AL1A3_HUMAN
ID AL1A3_HUMAN Reviewed; 512 AA.
AC P47895; Q6NT64;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Aldehyde dehydrogenase family 1 member A3;
DE EC=1.2.1.36 {ECO:0000269|PubMed:27759097};
DE AltName: Full=Aldehyde dehydrogenase 6;
DE AltName: Full=Retinaldehyde dehydrogenase 3;
DE Short=RALDH-3;
DE Short=RalDH3;
GN Name=ALDH1A3; Synonyms=ALDH6 {ECO:0000303|PubMed:7698756};
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], AND TISSUE SPECIFICITY.
RC TISSUE=Salivary gland;
RX PubMed=7698756; DOI=10.1006/geno.1994.1624;
RA Hsu L.C., Chang W.-C., Hiraoka L., Hsieh C.-L.;
RT "Molecular cloning, genomic organization, and chromosomal localization of
RT an additional human aldehyde dehydrogenase gene, ALDH6.";
RL Genomics 24:333-341(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
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 PROTEIN SEQUENCE OF 2-15; 253-263; 407-421; 432-446 AND 488-501, CLEAVAGE
RP OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Dozynkiewicz M., Norman J.C.;
RL Submitted (MAR-2009) to UniProtKB.
RN [4]
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 [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [6]
RP INVOLVEMENT IN MCOP8.
RX PubMed=23591992; DOI=10.1093/hmg/ddt179;
RA Yahyavi M., Abouzeid H., Gawdat G., de Preux A.S., Xiao T., Bardakjian T.,
RA Schneider A., Choi A., Jorgenson E., Baier H., El Sada M., Schorderet D.F.,
RA Slavotinek A.M.;
RT "ALDH1A3 loss of function causes bilateral anophthalmia/microphthalmia and
RT hypoplasia of the optic nerve and optic chiasm.";
RL Hum. Mol. Genet. 22:3250-3258(2013).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN COMPLEX WITH NAD AND ALL-TRANS
RP RETINOIC ACID, SUBUNIT, CATALYTIC ACTIVITY, ACTIVE SITE, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=27759097; DOI=10.1038/srep35710;
RA Moretti A., Li J., Donini S., Sobol R.W., Rizzi M., Garavaglia S.;
RT "Crystal structure of human aldehyde dehydrogenase 1A3 complexed with
RT NAD(+) and retinoic acid.";
RL Sci. Rep. 6:35710-35710(2016).
RN [8]
RP VARIANTS MCOP8 CYS-89 AND PRO-493, AND CHARACTERIZATION OF VARIANTS MCOP8
RP CYS-89 AND PRO-493.
RX PubMed=23312594; DOI=10.1016/j.ajhg.2012.12.003;
RA Fares-Taie L., Gerber S., Chassaing N., Clayton-Smith J., Hanein S.,
RA Silva E., Serey M., Serre V., Gerard X., Baumann C., Plessis G., Demeer B.,
RA Bretillon L., Bole C., Nitschke P., Munnich A., Lyonnet S., Calvas P.,
RA Kaplan J., Ragge N., Rozet J.M.;
RT "ALDH1A3 mutations cause recessive anophthalmia and microphthalmia.";
RL Am. J. Hum. Genet. 92:265-270(2013).
RN [9]
RP VARIANTS MCOP8 VAL-145 AND PHE-369.
RX PubMed=23646827; DOI=10.1111/cge.12184;
RA Aldahmesh M.A., Khan A.O., Hijazi H., Alkuraya F.S.;
RT "Mutations in ALDH1A3 cause Microphthalmia.";
RL Clin. Genet. 84:128-131(2013).
RN [10]
RP VARIANT MCOP8 LYS-466.
RX PubMed=24568872; DOI=10.1136/bjophthalmol-2013-304058;
RA Semerci C.N., Kalay E., Yildirim C., Dincer T., Olmez A., Toraman B.,
RA Kocyigit A., Bulgu Y., Okur V., Satiroglu-Tufan L., Akarsu N.A.;
RT "Novel splice-site and missense mutations in the ALDH1A3 gene underlying
RT autosomal recessive anophthalmia/microphthalmia.";
RL Br. J. Ophthalmol. 98:832-840(2014).
RN [11]
RP VARIANT MCOP8 TYR-174.
