ID BCAT1_HUMAN Reviewed; 386 AA. AC P54687; B3KY27; B7Z2M5; B7Z5L0; F5H5E4; Q68DQ7; Q96MY9; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 3. DT 16-OCT-2019, entry version 185. DE RecName: Full=Branched-chain-amino-acid aminotransferase, cytosolic; DE Short=BCAT(c); DE EC=2.6.1.42; DE AltName: Full=Protein ECA39; GN Name=BCAT1; Synonyms=BCT1, ECA39; 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; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT SER-330. RC TISSUE=Fetal brain; RX PubMed=8692959; DOI=10.1073/pnas.93.14.7143; RA Schuldiner O., Eden A., Ben-Yosef T., Yanuka O., Simchen G., RA Benvenisty N.; RT "ECA39, a conserved gene regulated by c-Myc in mice, is involved in RT G1/S cell cycle regulation in yeast."; RL Proc. Natl. Acad. Sci. U.S.A. 93:7143-7148(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 5). RC TISSUE=Brain, and Trachea; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Uterine endothelium; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., RA Kucherlapati R., Weinstock G., Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [5] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [7] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH GABAPENTIN. RX PubMed=16141215; DOI=10.1074/jbc.m506486200; RA Goto M., Miyahara I., Hirotsu K., Conway M., Yennawar N., Islam M.M., RA Hutson S.M.; RT "Structural determinants for branched-chain aminotransferase isozyme- RT specific inhibition by the anticonvulsant drug gabapentin."; RL J. Biol. Chem. 280:37246-37256(2005). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 21-386 IN COMPLEX WITH RP INHIBITOR. RX PubMed=16143519; DOI=10.1016/j.bmcl.2005.07.058; RA Hu L.Y., Boxer P.A., Kesten S.R., Lei H.J., Wustrow D.J., RA Moreland D.W., Zhang L., Ahn K., Ryder T.R., Liu X., Rubin J.R., RA Fahnoe K., Carroll R.T., Dutta S., Fahnoe D.C., Probert A.W., RA Roof R.L., Rafferty M.F., Kostlan C.R., Scholten J.D., Hood M., RA Ren X.D., Schielke G.P., Su T.Z., Taylor C.P., Mistry A., RA McConnell P., Hasemann C., Ohren J.; RT "The design and synthesis of human branched-chain amino acid RT aminotransferase inhibitors for treatment of neurodegenerative RT diseases."; RL Bioorg. Med. Chem. Lett. 16:2337-2340(2006). CC -!- FUNCTION: Catalyzes the first reaction in the catabolism of the CC essential branched chain amino acids leucine, isoleucine, and CC valine. CC -!- CATALYTIC ACTIVITY: CC Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + CC L-glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810, CC ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; CC EC=2.6.1.42; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2- CC oxopentanoate + L-glutamate; Xref=Rhea:RHEA:24801, CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, CC ChEBI:CHEBI:58045; EC=2.6.1.42; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L- CC glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851, CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; CC