ID AL1B1_HUMAN Reviewed; 517 AA. AC P30837; B2R8F0; Q8WX76; Q9BV45; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 23-FEB-2022, sequence version 4. DT 27-MAR-2024, entry version 208. DE RecName: Full=Aldehyde dehydrogenase X, mitochondrial; DE EC=1.2.1.3; DE AltName: Full=Aldehyde dehydrogenase 5; DE AltName: Full=Aldehyde dehydrogenase family 1 member B1; DE Flags: Precursor; GN Name=ALDH1B1; Synonyms=ALDH5, ALDHX; 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 [GENOMIC DNA], AND VARIANTS LEU-107 AND MET-253. RC TISSUE=Testis; RX PubMed=2061311; DOI=10.1016/s0021-9258(18)98890-3; RA Hsu L.C., Chang W.-C.; RT "Cloning and characterization of a new functional human aldehyde RT dehydrogenase gene."; RL J. Biol. Chem. 266:12257-12265(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS LEU-107 AND MET-253. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-253. RC TISSUE=Testis; 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., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., 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., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS LEU-107 AND MET-253. RC TISSUE=Eye; 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 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 [7] 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 [8] 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 [9] RP VARIANTS VAL-86 AND LEU-107. RX PubMed=8244338; DOI=10.1007/bf00216454; RA Sherman D., Dave V., Hsu L.C., Peters T.J., Yoshida A.; RT "Diverse polymorphism within a short coding region of the human aldehyde RT dehydrogenase-5 (ALDH5) gene."; RL Hum. Genet. 92:477-480(1993). CC -!- FUNCTION: ALDHs play a major role in the detoxification of alcohol- CC derived acetaldehyde. They are involved in the metabolism of CC corticosteroids, biogenic amines, neurotransmitters, and lipid CC peroxidation. CC -!- CATALYTIC ACTIVITY: CC Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH; CC Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945; EC=1.2.1.3; CC -!- PATHWAY: Alcohol metabolism; ethanol degradation; acetate from ethanol: CC step 2/2. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix. CC -!- TISSUE SPECIFICITY: Liver, testis and to a lesser extent in brain. CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC {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; M63967; AAA96830.1; -; Genomic_DNA. DR EMBL; BT007418; AAP36086.1; -; mRNA. DR EMBL; AK313344; BAG36147.1; -; mRNA. DR EMBL; AL135785; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC001619; AAH01619.1; -; mRNA. DR CCDS; CCDS6615.1; -. DR PIR; A40872; A40872. DR RefSeq; NP_000683.3; NM_000692.4. DR RefSeq; XP_011516104.1; XM_011517802.2. DR PDB; 7MJC; X-ray; 2.68 A; A/B=20-517. DR PDB; 7MJD; X-ray; 2.12 A; A/B=20-517. DR PDB; 7RAD; X-ray; 2.30 A; A/B=25-517. DR PDBsum; 7MJC; -. DR PDBsum; 7MJD; -. DR PDBsum; 7RAD; -. DR AlphaFoldDB; P30837; -. DR SMR; P30837; -. DR BioGRID; 106721; 204. DR IntAct; P30837; 46. DR MINT; P30837; -. DR STRING; 9606.ENSP00000366927; -. DR BindingDB; P30837; -. DR ChEMBL; CHEMBL4881; -. DR DrugBank; DB00157; NADH. DR GlyGen; P30837; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P30837; -. DR PhosphoSitePlus; P30837; -. DR SwissPalm; P30837; -. DR BioMuta; ALDH1B1; -. DR DMDM; 311033472; -. DR REPRODUCTION-2DPAGE; IPI00103467; -. DR EPD; P30837; -. DR jPOST; P30837; -. DR MassIVE; P30837; -. DR MaxQB; P30837; -. DR PaxDb; 9606-ENSP00000366927; -. DR PeptideAtlas; P30837; -. DR ProteomicsDB; 54740; -. DR Pumba; P30837; -. DR Antibodypedia; 12074; 334 antibodies from 35 providers. DR DNASU; 219; -. DR Ensembl; ENST00000377698.4; ENSP00000366927.3; ENSG00000137124.8. DR GeneID; 219; -. DR KEGG; hsa:219; -. DR MANE-Select; ENST00000377698.4; ENSP00000366927.3; NM_000692.5; NP_000683.3. DR