THRB_BOVIN
ID THRB_BOVIN Reviewed; 625 AA.
AC P00735; Q3MHK7;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 2.
DT 03-AUG-2022, entry version 225.
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;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3379642; DOI=10.1016/0022-2836(88)90331-2;
RA Irwin D.M., Robertson K.A., Macgillivray R.T.A.;
RT "Structure and evolution of the bovine prothrombin gene.";
RL J. Mol. Biol. 200:31-45(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6326805; DOI=10.1021/bi00303a007;
RA McGillivray R.T.A., Davie E.W.;
RT "Characterization of bovine prothrombin mRNA and its translation product.";
RL Biochemistry 23:1626-1634(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 44-625, DISULFIDE BONDS, GAMMA-CARBOXYGLUTAMATION AT
RP GLU-50; GLU-51; GLU-58; GLU-60; GLU-63; GLU-64; GLU-69; GLU-70; GLU-73 AND
RP GLU-76, AND GLYCOSYLATION AT ASN-120; ASN-144 AND ASN-419.
RA Magnusson S., Sottrup-Jensen L., Petersen T.E., Claeys H.;
RL (In) Hemker H.C., Veltkamp J.J. (eds.);
RL Boerhaave symposium on prothrombin and related coagulation factors,
RL pp.25-46, Leiden University Press, Leiden (1975).
RN [5]
RP GENE STRUCTURE.
RX PubMed=3000440; DOI=10.1021/bi00345a018;
RA Irwin D.M., Ahern K.G., Pearson G.D., McGillivray R.T.A.;
RT "Characterization of the bovine prothrombin gene.";
RL Biochemistry 24:6854-6861(1985).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF ACTIVATION PEPTIDE 1.
RX PubMed=3741841; DOI=10.1021/bi00362a001;
RA Park C.H., Tulinsky A.;
RT "Three-dimensional structure of the kringle sequence: structure of
RT prothrombin fragment 1.";
RL Biochemistry 25:3977-3982(1986).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF ACTIVATION PEPTIDE 1.
RX PubMed=1856869; DOI=10.1016/0022-2836(91)90025-2;
RA Seshadri T.-P., Tulinsky A., Skrzypczak-Jankun E., Park C.H.;
RT "Structure of bovine prothrombin fragment 1 refined at 2.25-A resolution.";
RL J. Mol. Biol. 220:481-494(1991).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF ACTIVATION PEPTIDE 1 IN COMPLEX
RP WITH CALCIUM IONS, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-120 AND
RP ASN-144.
RX PubMed=1547238; DOI=10.1021/bi00124a016;
RA Soriano-Garcia M., Padmanabhan K., de Vos A.M., Tulinsky A.;
RT "The Ca2+ ion and membrane binding structure of the Gla domain of Ca-
RT prothrombin fragment 1.";
RL Biochemistry 31:2554-2566(1992).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH FIBRINOGEN.
RX PubMed=1560020; DOI=10.1016/s0021-9258(18)42599-9;
RA Martin P.D., Robertson W., Turk D., Huber R., Bode W., Edwards B.F.P.;
RT "The structure of residues 7-16 of the A alpha-chain of human fibrinogen
RT bound to bovine thrombin at 2.3-A resolution.";
RL J. Biol. Chem. 267:7911-7920(1992).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 318-625 IN COMPLEX WITH HIRUDIN.
RX PubMed=1517214; DOI=10.1016/s0021-9258(19)37095-4;
RA Vitali J., Martin P.D., Malkowski M.G., Robertson W.D., Lazar J.B.,
RA Winant R.C., Johnson P.H., Edwards B.F.P.;
RT "The structure of a complex of bovine alpha-thrombin and recombinant
RT hirudin at 2.8-A resolution.";
RL J. Biol. Chem. 267:17670-17678(1992).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=1518046; DOI=10.1016/0022-2836(92)91054-s;
RA Brandstetter H., Turk D., Hoeffken H.W., Grosse D., Stuerzebecher J.,
RA Martin P.D., Edwards B.F.P., Bode W.;
RT "Refined 2.3 A X-ray crystal structure of bovine thrombin complexes formed
RT with the benzamidine and arginine-based thrombin inhibitors NAPAP, 4-TAPAP
RT and MQPA. A starting point for improving antithrombotics.";
RL J. Mol. Biol. 226:1085-1099(1992).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF COMPLEX WITH ORNITHODORIN.