RX PubMed=24024553; DOI=10.1111/cge.12277;
RA Roos L., Fang M., Dali C., Jensen H., Christoffersen N., Wu B., Zhang J.,
RA Xu R., Harris P., Xu X., Groenskov K., Tuemer Z.;
RT "A homozygous mutation in a consanguineous family consolidates the role of
RT ALDH1A3 in autosomal recessive microphthalmia.";
RL Clin. Genet. 86:276-281(2014).
RN [12]
RP VARIANT MCOP8 MET-71.
RX PubMed=23881059; DOI=10.1038/ejhg.2013.157;
RA Mory A., Ruiz F.X., Dagan E., Yakovtseva E.A., Kurolap A., Pares X.,
RA Farres J., Gershoni-Baruch R.;
RT "A missense mutation in ALDH1A3 causes isolated microphthalmia/anophthalmia
RT in nine individuals from an inbred Muslim kindred.";
RL Eur. J. Hum. Genet. 22:419-422(2014).
RN [13]
RP VARIANTS MCOP8 ARG-355; ARG-382 AND LYS-411.
RX PubMed=24777706; DOI=10.1002/humu.22580;
RA Abouzeid H., Favez T., Schmid A., Agosti C., Youssef M., Marzouk I.,
RA El Shakankiry N., Bayoumi N., Munier F.L., Schorderet D.F.;
RT "Mutations in ALDH1A3 represent a frequent cause of
RT microphthalmia/anophthalmia in consanguineous families.";
RL Hum. Mutat. 35:949-953(2014).
CC -!- FUNCTION: NAD-dependent aldehyde dehydrogenase that catalyzes the
CC formation of retinoic acid (PubMed:27759097). Has high activity with
CC all-trans retinal, and has much lower in vitro activity with
CC acetaldehyde (PubMed:27759097). Required for the biosynthesis of normal
CC levels of retinoic acid in the embryonic ocular and nasal regions;
CC retinoic acid is required for normal embryonic development of the eye
CC and the nasal region (By similarity). {ECO:0000250|UniProtKB:Q9JHW9,
CC ECO:0000269|PubMed:27759097}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinal + H2O + NAD(+) = all-trans-retinoate + 2
CC H(+) + NADH; Xref=Rhea:RHEA:42080, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17898, ChEBI:CHEBI:35291,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.36;
CC Evidence={ECO:0000269|PubMed:27759097};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9.3 uM for all-trans retinal {ECO:0000269|PubMed:27759097};
CC KM=4.8 uM for NAD {ECO:0000269|PubMed:27759097};
CC KM=2.4 mM for acetaldehyde {ECO:0000269|PubMed:27759097};
CC -!- PATHWAY: Cofactor metabolism; retinol metabolism.
CC {ECO:0000269|PubMed:27759097}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:27759097}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9JHW9}.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in many tissues and at
CC higher levels in salivary gland, stomach, and kidney.
CC {ECO:0000269|PubMed:7698756}.
CC -!- DISEASE: Microphthalmia, isolated, 8 (MCOP8) [MIM:615113]: A disorder
CC of eye formation, ranging from small size of a single eye to complete
CC bilateral absence of ocular tissues. Ocular abnormalities like
CC opacities of the cornea and lens, scaring of the retina and choroid,
CC and other abnormalities may also be present.
CC {ECO:0000269|PubMed:23312594, ECO:0000269|PubMed:23591992,
CC ECO:0000269|PubMed:23646827, ECO:0000269|PubMed:23881059,
CC ECO:0000269|PubMed:24024553, ECO:0000269|PubMed:24568872,
CC ECO:0000269|PubMed:24777706}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; U07919; AAA79036.1; -; mRNA.
DR EMBL; BC069274; AAH69274.1; -; mRNA.
DR CCDS; CCDS10389.1; -.
DR PIR; A55684; A55684.
DR RefSeq; NP_000684.2; NM_000693.3.
DR RefSeq; NP_001280744.1; NM_001293815.1.
DR PDB; 5FHZ; X-ray; 2.90 A; A/B/C/D/E/F/G/H=1-512.
DR PDB; 6S6W; X-ray; 3.25 A; A/B=20-508.
DR PDB; 6TE5; X-ray; 3.25 A; A/B=1-512.
DR PDB; 6TGW; X-ray; 2.80 A; A/B/C/D=1-512.
DR PDB; 6TRY; X-ray; 2.90 A; A/B=1-512.
