HIBCH_HUMAN
ID HIBCH_HUMAN Reviewed; 386 AA.
AC Q6NVY1; D3DPI4; Q53GA8; Q53GF2; Q53RF7; Q53TC6; Q92931; Q9BS94;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=3-hydroxyisobutyryl-CoA hydrolase, mitochondrial;
DE EC=3.1.2.4;
DE AltName: Full=3-hydroxyisobutyryl-coenzyme A hydrolase;
DE Short=HIB-CoA hydrolase;
DE Short=HIBYL-CoA-H;
DE Flags: Precursor;
GN Name=HIBCH;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=8824301; DOI=10.1074/jbc.271.42.26430;
RA Hawes J.W., Jaskiewicz J., Shimomura Y., Huang B., Bunting J., Harper E.T.,
RA Harris R.A.;
RT "Primary structure and tissue-specific expression of human beta-
RT hydroxyisobutyryl-coenzyme A hydrolase.";
RL J. Biol. Chem. 271:26430-26434(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-46.
RC TISSUE=Small intestine;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-46.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-46.
RC TISSUE=Testis;
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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-92, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [7]
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., Buerckstuemmer T.,
RA 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234 AND SER-356, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 32-386 IN COMPLEX WITH
RP 3-HYDROXY-2-METHYLPROPANOIC ACID AND QUERCETIN.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human beta-hydroxyisobutyryl-COA hydrolase in complex
RT with quercetin.";
RL Submitted (JAN-2008) to the PDB data bank.
RN [12]
RP VARIANT HIBCHD CYS-122.
RX PubMed=17160907; DOI=10.1086/510725;
RA Loupatty F.J., Clayton P.T., Ruiter J.P.N., Ofman R., Ijlst L., Brown G.K.,
RA Thorburn D.R., Harris R.A., Duran M., Desousa C., Krywawych S.,
RA Heales S.J.R., Wanders R.J.A.;
RT "Mutations in the gene encoding 3-hydroxyisobutyryl-CoA hydrolase results
RT in progressive infantile neurodegeneration.";
RL Am. J. Hum. Genet. 80:195-199(2007).
CC -!- FUNCTION: Hydrolyzes 3-hydroxyisobutyryl-CoA (HIBYL-CoA), a saline
CC catabolite. Has high activity toward isobutyryl-CoA. Could be an
CC isobutyryl-CoA dehydrogenase that functions in valine catabolism. Also
CC hydrolyzes 3-hydroxypropanoyl-CoA. {ECO:0000269|PubMed:8824301}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxy-2-methylpropanoyl-CoA + H2O = 3-hydroxy-2-
CC methylpropanoate + CoA + H(+); Xref=Rhea:RHEA:20888,
CC ChEBI:CHEBI:11805, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57340; EC=3.1.2.4;
CC Evidence={ECO:0000269|PubMed:8824301};
CC -!- PATHWAY: Amino-acid degradation; L-valine degradation.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6NVY1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6NVY1-2; Sequence=VSP_024780;
CC -!- TISSUE SPECIFICITY: Highly expressed in liver and kidney, also detected
CC in heart, muscle and brain (at protein level). Not detected in lung.
CC {ECO:0000269|PubMed:8824301}.
CC -!- DISEASE: 3-hydroxyisobutryl-CoA hydrolase deficiency (HIBCHD)
CC [MIM:250620]: An autosomal recessive inborn error of valine metabolism.
CC It causes severely delayed psychomotor development, neurodegeneration,
CC increased lactic acid, and brain lesions in the basal ganglia.
CC {ECO:0000269|PubMed:17160907}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC52114.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH05190.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAY24178.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAD96699.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAD96743.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U66669; AAC52114.1; ALT_INIT; mRNA.
DR EMBL; AK222979; BAD96699.1; ALT_INIT; mRNA.
DR EMBL; AK223023; BAD96743.1; ALT_INIT; mRNA.
DR EMBL; AC092178; AAY24178.1; ALT_INIT; Genomic_DNA.
DR EMBL; AC010679; AAX93234.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX10873.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX10875.1; -; Genomic_DNA.
DR EMBL; BC005190; AAH05190.2; ALT_INIT; mRNA.
DR EMBL; BC067822; AAH67822.1; -; mRNA.
DR CCDS; CCDS2304.1; -. [Q6NVY1-1]
DR CCDS; CCDS46475.1; -. [Q6NVY1-2]
DR RefSeq; NP_055177.2; NM_014362.3. [Q6NVY1-1]
DR RefSeq; NP_932164.1; NM_198047.2. [Q6NVY1-2]
DR RefSeq; XP_011509255.1; XM_011510953.1. [Q6NVY1-1]
DR PDB; 3BPT; X-ray; 1.50 A; A=32-386.
DR PDBsum; 3BPT; -.
