, B/D/F=361-618. DR PDB; 3HK3; X-ray; 1.94 A; A=317-360, B=361-618. DR PDB; 3HK6; X-ray; 3.20 A; A/C=317-360, B/D=361-618. DR PDB; 3HKI; X-ray; 2.20 A; A/D=317-360, B/E=361-618. DR PDBsum; 2OCV; -. DR PDBsum; 2PUX; -. DR PDBsum; 2PV9; -. DR PDBsum; 3EDX; -. DR PDBsum; 3HK3; -. DR PDBsum; 3HK6; -. DR PDBsum; 3HKI; -. DR AlphaFoldDB; P19221; -. DR SMR; P19221; -. DR BioGRID; 199568; 9. DR DIP; DIP-60968N; -. DR IntAct; P19221; 6. DR MINT; P19221; -. DR STRING; 10090.ENSMUSP00000028681; -. DR BindingDB; P19221; -. DR ChEMBL; CHEMBL1075308; -. DR MEROPS; S01.217; -. DR GlyCosmos; P19221; 4 sites, No reported glycans. DR GlyGen; P19221; 4 sites. DR iPTMnet; P19221; -. DR PhosphoSitePlus; P19221; -. DR SwissPalm; P19221; -. DR CPTAC; non-CPTAC-3432; -. DR CPTAC; non-CPTAC-5620; -. DR jPOST; P19221; -. DR PaxDb; 10090-ENSMUSP00000028681; -. DR PeptideAtlas; P19221; -. DR ProteomicsDB; 259185; -. DR Antibodypedia; 857; 1316 antibodies from 42 providers. DR DNASU; 14061; -. DR Ensembl; ENSMUST00000028681.15; ENSMUSP00000028681.9; ENSMUSG00000027249.16. DR GeneID; 14061; -. DR KEGG; mmu:14061; -. DR UCSC; uc008kwg.2; mouse. DR AGR; MGI:88380; -. DR CTD; 2147; -. DR MGI; MGI:88380; F2. DR VEuPathDB; HostDB:ENSMUSG00000027249; -. DR eggNOG; ENOG502QTSX; Eukaryota. DR GeneTree; ENSGT00940000154234; -. DR HOGENOM; CLU_006842_19_4_1; -. DR InParanoid; P19221; -. DR OMA; VMIFRKS; -. DR OrthoDB; 211181at2759; -. DR PhylomeDB; P19221; -. DR TreeFam; TF327329; -. DR Reactome; R-MMU-140837; Intrinsic Pathway of Fibrin Clot Formation. DR Reactome; R-MMU-140875; Common Pathway of Fibrin Clot Formation. DR Reactome; R-MMU-159740; Gamma-carboxylation of protein precursors. DR Reactome; R-MMU-159763; Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus. DR Reactome; R-MMU-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins. DR Reactome; R-MMU-202733; Cell surface interactions at the vascular wall. DR Reactome; R-MMU-375276; Peptide ligand-binding receptors. DR Reactome; R-MMU-416476; G alpha (q) signalling events. DR Reactome; R-MMU-456926; Thrombin signalling through proteinase activated receptors (PARs). DR Reactome; R-MMU-76009; Platelet Aggregation (Plug Formation). DR Reactome; R-MMU-977606; Regulation of Complement cascade. DR BioGRID-ORCS; 14061; 2 hits in 63 CRISPR screens. DR ChiTaRS; F2; mouse. DR EvolutionaryTrace; P19221; -. DR PRO; PR:P19221; -. DR Proteomes; UP000000589; Chromosome 2. DR RNAct; P19221; Protein. DR Bgee; ENSMUSG00000027249; Expressed in left lobe of liver and 54 other cell types or tissues. DR ExpressionAtlas; P19221; baseline and differential. DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL. DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl. DR GO; GO:0005615; C:extracellular space; ISO:MGI. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0004175; F:endopeptidase activity; IMP:MGI. DR GO; GO:0008201; F:heparin binding; ISO:MGI. DR GO; GO:0001530; F:lipopolysaccharide binding; ISO:MGI. DR GO; GO:0008233; F:peptidase activity; IMP:MGI. DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:MGI. DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI. DR GO; GO:0070053; F:thrombospondin receptor activity; ISO:MGI. DR GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW. DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; ISO:MGI. DR GO; GO:0007166; P:cell surface receptor signaling pathway; ISO:MGI. DR GO; GO:0051838; P:cytolysis by host of symbiont cells; ISO:MGI. DR GO; GO:0042730; P:fibrinolysis; ISO:MGI. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:MGI. DR GO; GO:1990806; P:ligand-gated ion channel signaling pathway; IDA:MGI. DR GO; GO:0048712; P:negative regulation of astrocyte differentiation; ISO:MGI. DR GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; ISO:MGI. DR GO; GO:0045861; P:negative regulation of proteolysis; ISO:MGI. DR GO; GO:0070945; P:neutrophil-mediated killing of gram-negative bacterium; ISO:MGI. DR GO; GO:0030168; P:platelet activation; IDA:MGI. DR GO; GO:0030194; P:positive regulation of blood coagulation; ISO:MGI. DR GO; GO:0030307; P:positive regulation of cell growth; IGI:MGI. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IGI:MGI. DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; ISO:MGI. DR GO; GO:0032024; P:positive regulation of insulin secretion; IDA:MGI. DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IGI:MGI. DR GO; GO:1900738; P:positive regulation of phospholipase C-activating G protein-coupled receptor signaling pathway; ISO:MGI. DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; ISO:MGI. DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI. DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; ISO:MGI. DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; ISO:MGI. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR GO; GO:0008360; P:regulation of cell shape; IGI:MGI. DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; ISO:MGI. DR GO; GO:0010468; P:regulation of gene expression; IDA:MGI. DR GO; GO:0009611; P:response to wounding; ISO:MGI. DR GO; GO:0070493; P:thrombin-activated receptor signaling pathway; ISO:MGI. 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. DR Genevisible; P19221; MM. PE 1: Evidence at protein level; KW 3D-structure; Acute phase; Blood coagulation; Calcium; KW Cleavage on pair of basic residues; Disulfide bond; KW Gamma-carboxyglutamic acid; Glycoprotein; Hemostasis; Hydrolase; Kringle; KW Protease; Reference proteome; Repeat; Serine protease; Signal; Zymogen. FT SIGNAL 1..24 FT /evidence="ECO:0000255" FT PROPEP 25..43 FT /id="PRO_0000028165" FT CHAIN 44..618 FT /note="Prothrombin" FT /id="PRO_0000028166" FT PEPTIDE 44..200 FT /note="Activation peptide fragment 1" FT /id="PRO_0000028167" FT PEPTIDE 201..324 FT /note="Activation peptide fragment 2" FT /id="PRO_0000028168" FT CHAIN 312..360 FT /note="Thrombin light chain" FT /id="PRO_0000028169" FT CHAIN 361..618 FT /note="Thrombin heavy chain" FT /id="PRO_0000028170" FT DOMAIN 44..90 FT /note="Gla" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463" FT DOMAIN 109..187 FT /note="Kringle 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121" FT DOMAIN 215..292 FT /note="Kringle 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121" FT DOMAIN 361..615 FT /note="Peptidase S1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT REGION 548..570 FT /note="High affinity receptor-binding region which is also FT known as the TP508 peptide" FT /evidence="ECO:0000250" FT ACT_SITE 403 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT ACT_SITE 459 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT ACT_SITE 565 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT SITE 200..201 FT /note="Cleavage; by thrombin" FT SITE 311..312 FT /note="Cleavage; by factor Xa" FT /evidence="ECO:0000250|UniProtKB:P00734" FT SITE 360..361 FT /note="Cleavage; by factor Xa" FT /evidence="ECO:0000250|UniProtKB:P00734" FT MOD_RES 50 FT /note="4-carboxyglutamate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, FT ECO:0000269|PubMed:2222810" FT MOD_RES 51 FT /note="4-carboxyglutamate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, FT ECO:0000269|PubMed:2222810" FT MOD_RES 58 FT /note="4-carboxyglutamate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, FT ECO:0000269|PubMed:2222810" FT MOD_RES 60 FT /note="4-carboxyglutamate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, FT ECO:0000269|PubMed:2222810" FT MOD_RES 63 FT /note="4-carboxyglutamate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, FT ECO:0000269|PubMed:2222810" FT MOD_RES 64 FT /note="4-carboxyglutamate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, FT ECO:0000269|PubMed:2222810" FT MOD_RES 69 FT /note="4-carboxyglutamate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, FT ECO:0000269|PubMed:2222810" FT MOD_RES 70 FT /note="4-carboxyglutamate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, FT ECO:0000269|PubMed:2222810" FT