GenomeNet

Database: UniProt
Entry: O94788
LinkDB: O94788
Original site: O94788 
ID   AL1A2_HUMAN             Reviewed;         518 AA.
AC   O94788; B3KY52; B4DZR2; F5H2Y9; H0YM00; Q2PJS6; Q8NHQ4; Q9UBR8; Q9UFY0;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 3.
DT   12-AUG-2020, entry version 183.
DE   RecName: Full=Retinal dehydrogenase 2;
DE            Short=RALDH 2;
DE            Short=RalDH2 {ECO:0000303|PubMed:9819382};
DE            EC=1.2.1.36 {ECO:0000269|PubMed:29240402};
DE   AltName: Full=Aldehyde dehydrogenase family 1 member A2;
DE   AltName: Full=Retinaldehyde-specific dehydrogenase type 2;
DE            Short=RALDH(II);
GN   Name=ALDH1A2; Synonyms=RALDH2;
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] (ISOFORMS 1 AND 4), AND VARIANT ILE-348.
RX   PubMed=9819382; DOI=10.1128/mcb.18.12.6939;
RA   Ono Y., Fukuhara N., Yoshie O.;
RT   "TAL1 and LIM-only proteins synergistically induce retinaldehyde
RT   dehydrogenase 2 expression in T-cell acute lymphoblastic leukemia by acting
RT   as cofactors for GATA3.";
RL   Mol. Cell. Biol. 18:6939-6950(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP   ILE-348.
RC   TISSUE=Testis, and Uterus;
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   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLY-50; VAL-110; ILE-348
RP   AND LYS-436.
RG   NIEHS SNPs program;
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16572171; DOI=10.1038/nature04601;
RA   Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA   Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA   FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA   Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA   Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA   DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA   Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA   Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA   Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA   O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA   Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA   Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT   "Analysis of the DNA sequence and duplication history of human chromosome
RT   15.";
RL   Nature 440:671-675(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 302-518 (ISOFORMS 1/2), AND
RP   VARIANT ILE-348.
RC   TISSUE=Testis;
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., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
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 TYR-168 AND SER-351, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=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] {ECO:0000244|PDB:4X2Q}
RP   X-RAY CRYSTALLOGRAPHY (2.94 ANGSTROMS) OF 21-518 IN COMPLEX WITH NAD.
RA   Goldstein A.S., Paik J., Moreb J., Haenisch M., Le Trong I., Stenkamp R.E.,
RA   Petrie A.G., Smith N., Mallochowski W.P., Amory J.K.;
RT   "Synthesis and in vitro testing of bisdichloroacetyldiamine analogs for use
RT   as a reversible male contraceptive.";
RL   Submitted (NOV-2014) to the PDB data bank.
RN   [10] {ECO:0000244|PDB:6ALJ, ECO:0000244|PDB:6B5G, ECO:0000244|PDB:6B5H, ECO:0000244|PDB:6B5I}
RP   X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF 26-518 IN COMPLEXES WITH NAD AND
RP   SYNTHETIC INHIBITORS, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, ACTIVE SITE,
RP   AND PATHWAY.
RX   PubMed=29240402; DOI=10.1021/acschembio.7b00685;
RA   Chen Y., Zhu J.Y., Hong K.H., Mikles D.C., Georg G.I., Goldstein A.S.,
RA   Amory J.K., Schonbrunn E.;
RT   "Structural Basis of ALDH1A2 Inhibition by Irreversible and Reversible
RT   Small Molecule Inhibitors.";
RL   ACS Chem. Biol. 13:582-590(2018).
CC   -!- FUNCTION: Converts retinaldehyde to retinoic acid (PubMed:29240402).
CC       Recognizes as substrates free retinal and cellular retinol-binding
CC       protein-bound retinal. Can metabolize octanal and decanal, but has only
CC       very low activity with benzaldehyde, acetaldehyde and propanal.
CC       Displays complete lack of activity with citral (By similarity).