RX PubMed=8947023;
RA van de Locht A., Stubbs M.T., Bode W., Friedrich T., Bollschweiler C.,
RA Hoffken W., Huber R.;
RT "The ornithodorin-thrombin crystal structure, a key to the TAP enigma?";
RL EMBO J. 15:6011-6017(1996).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF COMPLEX WITH TRIABIN.
RX PubMed=9342325; DOI=10.1073/pnas.94.22.11845;
RA Fuentes-Prior P., Noeske-Jungblut C., Donner P., Schleuning W.-D.,
RA Huber R., Bode W.;
RT "Structure of the thrombin complex with triabin, a lipocalin-like exosite-
RT binding inhibitor derived from a triatomine bug.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:11845-11850(1997).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 44-190 IN COMPLEX WITH CALCIUM AND
RP LYSOPHOSPHATIDYLSERINE.
RX PubMed=12923575; DOI=10.1038/nsb971;
RA Huang M., Rigby A.C., Morelli X., Grant M.A., Huang G., Furie B.,
RA Seaton B., Furie B.C.;
RT "Structural basis of membrane binding by Gla domains of vitamin K-dependent
RT proteins.";
RL Nat. Struct. Biol. 10:751-756(2003).
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 -!- INTERACTION:
CC P00735; Q4W8J9: coa; Xeno; NbExp=2; IntAct=EBI-990806, EBI-990838;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
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|Ref.4}.
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; V00135; CAA23451.1; -; mRNA.
DR EMBL; J00041; AAA30781.1; -; mRNA.
DR EMBL; BC105201; AAI05202.1; -; mRNA.
DR PIR; S02537; TBBO.
DR RefSeq; NP_776302.1; NM_173877.1.
DR RefSeq; XP_015330343.1; XM_015474857.1.
DR PDB; 1A0H; X-ray; 3.20 A; A/D=208-366, B/E=367-625.
DR PDB; 1AVG; X-ray; 2.60 A; H=367-625, L=326-366.
DR PDB; 1BBR; X-ray; 2.30 A; E=517-625, H=367-515, J/L/M=318-366, K/N=367-625.
DR PDB; 1ETR; X-ray; 2.20 A; H=367-625, L=318-366.
DR PDB; 1ETS; X-ray; 2.30 A; H=367-625, L=318-366.
DR PDB; 1ETT; X-ray; 2.50 A; H=367-625, L=318-366.
DR PDB; 1HRT; X-ray; 2.80 A; H=367-625, L=318-366.
DR PDB; 1ID5; X-ray; 2.50 A; H=367-622, L=318-366.
DR PDB; 1MKW; X-ray; 2.30 A; H=367-625, K=318-625, L=318-366.
DR PDB; 1MKX; X-ray; 2.20 A; H=367-625, K=318-625, L=318-366.
DR PDB; 1NL1; X-ray; 1.90 A; A=44-190.
DR PDB; 1NL2; X-ray; 2.30 A; A=44-189.
DR PDB; 1TBQ; X-ray; 3.10 A; H/K=367-625, J/L=318-366.
DR PDB; 1TBR; X-ray; 2.60 A; H/K=367-625, J/L=318-366.
DR PDB; 1TOC; X-ray; 3.10 A; A/C/E/G=318-366, B/D/F/H=367-625.
DR PDB; 1UCY; X-ray; 2.20 A; E=517-625, H=367-516, J/L/M=318-366, K/N=367-625.
DR PDB; 1UVT; X-ray; 2.50 A; H=367-625, L=318-366.
DR PDB; 1UVU; X-ray; 2.80 A; H=367-625, L=318-366.
DR PDB; 1VIT; X-ray; 3.20 A; F=367-516, G=517-625, H=367-625, L/M=318-366.
DR PDB; 1YCP; X-ray; 2.50 A; H=367-625, J/L=318-366, K=367-516, M=517-625.
