THRB_MOUSE
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 03-AUG-2022, entry version 215.
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, Spleen,
RC 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 -!- MISCELLANEOUS: Prothrombin is activated on the surface of a
CC phospholipid membrane that binds the amino end of prothrombin and
CC factors Va and Xa in Ca-dependent interactions; factor Xa removes the
CC activation peptide and cleaves the remaining part into light and heavy
CC chains. The activation process starts slowly because factor V itself
CC has to be activated by the initial, small amounts of thrombin.
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}.
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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; 5.
DR MINT; P19221; -.
DR STRING; 10090.ENSMUSP00000028681; -.
DR BindingDB; P19221; -.
DR ChEMBL; CHEMBL1075308; -.
DR MEROPS; S01.217; -.
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; P19221; -.
DR PeptideAtlas; P19221; -.
DR PRIDE; P19221; -.
DR ProteomicsDB; 259185; -.
DR Antibodypedia; 857; 1137 antibodies from 42 providers.
DR DNASU; 14061; -.
DR Ensembl; ENSMUST00000028681; ENSMUSP00000028681; ENSMUSG00000027249.
DR GeneID; 14061; -.
DR KEGG; mmu:14061; -.
DR UCSC; uc008kwg.2; mouse.
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; YCEEPVD; -.
DR OrthoDB; 1314811at2759; -.
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 60 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 52 other tissues.
DR ExpressionAtlas; P19221; baseline and differential.
DR Genevisible; P19221; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:1905370; C:serine-type endopeptidase complex; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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:0007596; P:blood coagulation; ISO:MGI.
DR GO; GO:0072377; P:blood coagulation, common pathway; 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: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:0090218; P:positive regulation of lipid kinase activity; ISO:MGI.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; 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; ISO:MGI.
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 GO; GO:0031638; P:zymogen activation; ISO:MGI.
DR CDD; cd00108; KR; 2.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
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; 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:SF10; PTHR24254:SF10; 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; 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 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 325..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 324..325
FT /note="Cleavage; by factor Xa"
FT SITE 360..361
FT /note="Cleavage; by factor Xa"
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