CC       {ECO:0000250|UniProtKB:Q63639, ECO:0000269|PubMed:29240402}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + NAD(+) + retinal = 2 H(+) + NADH + retinoate;
CC         Xref=Rhea:RHEA:16177, ChEBI:CHEBI:15035, ChEBI:CHEBI:15036,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.2.1.36;
CC         Evidence={ECO:0000269|PubMed:29240402};
CC   -!- PATHWAY: Cofactor metabolism; retinol metabolism.
CC       {ECO:0000269|PubMed:29240402}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:29240402}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=O94788-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O94788-2; Sequence=VSP_017363;
CC       Name=3;
CC         IsoId=O94788-3; Sequence=VSP_044496;
CC       Name=4;
CC         IsoId=O94788-4; Sequence=VSP_047259;
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/aldh1a2/";
DR   EMBL; AB015226; BAA34785.1; -; mRNA.
DR   EMBL; AB015227; BAA34786.1; -; mRNA.
DR   EMBL; AB015228; BAA34787.1; -; mRNA.
DR   EMBL; AK128709; BAG54714.1; -; mRNA.
DR   EMBL; AK303057; BAG64174.1; -; mRNA.
DR   EMBL; DQ322171; ABC40749.1; -; Genomic_DNA.
DR   EMBL; AC012653; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC018904; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC025431; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC066616; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC084781; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC030589; AAH30589.1; -; mRNA.
DR   EMBL; AL110299; CAB53740.2; -; mRNA.
DR   CCDS; CCDS10163.1; -. [O94788-1]
DR   CCDS; CCDS10164.1; -. [O94788-2]
DR   CCDS; CCDS45266.1; -. [O94788-4]
DR   CCDS; CCDS55968.1; -. [O94788-3]
DR   PIR; T14799; T14799.
DR   RefSeq; NP_001193826.1; NM_001206897.1. [O94788-3]
DR   RefSeq; NP_003879.2; NM_003888.3. [O94788-1]
DR   RefSeq; NP_733797.1; NM_170696.2. [O94788-2]
DR   RefSeq; NP_733798.1; NM_170697.2. [O94788-4]
DR   PDB; 4X2Q; X-ray; 2.94 A; A/B/C/D=21-518.
DR   PDB; 6ALJ; X-ray; 1.89 A; A/B/C/D=26-518.
DR   PDB; 6B5G; X-ray; 2.20 A; A/B/C/D=26-518.
DR   PDB; 6B5H; X-ray; 2.30 A; A/B/C/D=26-518.
DR   PDB; 6B5I; X-ray; 2.60 A; A/B/C/D=26-518.
DR   PDBsum; 4X2Q; -.
DR   PDBsum; 6ALJ; -.
DR   PDBsum; 6B5G; -.
DR   PDBsum; 6B5H; -.
DR   PDBsum; 6B5I; -.
DR   SMR; O94788; -.
DR   BioGRID; 114379; 10.
DR   IntAct; O94788; 5.
DR   STRING; 9606.ENSP00000249750; -.
DR   BindingDB; O94788; -.
DR   ChEMBL; CHEMBL3112384; -.
DR   DrugBank; DB00157; NADH.
DR   DrugBank; DB00755; Tretinoin.
DR   DrugBank; DB00162; Vitamin A.
DR   DrugCentral; O94788; -.
DR   iPTMnet; O94788; -.
DR   PhosphoSitePlus; O94788; -.
DR   BioMuta; ALDH1A2; -.
DR   EPD; O94788; -.
DR   jPOST; O94788; -.
DR   MassIVE; O94788; -.
DR   MaxQB; O94788; -.
DR   PaxDb; O94788; -.
DR   PeptideAtlas; O94788; -.
DR   PRIDE; O94788; -.
DR   ProteomicsDB; 26115; -.
DR   ProteomicsDB; 40109; -.
DR   ProteomicsDB; 50442; -. [O94788-1]
DR   ProteomicsDB; 50443; -. [O94788-2]
DR   Antibodypedia; 2127; 342 antibodies.
DR   DNASU; 8854; -.