DR PDB; 7A6Q; X-ray; 2.95 A; A/B=1-512.
DR PDBsum; 5FHZ; -.
DR PDBsum; 6S6W; -.
DR PDBsum; 6TE5; -.
DR PDBsum; 6TGW; -.
DR PDBsum; 6TRY; -.
DR PDBsum; 7A6Q; -.
DR AlphaFoldDB; P47895; -.
DR SMR; P47895; -.
DR BioGRID; 106722; 49.
DR IntAct; P47895; 16.
DR MINT; P47895; -.
DR STRING; 9606.ENSP00000332256; -.
DR BindingDB; P47895; -.
DR ChEMBL; CHEMBL3579; -.
DR DrugBank; DB00157; NADH.
DR DrugBank; DB00162; Vitamin A.
DR SwissLipids; SLP:000001878; -.
DR iPTMnet; P47895; -.
DR PhosphoSitePlus; P47895; -.
DR SwissPalm; P47895; -.
DR BioMuta; ALDH1A3; -.
DR DMDM; 52788258; -.
DR EPD; P47895; -.
DR jPOST; P47895; -.
DR MassIVE; P47895; -.
DR MaxQB; P47895; -.
DR PaxDb; P47895; -.
DR PeptideAtlas; P47895; -.
DR PRIDE; P47895; -.
DR ProteomicsDB; 55815; -.
DR Antibodypedia; 43944; 235 antibodies from 31 providers.
DR DNASU; 220; -.
DR Ensembl; ENST00000329841.10; ENSP00000332256.5; ENSG00000184254.17.
DR GeneID; 220; -.
DR KEGG; hsa:220; -.
DR MANE-Select; ENST00000329841.10; ENSP00000332256.5; NM_000693.4; NP_000684.2.
DR UCSC; uc002bwn.5; human.
DR CTD; 220; -.
DR DisGeNET; 220; -.
DR GeneCards; ALDH1A3; -.
DR HGNC; HGNC:409; ALDH1A3.
DR HPA; ENSG00000184254; Tissue enhanced (prostate, urinary bladder).
DR MalaCards; ALDH1A3; -.
DR MIM; 600463; gene.
DR MIM; 615113; phenotype.
DR neXtProt; NX_P47895; -.
DR OpenTargets; ENSG00000184254; -.
DR Orphanet; 98938; Colobomatous microphthalmia.
DR Orphanet; 35612; Nanophthalmos.
DR PharmGKB; PA24694; -.
DR VEuPathDB; HostDB:ENSG00000184254; -.
DR eggNOG; KOG2450; Eukaryota.
DR GeneTree; ENSGT00940000158815; -.
DR HOGENOM; CLU_005391_0_1_1; -.
DR InParanoid; P47895; -.
DR OMA; NDDLGEV; -.
DR OrthoDB; 153834at2759; -.
DR PhylomeDB; P47895; -.
DR TreeFam; TF300455; -.
DR BioCyc; MetaCyc:HS00013-MON; -.
DR BRENDA; 1.2.1.5; 2681.
DR PathwayCommons; P47895; -.
DR Reactome; R-HSA-5365859; RA biosynthesis pathway.
DR SignaLink; P47895; -.
DR SIGNOR; P47895; -.
DR UniPathway; UPA00912; -.
DR BioGRID-ORCS; 220; 6 hits in 1068 CRISPR screens.
DR ChiTaRS; ALDH1A3; human.
DR GeneWiki; ALDH1A3; -.
DR GenomeRNAi; 220; -.
DR Pharos; P47895; Tchem.
DR PRO; PR:P47895; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; P47895; protein.
DR Bgee; ENSG00000184254; Expressed in palpebral conjunctiva and 154 other tissues.
DR ExpressionAtlas; P47895; baseline and differential.
DR Genevisible; P47895; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IBA:GO_Central.
DR GO; GO:0004030; F:aldehyde dehydrogenase [NAD(P)+] activity; IDA:UniProtKB.
DR GO; GO:0070403; F:NAD+ binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0001758; F:retinal dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0070324; F:thyroid hormone binding; IEA:Ensembl.
DR GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
DR GO; GO:0031076; P:embryonic camera-type eye development; ISS:UniProtKB.
DR GO; GO:0048048; P:embryonic eye morphogenesis; ISS:UniProtKB.