MOD_RES 73 FT /note="4-carboxyglutamate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, FT ECO:0000269|PubMed:2222810" FT MOD_RES 76 FT /note="4-carboxyglutamate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463, FT ECO:0000269|PubMed:2222810" FT CARBOHYD 122 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:17330941" FT CARBOHYD 144 FT /note="N-linked (GlcNAc...) asparagine" FT CARBOHYD 413 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:17330941" FT CARBOHYD 553 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:17330941" FT DISULFID 61..66 FT /evidence="ECO:0000250" FT DISULFID 91..104 FT /evidence="ECO:0000250" FT DISULFID 109..187 FT /evidence="ECO:0000250" FT DISULFID 130..170 FT /evidence="ECO:0000250" FT DISULFID 158..182 FT /evidence="ECO:0000250" FT DISULFID 215..293 FT /evidence="ECO:0000250" FT DISULFID 236..276 FT /evidence="ECO:0000250" FT DISULFID 264..288 FT /evidence="ECO:0000250" FT DISULFID 333..479 FT /note="Interchain (between light and heavy chains)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121, FT ECO:0000255|PROSITE-ProRule:PRU00274, ECO:0000255|PROSITE- FT ProRule:PRU00463" FT DISULFID 388..404 FT /evidence="ECO:0000269|PubMed:17428793" FT DISULFID 533..547 FT /evidence="ECO:0000269|PubMed:17428793" FT DISULFID 561..591 FT /evidence="ECO:0000269|PubMed:17428793" FT MUTAGEN 565 FT /note="S->A: Loss of protease activity." FT /evidence="ECO:0000269|PubMed:17606903" FT HELIX 323..326 FT /evidence="ECO:0007829|PDB:2PUX" FT TURN 331..334 FT /evidence="ECO:0007829|PDB:3HK3" FT TURN 337..339 FT /evidence="ECO:0007829|PDB:3HK3" FT HELIX 340..342 FT /evidence="ECO:0007829|PDB:3HK3" FT HELIX 349..354 FT /evidence="ECO:0007829|PDB:3HK3" FT STRAND 375..380 FT /evidence="ECO:0007829|PDB:3HK3" FT TURN 381..384 FT /evidence="ECO:0007829|PDB:3HK3" FT STRAND 385..400 FT /evidence="ECO:0007829|PDB:3HK3" FT HELIX 402..404 FT /evidence="ECO:0007829|PDB:3HK3" FT HELIX 408..410 FT /evidence="ECO:0007829|PDB:3HK3" FT HELIX 416..418 FT /evidence="ECO:0007829|PDB:3HK3" FT STRAND 419..424 FT /evidence="ECO:0007829|PDB:3HK3" FT STRAND 427..430 FT /evidence="ECO:0007829|PDB:3HK3" FT TURN 433..435 FT /evidence="ECO:0007829|PDB:3HK3" FT STRAND 437..446 FT /evidence="ECO:0007829|PDB:3HK3" FT TURN 452..454 FT /evidence="ECO:0007829|PDB:3HK3" FT STRAND 461..467 FT /evidence="ECO:0007829|PDB:3HK3" FT HELIX 483..489 FT /evidence="ECO:0007829|PDB:3HK3" FT STRAND 495..500 FT /evidence="ECO:0007829|PDB:3HK3" FT STRAND 504..507 FT /evidence="ECO:0007829|PDB:2PUX" FT HELIX 512..515 FT /evidence="ECO:0007829|PDB:2PUX" FT STRAND 521..527 FT /evidence="ECO:0007829|PDB:3HK3" FT HELIX 530..535 FT /evidence="ECO:0007829|PDB:3HK3" FT STRAND 545..548 FT /evidence="ECO:0007829|PDB:3HK3" FT STRAND 554..556 FT /evidence="ECO:0007829|PDB:3EDX" FT HELIX 562..564 FT /evidence="ECO:0007829|PDB:3HK3" FT STRAND 568..572 FT /evidence="ECO:0007829|PDB:3HK3" FT TURN 574..576 FT /evidence="ECO:0007829|PDB:3HK3" FT STRAND 579..587 FT /evidence="ECO:0007829|PDB:3HK3" FT HELIX 591..593 FT /evidence="ECO:0007829|PDB:3HK3" FT STRAND 596..602 FT /evidence="ECO:0007829|PDB:3HK3" FT HELIX 604..606 FT /evidence="ECO:0007829|PDB:3HK3" FT HELIX 607..617 FT /evidence="ECO:0007829|PDB:3HK3" SQ SEQUENCE 618 AA; 70269 MW; B89F719AAFD601E0 CRC64; MSHVRGLGLP GCLALAALVS LVHSQHVFLA PQQALSLLQR VRRANSGFLE ELRKGNLERE CVEEQCSYEE AFEALESPQD TDVFWAKYTV CDSVRKPRET FMDCLEGRCA MDLGVNYLGT VNVTHTGIQC QLWRSRYPHK PEINSTTHPG ADLKENFCRN PDSSTTGPWC YTTDPTVRRE ECSVPVCGQE GRTTVVMTPR SGGSKDNLSP PLGQCLTERG RLYQGNLAVT TLGSPCLPWN SLPAKTLSKY QDFDPEVKLV ENFCRNPDWD EEGAWCYVAG QPGDFEYCNL NYCEEAVGEE NYDVDESIAG RTTDAEFHTF FNEKTFGLGE ADCGLRPLFE KKSLKDTTEK ELLDSYIDGR IVEGWDAEKG IAPWQVMLFR KSPQELLCGA SLISDRWVLT AAHCILYPPW DKNFTENDLL VRIGKHSRTR YERNVEKISM LEKIYVHPRY NWRENLDRDI ALLKLKKPVP FSDYIHPVCL PDKQTVTSLL RAGYKGRVTG WGNLRETWTT NINEIQPSVL QVVNLPIVER PVCKASTRIR ITDNMFCAGF KVNDTKRGDA CEGDSGGPFV MKSPFNNRWY QMGIVSWGEG CDRKGKYGFY THVFRLKRWI QKVIDQFG //