DR   Ensembl; ENST00000249750; ENSP00000249750; ENSG00000128918. [O94788-1]
DR   Ensembl; ENST00000347587; ENSP00000309623; ENSG00000128918. [O94788-2]
DR   Ensembl; ENST00000537372; ENSP00000438296; ENSG00000128918. [O94788-3]
DR   Ensembl; ENST00000559517; ENSP00000453408; ENSG00000128918. [O94788-4]
DR   GeneID; 8854; -.
DR   KEGG; hsa:8854; -.
DR   UCSC; uc002aew.4; human. [O94788-1]
DR   CTD; 8854; -.
DR   DisGeNET; 8854; -.
DR   EuPathDB; HostDB:ENSG00000128918.14; -.
DR   GeneCards; ALDH1A2; -.
DR   HGNC; HGNC:15472; ALDH1A2.
DR   HPA; ENSG00000128918; Low tissue specificity.
DR   MIM; 603687; gene.
DR   neXtProt; NX_O94788; -.
DR   OpenTargets; ENSG00000128918; -.
DR   PharmGKB; PA24693; -.
DR   eggNOG; KOG2450; Eukaryota.
DR   GeneTree; ENSGT00940000158898; -.
DR   HOGENOM; CLU_005391_0_0_1; -.
DR   InParanoid; O94788; -.
DR   KO; K07249; -.
DR   OMA; ERWSPAC; -.
DR   OrthoDB; 153834at2759; -.
DR   PhylomeDB; O94788; -.
DR   TreeFam; TF300455; -.
DR   BioCyc; MetaCyc:HS05232-MONOMER; -.
DR   PathwayCommons; O94788; -.
DR   Reactome; R-HSA-5365859; RA biosynthesis pathway.
DR   UniPathway; UPA00912; -.
DR   BioGRID-ORCS; 8854; 3 hits in 876 CRISPR screens.
DR   ChiTaRS; ALDH1A2; human.
DR   GeneWiki; ALDH1A2; -.
DR   GenomeRNAi; 8854; -.
DR   Pharos; O94788; Tbio.
DR   PRO; PR:O94788; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; O94788; protein.
DR   Bgee; ENSG00000128918; Expressed in adrenal tissue and 189 other tissues.
DR   ExpressionAtlas; O94788; baseline and differential.
DR   Genevisible; O94788; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0004028; F:3-chloroallyl aldehyde dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IBA:GO_Central.
DR   GO; GO:0016918; F:retinal binding; ISS:UniProtKB.
DR   GO; GO:0001758; F:retinal dehydrogenase activity; IDA:UniProtKB.
DR   GO; GO:0042904; P:9-cis-retinoic acid biosynthetic process; IEA:Ensembl.
DR   GO; GO:0001568; P:blood vessel development; IEA:Ensembl.
DR   GO; GO:0048738; P:cardiac muscle tissue development; IEA:Ensembl.
DR   GO; GO:0071300; P:cellular response to retinoic acid; IEA:Ensembl.
DR   GO; GO:0009855; P:determination of bilateral symmetry; IEA:Ensembl.
DR   GO; GO:0031076; P:embryonic camera-type eye development; IEA:Ensembl.
DR   GO; GO:0048566; P:embryonic digestive tract development; IEA:Ensembl.
DR   GO; GO:0035115; P:embryonic forelimb morphogenesis; IEA:Ensembl.
DR   GO; GO:0060324; P:face development; IEA:Ensembl.
DR   GO; GO:0003007; P:heart morphogenesis; IEA:Ensembl.
DR   GO; GO:0030902; P:hindbrain development; IEA:Ensembl.
DR   GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR   GO; GO:0001889; P:liver development; IEA:Ensembl.
DR   GO; GO:0030324; P:lung development; IEA:Ensembl.
DR   GO; GO:0007494; P:midgut development; IEA:Ensembl.
DR   GO; GO:0016331; P:morphogenesis of embryonic epithelium; IEA:Ensembl.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB.
DR   GO; GO:0014032; P:neural crest cell development; IEA:Ensembl.