DR PDB; 2A1D; X-ray; 3.50 A; A/E=326-366, B/F=367-625.
DR PDB; 2HPP; X-ray; 3.30 A; P=214-292.
DR PDB; 2ODY; X-ray; 2.35 A; A/C=318-366, B/D=367-625.
DR PDB; 2PF1; X-ray; 2.80 A; A=44-199.
DR PDB; 2PF2; X-ray; 2.20 A; A=44-199.
DR PDB; 2SPT; X-ray; 2.50 A; A=44-188.
DR PDB; 3PMA; X-ray; 2.20 A; A/C=336-364, B/D=367-625.
DR PDB; 3PMB; X-ray; 2.90 A; A/C=336-364, B/D=367-625.
DR PDBsum; 1A0H; -.
DR PDBsum; 1AVG; -.
DR PDBsum; 1BBR; -.
DR PDBsum; 1ETR; -.
DR PDBsum; 1ETS; -.
DR PDBsum; 1ETT; -.
DR PDBsum; 1HRT; -.
DR PDBsum; 1ID5; -.
DR PDBsum; 1MKW; -.
DR PDBsum; 1MKX; -.
DR PDBsum; 1NL1; -.
DR PDBsum; 1NL2; -.
DR PDBsum; 1TBQ; -.
DR PDBsum; 1TBR; -.
DR PDBsum; 1TOC; -.
DR PDBsum; 1UCY; -.
DR PDBsum; 1UVT; -.
DR PDBsum; 1UVU; -.
DR PDBsum; 1VIT; -.
DR PDBsum; 1YCP; -.
DR PDBsum; 2A1D; -.
DR PDBsum; 2HPP; -.
DR PDBsum; 2ODY; -.
DR PDBsum; 2PF1; -.
DR PDBsum; 2PF2; -.
DR PDBsum; 2SPT; -.
DR PDBsum; 3PMA; -.
DR PDBsum; 3PMB; -.
DR AlphaFoldDB; P00735; -.
DR SMR; P00735; -.
DR DIP; DIP-6099N; -.
DR IntAct; P00735; 2.
DR STRING; 9913.ENSBTAP00000009406; -.
DR BindingDB; P00735; -.
DR ChEMBL; CHEMBL4471; -.
DR DrugCentral; P00735; -.
DR Allergome; 1245; Bos d Thrombin.
DR MEROPS; S01.217; -.
DR GlyConnect; 517; 3 N-Linked glycans.
DR iPTMnet; P00735; -.
DR PaxDb; P00735; -.
DR PeptideAtlas; P00735; -.
DR PRIDE; P00735; -.
DR GeneID; 280685; -.
DR KEGG; bta:280685; -.
DR CTD; 2147; -.
DR eggNOG; ENOG502QTSX; Eukaryota.
DR HOGENOM; CLU_006842_19_4_1; -.
DR InParanoid; P00735; -.
DR OrthoDB; 1314811at2759; -.
DR TreeFam; TF327329; -.
DR BRENDA; 3.4.21.5; 908.
DR SABIO-RK; P00735; -.
DR EvolutionaryTrace; P00735; -.
DR PRO; PR:P00735; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0070051; F:fibrinogen binding; IPI:BHF-UCL.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:BHF-UCL.
DR GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR GO; GO:0030168; P:platelet activation; IBA:GO_Central.
DR GO; GO:0030194; P:positive regulation of blood coagulation; IDA:BHF-UCL.
DR GO; GO:0051258; P:protein polymerization; IDA:BHF-UCL.
DR GO; GO:0006508; P:proteolysis; IDA:BHF-UCL.