UCSC; uc004aay.4; human. DR AGR; HGNC:407; -. DR CTD; 219; -. DR DisGeNET; 219; -. DR GeneCards; ALDH1B1; -. DR HGNC; HGNC:407; ALDH1B1. DR HPA; ENSG00000137124; Tissue enhanced (liver, smooth muscle). DR MIM; 100670; gene. DR neXtProt; NX_P30837; -. DR OpenTargets; ENSG00000137124; -. DR PharmGKB; PA24695; -. DR VEuPathDB; HostDB:ENSG00000137124; -. DR eggNOG; KOG2450; Eukaryota. DR GeneTree; ENSGT00940000162530; -. DR HOGENOM; CLU_005391_0_2_1; -. DR InParanoid; P30837; -. DR OMA; WVNRYGR; -. DR OrthoDB; 2291791at2759; -. DR PhylomeDB; P30837; -. DR TreeFam; TF300455; -. DR BRENDA; 1.2.1.3; 2681. DR PathwayCommons; P30837; -. DR Reactome; R-HSA-71384; Ethanol oxidation. DR SABIO-RK; P30837; -. DR SignaLink; P30837; -. DR UniPathway; UPA00780; UER00768. DR BioGRID-ORCS; 219; 13 hits in 1164 CRISPR screens. DR ChiTaRS; ALDH1B1; human. DR GeneWiki; ALDH1B1; -. DR GenomeRNAi; 219; -. DR Pharos; P30837; Tchem. DR PRO; PR:P30837; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; P30837; Protein. DR Bgee; ENSG00000137124; Expressed in buccal mucosa cell and 143 other cell types or tissues. DR ExpressionAtlas; P30837; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome. DR GO; GO:0005739; C:mitochondrion; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IBA:GO_Central. DR GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC. DR GO; GO:0051287; F:NAD binding; ISS:CAFA. DR GO; GO:0005975; P:carbohydrate metabolic process; NAS:ProtInc. DR GO; GO:0006068; P:ethanol catabolic process; IEA:UniProtKB-UniPathway. DR CDD; cd07141; ALDH_F1AB_F2_RALDH1; 1. DR InterPro; IPR016161; Ald_DH/histidinol_DH. DR InterPro; IPR016163; Ald_DH_C. DR InterPro; IPR016160; Ald_DH_CS_CYS. DR InterPro; IPR029510; Ald_DH_CS_GLU. DR InterPro; IPR016162; Ald_DH_N. DR InterPro; IPR015590; Aldehyde_DH_dom. DR PANTHER; PTHR11699:SF207; ALDEHYDE DEHYDROGENASE X, MITOCHONDRIAL; 1. DR PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1. DR Pfam; PF00171; Aldedh; 1. DR SUPFAM; SSF53720; ALDH-like; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1. DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1. DR Genevisible; P30837; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Mitochondrion; NAD; Oxidoreductase; KW Reference proteome; Transit peptide. FT TRANSIT 1..17 FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN 18..517 FT /note="Aldehyde dehydrogenase X, mitochondrial" FT /id="PRO_0000007172" FT ACT_SITE 285 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007, FT ECO:0000255|PROSITE-ProRule:PRU10008" FT ACT_SITE 319 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007, FT ECO:0000255|PROSITE-ProRule:PRU10008" FT BINDING 262..267 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT SITE 186 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250" FT MOD_RES 51 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9CZS1" FT MOD_RES 52 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9CZS1" FT MOD_RES 52 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9CZS1" FT MOD_RES 81 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9CZS1" FT MOD_RES 364 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9CZS1" FT MOD_RES 364 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9CZS1" FT MOD_RES 383 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9CZS1" FT MOD_RES 383 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9CZS1" FT MOD_RES 399 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9CZS1" FT MOD_RES 399 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9CZS1" FT MOD_RES 414 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9CZS1" FT MOD_RES 414 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9CZS1" FT MOD_RES 426 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9CZS1" FT MOD_RES 426 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9CZS1" FT