DR   GO; GO:0021915; P:neural tube development; IMP:UniProtKB.
DR   GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
DR   GO; GO:0031016; P:pancreas development; IEA:Ensembl.
DR   GO; GO:0021983; P:pituitary gland development; IEA:Ensembl.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR   GO; GO:0009954; P:proximal/distal pattern formation; IEA:Ensembl.
DR   GO; GO:0001936; P:regulation of endothelial cell proliferation; IEA:Ensembl.
DR   GO; GO:0034097; P:response to cytokine; IDA:UniProtKB.
DR   GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR   GO; GO:0033189; P:response to vitamin A; IEA:Ensembl.
DR   GO; GO:0042574; P:retinal metabolic process; IEA:Ensembl.
DR   GO; GO:0002138; P:retinoic acid biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0042573; P:retinoic acid metabolic process; ISS:UniProtKB.
DR   GO; GO:0090242; P:retinoic acid receptor signaling pathway involved in somitogenesis; IEA:Ensembl.
DR   GO; GO:0042572; P:retinol metabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0035799; P:ureter maturation; IEA:Ensembl.
DR   GO; GO:0006776; P:vitamin A metabolic process; NAS:UniProtKB.
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; Alternative splicing; Cytoplasm; NAD; Oxidoreductase;
KW   Phosphoprotein; Polymorphism; Reference proteome.
FT   CHAIN           1..518
FT                   /note="Retinal dehydrogenase 2"
FT                   /id="PRO_0000056422"
FT   NP_BIND         184..186
FT                   /note="NAD"
FT                   /evidence="ECO:0000244|PDB:4X2Q, ECO:0000244|PDB:6ALJ,
FT                   ECO:0000244|PDB:6B5G, ECO:0000244|PDB:6B5H,
FT                   ECO:0000269|PubMed:29240402"
FT   NP_BIND         210..213
FT                   /note="NAD"
FT                   /evidence="ECO:0000244|PDB:4X2Q, ECO:0000244|PDB:6ALJ,
FT                   ECO:0000244|PDB:6B5G, ECO:0000244|PDB:6B5H,
FT                   ECO:0000269|PubMed:29240402"
FT   NP_BIND         264..266
FT                   /note="NAD"
FT                   /evidence="ECO:0000244|PDB:6ALJ, ECO:0000244|PDB:6B5G,
FT                   ECO:0000244|PDB:6B5H, ECO:0000269|PubMed:29240402"
FT   NP_BIND         366..370
FT                   /note="NAD"
FT                   /evidence="ECO:0000244|PDB:6ALJ, ECO:0000244|PDB:6B5G,
FT                   ECO:0000244|PDB:6B5H, ECO:0000269|PubMed:29240402"
FT   ACT_SITE        286
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT                   ECO:0000255|PROSITE-ProRule:PRU10008"
FT   ACT_SITE        320
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT                   ECO:0000255|PROSITE-ProRule:PRU10008,
FT                   ECO:0000269|PubMed:29240402"
FT   BINDING         417
FT                   /note="NAD"
FT                   /evidence="ECO:0000244|PDB:6ALJ, ECO:0000244|PDB:6B5G,
FT                   ECO:0000244|PDB:6B5H, ECO:0000269|PubMed:29240402"
FT   SITE            187
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         168
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         351
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   VAR_SEQ         1..96
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:9819382"
FT                   /id="VSP_047259"
FT   VAR_SEQ         1..39
FT                   /note="MTSSKIEMPGEVKADPAALMASLHLLPSPTPNLEIKYTK -> MKNQCETVW
FT                   LKSPIKLKL (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_044496"
FT   VAR_SEQ         229..266
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_017363"
FT   VARIANT         50
FT                   /note="E -> G (in dbSNP:rs34266719)"