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; Direct protein sequencing;
KW Disulfide bond; Gamma-carboxyglutamic acid; Glycoprotein; Hemostasis;
KW Hydrolase; Kringle; Protease; Reference proteome; Repeat; Secreted;
KW Serine protease; Signal; Zymogen.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..43
FT /evidence="ECO:0000269|Ref.4"
FT /id="PRO_0000028153"
FT CHAIN 44..625
FT /note="Prothrombin"
FT /id="PRO_0000028154"
FT PEPTIDE 44..199
FT /note="Activation peptide fragment 1"
FT /id="PRO_0000028155"
FT PEPTIDE 200..317
FT /note="Activation peptide fragment 2"
FT /id="PRO_0000028156"
FT CHAIN 318..366
FT /note="Thrombin light chain"
FT /id="PRO_0000028157"
FT CHAIN 367..625
FT /note="Thrombin heavy chain"
FT /id="PRO_0000028158"
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 214..292
FT /note="Kringle 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 367..621
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 554..576
FT /note="High affinity receptor-binding region which is also
FT known as the TP508 peptide"
FT /evidence="ECO:0000250"
FT ACT_SITE 409
FT /note="Charge relay system"
FT ACT_SITE 465
FT /note="Charge relay system"
FT ACT_SITE 571
FT /note="Charge relay system"
FT SITE 199..200
FT /note="Cleavage; by thrombin"
FT SITE 317..318
FT /note="Cleavage; by factor Xa"
FT SITE 366..367
FT /note="Cleavage; by factor Xa"
FT MOD_RES 50
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|Ref.4"
FT MOD_RES 51
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|Ref.4"
FT MOD_RES 58
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|Ref.4"
FT MOD_RES 60
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|Ref.4"
FT MOD_RES 63
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|Ref.4"
FT MOD_RES 64
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|Ref.4"
FT MOD_RES 69
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|Ref.4"
FT MOD_RES 70
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|Ref.4"
FT MOD_RES 73
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|Ref.4"
FT MOD_RES 76
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|Ref.4"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1547238, ECO:0000269|Ref.4"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1547238, ECO:0000269|Ref.4"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|Ref.4"
FT DISULFID 61..66
FT DISULFID 91..104
FT DISULFID 109..187
FT DISULFID 130..170
FT DISULFID 158..182
FT DISULFID 214..292
FT DISULFID 235..275
FT DISULFID 263..287
FT DISULFID 339..485
FT /note="Interchain (between light and heavy chains)"
FT DISULFID 394..410
FT DISULFID 539..553
FT DISULFID 567..597
FT VARIANT 600
FT /note="D -> N"
FT CONFLICT 231
FT /note="S -> H (in Ref. 2; AAA30781)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="D -> H (in Ref. 2; AAA30781)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="D -> N (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 353
FT /note="Q -> E (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="E -> Q (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="L -> P (in Ref. 3; AAI05202)"
FT /evidence="ECO:0000305"
FT CONFLICT 549..550
FT /note="DN -> ND (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:1NL1"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:1NL1"
FT HELIX 57..61
FT /evidence="ECO:0007829|PDB:1NL1"
FT HELIX 68..74
FT /evidence="ECO:0007829|PDB:1NL1"
FT HELIX 78..90
FT /evidence="ECO:0007829|PDB:1NL1"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:1NL1"
FT HELIX 98..106
FT /evidence="ECO:0007829|PDB:1NL1"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:1NL1"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:2PF2"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:2PF2"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:1NL1"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:1NL1"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:2PF1"