DR GO; GO:0060324; P:face development; IEA:Ensembl.
DR GO; GO:0070384; P:Harderian gland development; IEA:Ensembl.
DR GO; GO:0042472; P:inner ear morphogenesis; IEA:Ensembl.
DR GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl.
DR GO; GO:0021768; P:nucleus accumbens development; IEA:Ensembl.
DR GO; GO:0060166; P:olfactory pit development; IEA:Ensembl.
DR GO; GO:0002072; P:optic cup morphogenesis involved in camera-type eye development; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR GO; GO:0042574; P:retinal metabolic process; IDA:UniProtKB.
DR GO; GO:0002138; P:retinoic acid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0042573; P:retinoic acid metabolic process; IDA:UniProtKB.
DR GO; GO:0042572; P:retinol metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0060013; P:righting reflex; IEA:Ensembl.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 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 Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Disease variant; Lipid metabolism; Microphthalmia; NAD; Oxidoreductase;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PubMed:22814378"
FT CHAIN 2..512
FT /note="Aldehyde dehydrogenase family 1 member A3"
FT /id="PRO_0000056478"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 280
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008,
FT ECO:0000305|PubMed:27759097"
FT ACT_SITE 314
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 204
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:27759097,
FT ECO:0007744|PDB:5FHZ"
FT BINDING 207
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:27759097,
FT ECO:0007744|PDB:5FHZ"
FT BINDING 257..262
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:27759097,
FT ECO:0007744|PDB:5FHZ"
FT BINDING 361
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:27759097,
FT ECO:0007744|PDB:5FHZ"
FT BINDING 411
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:27759097,
FT ECO:0007744|PDB:5FHZ"
FT SITE 181
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PubMed:22814378"
FT VARIANT 71
FT /note="V -> M (in MCOP8; dbSNP:rs386834230)"
FT /evidence="ECO:0000269|PubMed:23881059"
FT /id="VAR_072332"
FT VARIANT 89
FT /note="R -> C (in MCOP8; does not affect ALDH1A3
FT expression; results in strongly reduced protein levels;
FT dbSNP:rs397514652)"
FT /evidence="ECO:0000269|PubMed:23312594"
FT /id="VAR_069322"
FT VARIANT 145
FT /note="A -> V (in MCOP8; dbSNP:rs754619607)"
FT /evidence="ECO:0000269|PubMed:23646827"
FT /id="VAR_069323"
FT VARIANT 174
FT /note="C -> Y (in MCOP8)"
FT /evidence="ECO:0000269|PubMed:24024553"
FT /id="VAR_072333"
FT VARIANT 355
FT /note="P -> R (in MCOP8)"
FT /evidence="ECO:0000269|PubMed:24777706"
FT /id="VAR_072334"
FT VARIANT 369
FT /note="I -> F (in MCOP8)"
FT /evidence="ECO:0000269|PubMed:23646827"
FT /id="VAR_069324"
FT VARIANT 382
FT /note="G -> R (in MCOP8)"
FT /evidence="ECO:0000269|PubMed:24777706"
FT /id="VAR_072335"
FT VARIANT 386
FT /note="M -> V (in dbSNP:rs3803430)"
FT /id="VAR_019706"
FT VARIANT 411
FT /note="E -> K (in MCOP8)"
FT /evidence="ECO:0000269|PubMed:24777706"
FT /id="VAR_072336"
FT VARIANT 466
FT /note="N -> K (in MCOP8)"
FT /evidence="ECO:0000269|PubMed:24568872"
FT /id="VAR_072337"
FT VARIANT 493
FT /note="A -> P (in MCOP8; does not affect ALDH1A3
FT expression; results in strongly reduced protein levels;
FT dbSNP:rs397514653)"
FT /evidence="ECO:0000269|PubMed:23312594"
FT /id="VAR_069325"