DR AlphaFoldDB; Q6NVY1; -.
DR SMR; Q6NVY1; -.
DR BioGRID; 117658; 78.
DR IntAct; Q6NVY1; 12.
DR STRING; 9606.ENSP00000352706; -.
DR ChEMBL; CHEMBL3817723; -.
DR DrugBank; DB04216; Quercetin.
DR GlyGen; Q6NVY1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6NVY1; -.
DR MetOSite; Q6NVY1; -.
DR PhosphoSitePlus; Q6NVY1; -.
DR BioMuta; HIBCH; -.
DR DMDM; 146324905; -.
DR REPRODUCTION-2DPAGE; IPI00419802; -.
DR EPD; Q6NVY1; -.
DR jPOST; Q6NVY1; -.
DR MassIVE; Q6NVY1; -.
DR MaxQB; Q6NVY1; -.
DR PaxDb; Q6NVY1; -.
DR PeptideAtlas; Q6NVY1; -.
DR PRIDE; Q6NVY1; -.
DR ProteomicsDB; 66734; -. [Q6NVY1-1]
DR ProteomicsDB; 66735; -. [Q6NVY1-2]
DR Antibodypedia; 34034; 299 antibodies from 27 providers.
DR DNASU; 26275; -.
DR Ensembl; ENST00000359678.10; ENSP00000352706.5; ENSG00000198130.16. [Q6NVY1-1]
DR Ensembl; ENST00000392332.7; ENSP00000376144.3; ENSG00000198130.16. [Q6NVY1-2]
DR GeneID; 26275; -.
DR KEGG; hsa:26275; -.
DR MANE-Select; ENST00000359678.10; ENSP00000352706.5; NM_014362.4; NP_055177.2.
DR UCSC; uc002uru.3; human. [Q6NVY1-1]
DR CTD; 26275; -.
DR DisGeNET; 26275; -.
DR GeneCards; HIBCH; -.
DR HGNC; HGNC:4908; HIBCH.
DR HPA; ENSG00000198130; Low tissue specificity.
DR MalaCards; HIBCH; -.
DR MIM; 250620; phenotype.
DR MIM; 610690; gene.
DR neXtProt; NX_Q6NVY1; -.
DR OpenTargets; ENSG00000198130; -.
DR Orphanet; 88639; Neurodegeneration due to 3-hydroxyisobutyryl-CoA hydrolase deficiency.
DR PharmGKB; PA29281; -.
DR VEuPathDB; HostDB:ENSG00000198130; -.
DR eggNOG; KOG1684; Eukaryota.
DR GeneTree; ENSGT00890000139491; -.
DR HOGENOM; CLU_009834_22_1_1; -.
DR InParanoid; Q6NVY1; -.
DR OMA; GKPYIAF; -.
DR PhylomeDB; Q6NVY1; -.
DR TreeFam; TF314329; -.
DR BRENDA; 3.1.2.4; 2681.
DR PathwayCommons; Q6NVY1; -.
DR Reactome; R-HSA-70895; Branched-chain amino acid catabolism.
DR SABIO-RK; Q6NVY1; -.
DR SignaLink; Q6NVY1; -.
DR UniPathway; UPA00362; -.
DR BioGRID-ORCS; 26275; 39 hits in 1082 CRISPR screens.
DR ChiTaRS; HIBCH; human.
DR EvolutionaryTrace; Q6NVY1; -.
DR GenomeRNAi; 26275; -.
DR Pharos; Q6NVY1; Tbio.
DR PRO; PR:Q6NVY1; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q6NVY1; protein.
DR Bgee; ENSG00000198130; Expressed in nephron tubule and 211 other tissues.
DR ExpressionAtlas; Q6NVY1; baseline and differential.
DR Genevisible; Q6NVY1; HS.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0003860; F:3-hydroxyisobutyryl-CoA hydrolase activity; IDA:UniProtKB.
DR GO; GO:0009083; P:branched-chain amino acid catabolic process; TAS:Reactome.
DR GO; GO:0006574; P:valine catabolic process; IBA:GO_Central.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR045004; ECH_dom.
DR InterPro; IPR032259; HIBYL-CoA-H.
DR PANTHER; PTHR43176; PTHR43176; 1.
DR Pfam; PF16113; ECH_2; 1.
DR SUPFAM; SSF52096; SSF52096; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing;
KW Branched-chain amino acid catabolism; Disease variant; Hydrolase;
KW Mitochondrion; Phosphoprotein; Reference proteome; Transit peptide.