FT STRAND 168..174
FT /evidence="ECO:0007829|PDB:1NL1"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:1NL1"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:2PF1"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:2PF1"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:1A0H"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:1A0H"
FT HELIX 243..246
FT /evidence="ECO:0007829|PDB:1A0H"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:2HPP"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:2HPP"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:1A0H"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:1A0H"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:1A0H"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:1A0H"
FT STRAND 310..313
FT /evidence="ECO:0007829|PDB:1A0H"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:1A0H"
FT HELIX 329..332
FT /evidence="ECO:0007829|PDB:2ODY"
FT TURN 337..340
FT /evidence="ECO:0007829|PDB:1ETR"
FT TURN 343..345
FT /evidence="ECO:0007829|PDB:1ETR"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:1ETR"
FT HELIX 355..362
FT /evidence="ECO:0007829|PDB:1ETR"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:1MKX"
FT STRAND 375..377
FT /evidence="ECO:0007829|PDB:2A1D"
FT STRAND 381..386
FT /evidence="ECO:0007829|PDB:1ETR"
FT TURN 387..390
FT /evidence="ECO:0007829|PDB:1ETR"
FT STRAND 391..400
FT /evidence="ECO:0007829|PDB:1ETR"
FT STRAND 403..406
FT /evidence="ECO:0007829|PDB:1ETR"
FT HELIX 408..410
FT /evidence="ECO:0007829|PDB:1ETR"
FT HELIX 414..416
FT /evidence="ECO:0007829|PDB:1ETR"
FT STRAND 424..430
FT /evidence="ECO:0007829|PDB:1ETR"
FT STRAND 433..436
FT /evidence="ECO:0007829|PDB:1ETR"
FT TURN 439..441
FT /evidence="ECO:0007829|PDB:1ETR"
FT STRAND 443..445
FT /evidence="ECO:0007829|PDB:1ETR"
FT STRAND 447..452
FT /evidence="ECO:0007829|PDB:1ETR"
FT TURN 458..461
FT /evidence="ECO:0007829|PDB:1ETR"
FT STRAND 467..473
FT /evidence="ECO:0007829|PDB:1ETR"
FT HELIX 489..495
FT /evidence="ECO:0007829|PDB:1ETR"
FT STRAND 501..506
FT /evidence="ECO:0007829|PDB:1ETR"
FT STRAND 510..513
FT /evidence="ECO:0007829|PDB:1UCY"
FT STRAND 516..518
FT /evidence="ECO:0007829|PDB:1ETR"
FT STRAND 520..522
FT /evidence="ECO:0007829|PDB:1UCY"
FT STRAND 527..533
FT /evidence="ECO:0007829|PDB:1ETR"
FT HELIX 536..541
FT /evidence="ECO:0007829|PDB:1ETR"
FT STRAND 543..545
FT /evidence="ECO:0007829|PDB:1ETT"
FT STRAND 551..554
FT /evidence="ECO:0007829|PDB:1ETR"
FT HELIX 558..560
FT /evidence="ECO:0007829|PDB:1ETR"
FT TURN 568..572
FT /evidence="ECO:0007829|PDB:1ETR"
FT STRAND 574..578
FT /evidence="ECO:0007829|PDB:1ETR"
FT TURN 580..582
FT /evidence="ECO:0007829|PDB:1ETR"
FT STRAND 585..591
FT /evidence="ECO:0007829|PDB:1ETR"
FT STRAND 595..598
FT /evidence="ECO:0007829|PDB:1ETR"
FT STRAND 604..608
FT /evidence="ECO:0007829|PDB:1ETR"
FT TURN 609..612
FT /evidence="ECO:0007829|PDB:1ETR"
FT HELIX 613..621
FT /evidence="ECO:0007829|PDB:1ETR"
SQ SEQUENCE 625 AA; 70506 MW; 95AFF17C23AD78F9 CRC64;
MARVRGPRLP GCLALAALFS LVHSQHVFLA HQQASSLLQR ARRANKGFLE EVRKGNLERE
CLEEPCSREE AFEALESLSA TDAFWAKYTA CESARNPREK LNECLEGNCA EGVGMNYRGN
VSVTRSGIEC QLWRSRYPHK PEINSTTHPG ADLRENFCRN PDGSITGPWC YTTSPTLRRE
ECSVPVCGQD RVTVEVIPRS GGSTTSQSPL LETCVPDRGR EYRGRLAVTT SGSRCLAWSS
EQAKALSKDQ DFNPAVPLAE NFCRNPDGDE EGAWCYVADQ PGDFEYCDLN YCEEPVDGDL
GDRLGEDPDP DAAIEGRTSE DHFQPFFNEK TFGAGEADCG LRPLFEKKQV QDQTEKELFE
SYIEGRIVEG QDAEVGLSPW QVMLFRKSPQ ELLCGASLIS DRWVLTAAHC LLYPPWDKNF
TVDDLLVRIG KHSRTRYERK VEKISMLDKI YIHPRYNWKE NLDRDIALLK LKRPIELSDY
IHPVCLPDKQ TAAKLLHAGF KGRVTGWGNR RETWTTSVAE VQPSVLQVVN LPLVERPVCK
ASTRIRITDN MFCAGYKPGE GKRGDACEGD SGGPFVMKSP YNNRWYQMGI VSWGEGCDRD
GKYGFYTHVF RLKKWIQKVI DRLGS