FT CONFLICT 15
FT /note="R -> G (in Ref. 1; AAA79036)"
FT /evidence="ECO:0000305"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:6TGW"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:6TGW"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:6TGW"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:6TGW"
FT STRAND 57..64
FT /evidence="ECO:0007829|PDB:6TGW"
FT HELIX 68..82
FT /evidence="ECO:0007829|PDB:6TGW"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:6TGW"
FT HELIX 93..109
FT /evidence="ECO:0007829|PDB:6TGW"
FT HELIX 111..122
FT /evidence="ECO:0007829|PDB:6TGW"
FT HELIX 126..131
FT /evidence="ECO:0007829|PDB:6TGW"
FT HELIX 133..145
FT /evidence="ECO:0007829|PDB:6TGW"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:6TGW"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:6TGW"
FT STRAND 162..170
FT /evidence="ECO:0007829|PDB:6TGW"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:6TGW"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:6TGW"
FT HELIX 183..196
FT /evidence="ECO:0007829|PDB:6TGW"
FT STRAND 200..204
FT /evidence="ECO:0007829|PDB:6TGW"
FT HELIX 211..223
FT /evidence="ECO:0007829|PDB:6TGW"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:6TGW"
FT HELIX 237..245
FT /evidence="ECO:0007829|PDB:6TGW"
FT STRAND 252..257
FT /evidence="ECO:0007829|PDB:6TGW"
FT HELIX 259..271
FT /evidence="ECO:0007829|PDB:6TGW"
FT STRAND 276..280
FT /evidence="ECO:0007829|PDB:6TGW"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:6TGW"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:6TE5"
FT HELIX 295..307
FT /evidence="ECO:0007829|PDB:6TGW"
FT HELIX 308..311
FT /evidence="ECO:0007829|PDB:6TGW"
FT STRAND 319..323
FT /evidence="ECO:0007829|PDB:6TGW"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:6TRY"
FT HELIX 327..340
FT /evidence="ECO:0007829|PDB:6TGW"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:5FHZ"
FT HELIX 359..374
FT /evidence="ECO:0007829|PDB:6TGW"
FT STRAND 378..381
FT /evidence="ECO:0007829|PDB:6TGW"
FT STRAND 384..386
FT /evidence="ECO:0007829|PDB:5FHZ"
FT STRAND 387..389
FT /evidence="ECO:0007829|PDB:6TGW"
FT STRAND 396..400
FT /evidence="ECO:0007829|PDB:6TGW"
FT STRAND 403..405
FT /evidence="ECO:0007829|PDB:6TRY"
FT HELIX 406..408
FT /evidence="ECO:0007829|PDB:6TGW"
FT STRAND 414..423
FT /evidence="ECO:0007829|PDB:6TGW"
FT HELIX 425..432
FT /evidence="ECO:0007829|PDB:6TGW"
FT STRAND 435..444
FT /evidence="ECO:0007829|PDB:6TGW"
FT HELIX 448..457
FT /evidence="ECO:0007829|PDB:6TGW"
FT STRAND 461..466
FT /evidence="ECO:0007829|PDB:6TGW"
FT HELIX 481..483
FT /evidence="ECO:0007829|PDB:6TRY"
FT STRAND 484..486
FT /evidence="ECO:0007829|PDB:6TGW"
FT STRAND 488..490
FT /evidence="ECO:0007829|PDB:6TRY"
FT HELIX 492..496
FT /evidence="ECO:0007829|PDB:6TGW"
FT STRAND 498..506
FT /evidence="ECO:0007829|PDB:6TGW"
SQ SEQUENCE 512 AA; 56108 MW; 1BFCF4F56F0FE89A CRC64;
MATANGAVEN GQPDRKPPAL PRPIRNLEVK FTKIFINNEW HESKSGKKFA TCNPSTREQI
CEVEEGDKPD VDKAVEAAQV AFQRGSPWRR LDALSRGRLL HQLADLVERD RATLAALETM
DTGKPFLHAF FIDLEGCIRT LRYFAGWADK IQGKTIPTDD NVVCFTRHEP IGVCGAITPW
NFPLLMLVWK LAPALCCGNT MVLKPAEQTP LTALYLGSLI KEAGFPPGVV NIVPGFGPTV
GAAISSHPQI NKIAFTGSTE VGKLVKEAAS RSNLKRVTLE LGGKNPCIVC ADADLDLAVE
CAHQGVFFNQ GQCCTAASRV FVEEQVYSEF VRRSVEYAKK RPVGDPFDVK TEQGPQIDQK
QFDKILELIE SGKKEGAKLE CGGSAMEDKG LFIKPTVFSE VTDNMRIAKE EIFGPVQPIL
KFKSIEEVIK RANSTDYGLT AAVFTKNLDK ALKLASALES GTVWINCYNA LYAQAPFGGF
KMSGNGRELG EYALAEYTEV KTVTIKLGDK NP