EC=2.6.1.42; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=P54687-1; Sequence=Displayed; CC Name=2; CC IsoId=P54687-2; Sequence=VSP_042651, VSP_042652; CC Note=No experimental confirmation available.; CC Name=3; CC IsoId=P54687-3; Sequence=VSP_042652; CC Note=No experimental confirmation available.; CC Name=4; CC IsoId=P54687-4; Sequence=VSP_043560; CC Note=No experimental confirmation available.; CC Name=5; CC IsoId=P54687-5; Sequence=VSP_046057; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: During embryogenesis, expressed in the brain CC and kidney. Overexpressed in MYC-induced tumors such as Burkitt's CC lymphoma. CC -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent CC aminotransferase family. {ECO:0000305}. 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; U21551; AAB08528.1; -; mRNA. DR EMBL; AK056255; BAB71129.1; -; mRNA. DR EMBL; AK128527; BAG54689.1; -; mRNA. DR EMBL; AK294879; BAH11911.1; -; mRNA. DR EMBL; AK299088; BAH12946.1; -; mRNA. DR EMBL; CR749308; CAH18163.1; -; mRNA. DR EMBL; AC023796; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC026310; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC092867; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR CCDS; CCDS44845.1; -. [P54687-1] DR CCDS; CCDS53760.1; -. [P54687-4] DR CCDS; CCDS53761.1; -. [P54687-5] DR CCDS; CCDS53762.1; -. [P54687-2] DR CCDS; CCDS53763.1; -. [P54687-3] DR RefSeq; NP_001171562.1; NM_001178091.1. [P54687-3] DR RefSeq; NP_001171563.1; NM_001178092.1. [P54687-2] DR RefSeq; NP_001171564.1; NM_001178093.1. [P54687-5] DR RefSeq; NP_001171565.1; NM_001178094.1. [P54687-4] DR RefSeq; NP_005495.2; NM_005504.6. [P54687-1] DR PDB; 2ABJ; X-ray; 2.20 A; A/D/G/J=21-386. DR PDB; 2COG; X-ray; 2.10 A; A/B=1-386. DR PDB; 2COI; X-ray; 1.90 A; A/B=1-386. DR PDB; 2COJ; X-ray; 2.40 A; A/B=1-386. DR PDBsum; 2ABJ; -. DR PDBsum; 2COG; -. DR PDBsum; 2COI; -. DR PDBsum; 2COJ; -. DR SMR; P54687; -. DR BioGrid; 107061; 41. DR IntAct; P54687; 23. DR MINT; P54687; -. DR STRING; 9606.ENSP00000443459; -. DR BindingDB; P54687; -. DR ChEMBL; CHEMBL4679; -. DR DrugBank; DB00996; Gabapentin. DR DrugBank; DB00142; Glutamic Acid. DR DrugBank; DB00167; Isoleucine. DR DrugBank; DB00149; L-Leucine. DR DrugBank; DB00161; L-Valine. DR DrugBank; DB07544; N'-(5-CHLOROBENZOFURAN-2-CARBONYL)-2-(TRIFLUOROMETHYL)BENZENESULFONOHYDRAZIDE. DR DrugBank; DB00114; Pyridoxal phosphate. DR iPTMnet; P54687; -. DR PhosphoSitePlus; P54687; -. DR SwissPalm; P54687; -. DR BioMuta; BCAT1; -. DR DMDM; 215274162; -. DR EPD; P54687; -. DR jPOST; P54687; -. DR MassIVE; P54687; -. DR MaxQB; P54687; -. DR PaxDb; P54687; -. DR PeptideAtlas; P54687; -. DR PRIDE; P54687; -. DR ProteomicsDB; 26852; -. DR ProteomicsDB; 56691; -. [P54687-1] DR ProteomicsDB; 56692; -. [P54687-2] DR ProteomicsDB; 56693; -. [P54687-3] DR ProteomicsDB; 56694; -. [P54687-4] DR Ensembl; ENST00000261192; ENSP00000261192; ENSG00000060982. [P54687-1] DR Ensembl; ENST00000342945; ENSP00000339805; ENSG00000060982. [P54687-2] DR Ensembl; ENST00000538118; ENSP00000440817; ENSG00000060982. [P54687-4] DR