FT TRANSIT 1..32
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 33..386
FT /note="3-hydroxyisobutyryl-CoA hydrolase, mitochondrial"
FT /id="PRO_0000284929"
FT BINDING 121
FT /ligand="substrate"
FT BINDING 146
FT /ligand="substrate"
FT BINDING 169
FT /ligand="substrate"
FT BINDING 177
FT /ligand="substrate"
FT MOD_RES 55
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8QZS1"
FT MOD_RES 55
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8QZS1"
FT MOD_RES 92
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 92
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8QZS1"
FT MOD_RES 221
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8QZS1"
FT MOD_RES 221
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8QZS1"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 257
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8QZS1"
FT MOD_RES 297
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8QZS1"
FT MOD_RES 297
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8QZS1"
FT MOD_RES 301
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8QZS1"
FT MOD_RES 353
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8QZS1"
FT MOD_RES 353
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8QZS1"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 360
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8QZS1"
FT MOD_RES 365
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8QZS1"
FT MOD_RES 377
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8QZS1"
FT VAR_SEQ 338..385
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_024780"
FT VARIANT 46
FT /note="T -> A (in dbSNP:rs1058180)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2,
FT ECO:0000269|Ref.4"
FT /id="VAR_031869"
FT VARIANT 122
FT /note="Y -> C (in HIBCHD; dbSNP:rs121918329)"
FT /evidence="ECO:0000269|PubMed:17160907"
FT /id="VAR_031870"
FT CONFLICT 41
FT /note="E -> G (in Ref. 5; AAH67822)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="L -> V (in Ref. 1; AAC52114)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="Q -> R (in Ref. 2; BAD96699)"
FT /evidence="ECO:0000305"
FT CONFLICT 184..198
FT /note="LPRLQGKLGYFLALT -> FATTPRKTWLLPCIN (in Ref. 1;
FT AAC52114)"
FT /evidence="ECO:0000305"
FT CONFLICT 369
FT /note="E -> K (in Ref. 2; BAD96699)"
FT /evidence="ECO:0000305"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:3BPT"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:3BPT"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:3BPT"
FT HELIX 62..77
FT /evidence="ECO:0007829|PDB:3BPT"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:3BPT"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:3BPT"
FT HELIX 100..107
FT /evidence="ECO:0007829|PDB:3BPT"
FT HELIX 114..129
FT /evidence="ECO:0007829|PDB:3BPT"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:3BPT"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:3BPT"
FT HELIX 146..149
FT /evidence="ECO:0007829|PDB:3BPT"
FT TURN 150..153
FT /evidence="ECO:0007829|PDB:3BPT"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:3BPT"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:3BPT"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:3BPT"
FT HELIX 180..186
FT /evidence="ECO:0007829|PDB:3BPT"
FT HELIX 191..198
FT /evidence="ECO:0007829|PDB:3BPT"
FT HELIX 205..209
FT /evidence="ECO:0007829|PDB:3BPT"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:3BPT"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:3BPT"
FT HELIX 222..231
FT /evidence="ECO:0007829|PDB:3BPT"
FT HELIX 237..250
FT /evidence="ECO:0007829|PDB:3BPT"
FT TURN 253..256
FT /evidence="ECO:0007829|PDB:3BPT"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:3BPT"
FT HELIX 265..271
FT /evidence="ECO:0007829|PDB:3BPT"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:3BPT"
FT HELIX 277..287
FT /evidence="ECO:0007829|PDB:3BPT"
FT HELIX 290..299
FT /evidence="ECO:0007829|PDB:3BPT"
FT HELIX 304..317
FT /evidence="ECO:0007829|PDB:3BPT"
FT HELIX 322..337
FT /evidence="ECO:0007829|PDB:3BPT"
FT HELIX 341..349
FT /evidence="ECO:0007829|PDB:3BPT"
FT HELIX 364..366
FT /evidence="ECO:0007829|PDB:3BPT"
FT HELIX 369..376
FT /evidence="ECO:0007829|PDB:3BPT"
FT HELIX 380..382
FT /evidence="ECO:0007829|PDB:3BPT"
SQ SEQUENCE 386 AA; 43482 MW; 11B0632ED1DF2FFA CRC64;
MGQREMWRLM SRFNAFKRTN TILHHLRMSK HTDAAEEVLL EKKGCTGVIT LNRPKFLNAL
TLNMIRQIYP QLKKWEQDPE TFLIIIKGAG GKAFCAGGDI RVISEAEKAK QKIAPVFFRE
EYMLNNAVGS CQKPYVALIH GITMGGGVGL SVHGQFRVAT EKCLFAMPET AIGLFPDVGG
GYFLPRLQGK LGYFLALTGF RLKGRDVYRA GIATHFVDSE KLAMLEEDLL ALKSPSKENI
ASVLENYHTE SKIDRDKSFI LEEHMDKINS CFSANTVEEI IENLQQDGSS FALEQLKVIN
KMSPTSLKIT LRQLMEGSSK TLQEVLTMEY RLSQACMRGH DFHEGVRAVL IDKDQSPKWK
PADLKEVTEE DLNNHFKSLG SSDLKF