MOD_RES 429 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9CZS1" FT VARIANT 86 FT /note="A -> V (in dbSNP:rs2228093)" FT /evidence="ECO:0000269|PubMed:8244338" FT /id="VAR_002257" FT VARIANT 107 FT /note="R -> L (in dbSNP:rs2073478)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:2061311, ECO:0000269|PubMed:8244338, FT ECO:0000269|Ref.2" FT /id="VAR_002258" FT VARIANT 202 FT /note="T -> I (in dbSNP:rs4646773)" FT /id="VAR_029891" FT VARIANT 253 FT /note="V -> M (in dbSNP:rs4878199)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:2061311, FT ECO:0000269|Ref.2" FT /id="VAR_029892" FT CONFLICT 18 FT /note="R -> L (in Ref. 1; AAA96830)" FT /evidence="ECO:0000305" FT CONFLICT 164 FT /note="D -> H (in Ref. 1; AAA96830)" FT /evidence="ECO:0000305" FT STRAND 38..41 FT /evidence="ECO:0007829|PDB:7MJD" FT STRAND 44..46 FT /evidence="ECO:0007829|PDB:7MJD" FT STRAND 53..57 FT /evidence="ECO:0007829|PDB:7MJD" FT TURN 59..61 FT /evidence="ECO:0007829|PDB:7MJD" FT STRAND 64..69 FT /evidence="ECO:0007829|PDB:7MJD" FT HELIX 73..87 FT /evidence="ECO:0007829|PDB:7MJD" FT HELIX 92..95 FT /evidence="ECO:0007829|PDB:7MJD" FT HELIX 98..114 FT /evidence="ECO:0007829|PDB:7MJD" FT HELIX 116..127 FT /evidence="ECO:0007829|PDB:7MJD" FT HELIX 131..136 FT /evidence="ECO:0007829|PDB:7MJD" FT HELIX 138..152 FT /evidence="ECO:0007829|PDB:7MJD" FT TURN 153..155 FT /evidence="ECO:0007829|PDB:7MJD" FT STRAND 164..175 FT /evidence="ECO:0007829|PDB:7MJD" FT STRAND 178..182 FT /evidence="ECO:0007829|PDB:7MJD" FT STRAND 185..187 FT /evidence="ECO:0007829|PDB:7MJD" FT HELIX 188..201 FT /evidence="ECO:0007829|PDB:7MJD" FT STRAND 205..210 FT /evidence="ECO:0007829|PDB:7MJD" FT STRAND 212..214 FT /evidence="ECO:0007829|PDB:7MJC" FT HELIX 216..228 FT /evidence="ECO:0007829|PDB:7MJD" FT STRAND 234..240 FT /evidence="ECO:0007829|PDB:7MJD" FT TURN 242..244 FT /evidence="ECO:0007829|PDB:7MJD" FT HELIX 245..251 FT /evidence="ECO:0007829|PDB:7MJD" FT STRAND 257..262 FT /evidence="ECO:0007829|PDB:7MJD" FT HELIX 264..276 FT /evidence="ECO:0007829|PDB:7MJD" FT STRAND 281..285 FT /evidence="ECO:0007829|PDB:7MJD" FT STRAND 290..294 FT /evidence="ECO:0007829|PDB:7MJD" FT HELIX 300..312 FT /evidence="ECO:0007829|PDB:7MJD" FT HELIX 313..316 FT /evidence="ECO:0007829|PDB:7MJD" FT STRAND 322..328 FT /evidence="ECO:0007829|PDB:7MJD" FT HELIX 329..331 FT /evidence="ECO:0007829|PDB:7MJD" FT HELIX 332..345 FT /evidence="ECO:0007829|PDB:7MJD" FT HELIX 364..379 FT /evidence="ECO:0007829|PDB:7MJD" FT STRAND 383..386 FT /evidence="ECO:0007829|PDB:7MJD" FT STRAND 389..396 FT /evidence="ECO:0007829|PDB:7MJD" FT STRAND 401..405 FT /evidence="ECO:0007829|PDB:7MJD" FT HELIX 411..414 FT /evidence="ECO:0007829|PDB:7MJD" FT STRAND 419..427 FT /evidence="ECO:0007829|PDB:7MJD" FT HELIX 430..438 FT /evidence="ECO:0007829|PDB:7MJD" FT STRAND 444..449 FT /evidence="ECO:0007829|PDB:7MJD" FT HELIX 453..462 FT /evidence="ECO:0007829|PDB:7MJD" FT STRAND 466..471 FT /evidence="ECO:0007829|PDB:7MJD" FT HELIX 486..488 FT /evidence="ECO:0007829|PDB:7MJD" FT STRAND 489..491 FT /evidence="ECO:0007829|PDB:7MJD" FT HELIX 497..502 FT /evidence="ECO:0007829|PDB:7MJD" FT STRAND 503..511 FT /evidence="ECO:0007829|PDB:7MJD" SQ SEQUENCE 517 AA; 57249 MW; B877BD45FEC70025 CRC64; MLRFLAPRLL SLQGRTARYS SAAALPSPIL NPDIPYNQLF INNEWQDAVS KKTFPTVNPT TGEVIGHVAE GDRADVDRAV KAAREAFRLG SPWRRMDASE RGRLLNRLAD LVERDRVYLA SLETLDNGKP FQESYALDLD EVIKVYRYFA GWADKWHGKT IPMDGQHFCF TRHEPVGVCG QIIPWNFPLV MQGWKLAPAL ATGNTVVMKV AEQTPLSALY LASLIKEAGF PPGVVNIITG YGPTAGAAIA QHVDVDKVAF TGSTEVGHLI QKAAGDSNLK RVTLELGGKS PSIVLADADM EHAVEQCHEA LFFNMGQCCC AGSRTFVEES IYNEFLERTV EKAKQRKVGN PFELDTQQGP QVDKEQFERV LGYIQLGQKE GAKLLCGGER FGERGFFIKP TVFGGVQDDM RIAKEEIFGP VQPLFKFKKI EEVVERANNT RYGLAAAVFT RDLDKAMYFT QALQAGTVWV NTYNIVTCHT PFGGFKESGN GRELGEDGLK AYTEVKTVTI KVPQKNS //