Ensembl; ENST00000539282; ENSP00000443459; ENSG00000060982. [P54687-5] DR Ensembl; ENST00000539780; ENSP00000440827; ENSG00000060982. [P54687-3] DR GeneID; 586; -. DR KEGG; hsa:586; -. DR UCSC; uc001rgc.4; human. [P54687-1] DR CTD; 586; -. DR DisGeNET; 586; -. DR GeneCards; BCAT1; -. DR HGNC; HGNC:976; BCAT1. DR HPA; HPA048592; -. DR MIM; 113520; gene. DR neXtProt; NX_P54687; -. DR OpenTargets; ENSG00000060982; -. DR PharmGKB; PA25288; -. DR eggNOG; KOG0975; Eukaryota. DR eggNOG; COG0115; LUCA. DR GeneTree; ENSGT00390000009532; -. DR HOGENOM; HOG000276704; -. DR InParanoid; P54687; -. DR KO; K00826; -. DR OMA; LTEVFAC; -. DR OrthoDB; 853728at2759; -. DR PhylomeDB; P54687; -. DR TreeFam; TF300882; -. DR BRENDA; 2.6.1.42; 2681. DR Reactome; R-HSA-70895; Branched-chain amino acid catabolism. DR SABIO-RK; P54687; -. DR ChiTaRS; BCAT1; human. DR EvolutionaryTrace; P54687; -. DR GenomeRNAi; 586; -. DR Pharos; P54687; -. DR PRO; PR:P54687; -. DR Proteomes; UP000005640; Chromosome 12. DR Bgee; ENSG00000060982; Expressed in 195 organ(s), highest expression level in visceral pleura. DR ExpressionAtlas; P54687; baseline and differential. DR Genevisible; P54687; HS. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central. DR GO; GO:0004084; F:branched-chain-amino-acid transaminase activity; IBA:GO_Central. DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl. DR GO; GO:0052656; F:L-isoleucine transaminase activity; IEA:UniProtKB-EC. DR GO; GO:0052654; F:L-leucine transaminase activity; IEA:UniProtKB-EC. DR GO; GO:0052655; F:L-valine transaminase activity; IEA:UniProtKB-EC. DR GO; GO:0009082; P:branched-chain amino acid biosynthetic process; TAS:ProtInc. DR GO; GO:0009083; P:branched-chain amino acid catabolic process; TAS:Reactome. DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:ProtInc. DR GO; GO:0009098; P:leucine biosynthetic process; IBA:GO_Central. DR GO; GO:0009099; P:valine biosynthetic process; IBA:GO_Central. DR CDD; cd01557; BCAT_beta_family; 1. DR InterPro; IPR001544; Aminotrans_IV. DR InterPro; IPR018300; Aminotrans_IV_CS. DR InterPro; IPR036038; Aminotransferase-like. DR InterPro; IPR005786; B_amino_transII. DR InterPro; IPR033939; BCAT_family. DR Pfam; PF01063; Aminotran_4; 1. DR PIRSF; PIRSF006468; BCAT1; 1. DR SUPFAM; SSF56752; SSF56752; 1. DR TIGRFAMs; TIGR01123; ilvE_II; 1. DR PROSITE; PS00770; AA_TRANSFER_CLASS_4; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; KW Amino-acid biosynthesis; Aminotransferase; KW Branched-chain amino acid biosynthesis; Complete proteome; Cytoplasm; KW Polymorphism; Pyridoxal phosphate; Reference proteome; Transferase. FT CHAIN 1 386 Branched-chain-amino-acid FT aminotransferase, cytosolic. FT /FTId=PRO_0000103292. FT MOD_RES 1 1 N-acetylmethionine. FT {ECO:0000244|PubMed:19413330}. FT MOD_RES 222 222 N6-(pyridoxal phosphate)lysine. FT {ECO:0000250}. FT VAR_SEQ 1 25 MKDCSNGCSAECTGEGGSKEVVGTF -> M (in FT isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_042651. FT VAR_SEQ 1 2 MK -> M (in isoform 4). FT {ECO:0000303|PubMed:17974005}. FT /FTId=VSP_043560. FT VAR_SEQ 1 2 MK -> MASPLRSAAALARQ (in isoform 5). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_046057. FT VAR_SEQ 94 130 Missing (in isoform 2 and isoform 3). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_042652. FT VARIANT 59 59 T -> M (in dbSNP:rs17374285). FT /FTId=VAR_047681. FT VARIANT 321 321 E -> K (in dbSNP:rs7313020). FT /FTId=VAR_019614. FT VARIANT 330 330 G -> S (in dbSNP:rs1057204). FT {ECO:0000269|PubMed:8692959}. FT /FTId=VAR_047682. FT CONFLICT 2 2 Missing (in Ref. 1; AAB08528). FT {ECO:0000305}. FT CONFLICT 8 8 Missing (in Ref. 1; AAB08528). FT {ECO:0000305}. FT CONFLICT 165 165 T -> A (in Ref. 1; AAB08528). FT {ECO:0000305}. FT CONFLICT 237 237 A -> D (in Ref. 1; AAB08528). FT {ECO:0000305}. FT CONFLICT 251 251 E -> R (in Ref. 1; AAB08528). FT {ECO:0000305}. FT CONFLICT 300 300 Q -> P (in Ref. 2; BAH11911). FT {ECO:0000305}. FT CONFLICT 317 317 T -> S (in Ref. 2; BAB71129). FT {ECO:0000305}. FT HELIX 27 29 {ECO:0000244|PDB:2COI}. FT HELIX 44 46 {ECO:0000244|PDB:2ABJ}. FT TURN 49 51 {ECO:0000244|PDB:2COG}. FT STRAND 55 63 {ECO:0000244|PDB:2COI}. FT TURN 64 66 {ECO:0000244|PDB:2COI}. FT STRAND 72 75 {ECO:0000244|PDB:2COI}. FT STRAND 79 81 {ECO:0000244|PDB:2COI}. FT HELIX 86 89 {ECO:0000244|PDB:2COI}. FT STRAND 93 95 {ECO:0000244|PDB:2COI}. FT STRAND 98 102 {ECO:0000244|PDB:2COI}. FT STRAND 108 112 {ECO:0000244|PDB:2COI}. FT HELIX 113 126 {ECO:0000244|PDB:2COI}. FT HELIX 134 147 {ECO:0000244|PDB:2COI}. FT HELIX 149 151 {ECO:0000244|PDB:2COI}. FT STRAND 154 157 {ECO:0000244|PDB:2COI}. FT STRAND 159 168 {ECO:0000244|PDB:2COI}. FT STRAND 179 190 {ECO:0000244|PDB:2COI}. FT STRAND 202 206 {ECO:0000244|PDB:2COI}. FT HELIX 225 228 {ECO:0000244|PDB:2COI}. FT HELIX 231 238 {ECO:0000244|PDB:2COI}. FT TURN 239 241 {ECO:0000244|PDB:2COI}. FT STRAND 243 249 {ECO:0000244|PDB:2COI}. FT TURN 250 253 {ECO:0000244|PDB:2COI}. FT STRAND 254 258 {ECO:0000244|PDB:2COI}. FT STRAND 261 268 {ECO:0000244|PDB:2COI}. FT STRAND 274 278 {ECO:0000244|PDB:2COI}. FT STRAND 282 285 {ECO:0000244|PDB:2COI}. FT HELIX 289 301 {ECO:0000244|PDB:2COI}. FT STRAND 303 308 {ECO:0000244|PDB:2COI}. FT HELIX 313 320 {ECO:0000244|PDB:2COI}. FT TURN 321 323 {ECO:0000244|PDB:2COI}. FT STRAND 325 332 {ECO:0000244|PDB:2COI}. FT TURN 333 335 {ECO:0000244|PDB:2COI}. FT STRAND 336 351 {ECO:0000244|PDB:2COI}. FT HELIX 353 357 {ECO:0000244|PDB:2COI}. FT HELIX 360 373 {ECO:0000244|PDB:2COI}. FT STRAND 382 384 {ECO:0000244|PDB:2COI}. SQ SEQUENCE 386 AA; 42966 MW; A43535303A702512 CRC64; MKDCSNGCSA ECTGEGGSKE VVGTFKAKDL IVTPATILKE KPDPNNLVFG TVFTDHMLTV EWSSEFGWEK PHIKPLQNLS LHPGSSALHY AVELFEGLKA FRGVDNKIRL FQPNLNMDRM YRSAVRATLP VFDKEELLEC IQQLVKLDQE WVPYSTSASL YIRPTFIGTE PSLGVKKPTK ALLFVLLSPV GPYFSSGTFN PVSLWANPKY VRAWKGGTGD CKMGGNYGSS LFAQCEAVDN GCQQVLWLYG EDHQITEVGT MNLFLYWINE DGEEELATPP LDGIILPGVT RRCILDLAHQ WGEFKVSERY LTMDDLTTAL EGNRVREMFG SGTACVVCPV SDILYKGETI HIPTMENGPK LASRILSKLT DIQYGREESD WTIVLS //