FT                   /evidence="ECO:0000269|Ref.3"
FT                   /id="VAR_025439"
FT   VARIANT         110
FT                   /note="A -> V (in dbSNP:rs35365164)"
FT                   /evidence="ECO:0000269|Ref.3"
FT                   /id="VAR_025440"
FT   VARIANT         348
FT                   /note="V -> I (in dbSNP:rs4646626)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:17974005, ECO:0000269|PubMed:9819382,
FT                   ECO:0000269|Ref.3"
FT                   /id="VAR_025441"
FT   VARIANT         436
FT                   /note="E -> K (in dbSNP:rs34744827)"
FT                   /evidence="ECO:0000269|Ref.3"
FT                   /id="VAR_025442"
FT   CONFLICT        231
FT                   /note="F -> L (in Ref. 2; BAG64174)"
FT                   /evidence="ECO:0000305"
FT   STRAND          39..42
FT                   /evidence="ECO:0000244|PDB:6ALJ"
FT   STRAND          45..47
FT                   /evidence="ECO:0000244|PDB:6ALJ"
FT   STRAND          54..58
FT                   /evidence="ECO:0000244|PDB:6ALJ"
FT   TURN            60..62
FT                   /evidence="ECO:0000244|PDB:6ALJ"
FT   STRAND          65..70
FT                   /evidence="ECO:0000244|PDB:6ALJ"
FT   HELIX           74..87
FT                   /evidence="ECO:0000244|PDB:6ALJ"
FT   HELIX           93..96
FT                   /evidence="ECO:0000244|PDB:6ALJ"
FT   HELIX           99..115
FT                   /evidence="ECO:0000244|PDB:6ALJ"
FT   HELIX           117..128
FT                   /evidence="ECO:0000244|PDB:6ALJ"
FT   HELIX           132..137
FT                   /evidence="ECO:0000244|PDB:6ALJ"
FT   HELIX           139..151
FT                   /evidence="ECO:0000244|PDB:6ALJ"
FT   HELIX           154..156
FT                   /evidence="ECO:0000244|PDB:6ALJ"
FT   STRAND          159..162
FT                   /evidence="ECO:0000244|PDB:6ALJ"
FT   STRAND          165..176
FT                   /evidence="ECO:0000244|PDB:6ALJ"
FT   STRAND          178..183
FT                   /evidence="ECO:0000244|PDB:6ALJ"
FT   STRAND          186..188
FT                   /evidence="ECO:0000244|PDB:6ALJ"
FT   HELIX           189..202
FT                   /evidence="ECO:0000244|PDB:6ALJ"
FT   STRAND          206..210
FT                   /evidence="ECO:0000244|PDB:6ALJ"
FT   STRAND          213..215
FT                   /evidence="ECO:0000244|PDB:6B5I"
FT   HELIX           217..229
FT                   /evidence="ECO:0000244|PDB:6ALJ"
FT   STRAND          235..238
FT                   /evidence="ECO:0000244|PDB:6ALJ"
FT   TURN            243..245
FT                   /evidence="ECO:0000244|PDB:6ALJ"
FT   HELIX           246..251
FT                   /evidence="ECO:0000244|PDB:6ALJ"
FT   STRAND          258..263
FT                   /evidence="ECO:0000244|PDB:6ALJ"
FT   HELIX           265..277
FT                   /evidence="ECO:0000244|PDB:6ALJ"
FT   STRAND          282..286
FT                   /evidence="ECO:0000244|PDB:6ALJ"
FT   STRAND          292..295
FT                   /evidence="ECO:0000244|PDB:6ALJ"
FT   HELIX           301..313
FT                   /evidence="ECO:0000244|PDB:6ALJ"
FT   HELIX           314..317
FT                   /evidence="ECO:0000244|PDB:6ALJ"
FT   STRAND          325..329
FT                   /evidence="ECO:0000244|PDB:6ALJ"
FT   HELIX           330..346
FT                   /evidence="ECO:0000244|PDB:6ALJ"
FT   HELIX           365..380
FT                   /evidence="ECO:0000244|PDB:6ALJ"
FT   STRAND          384..387
FT                   /evidence="ECO:0000244|PDB:6ALJ"
FT   STRAND          393..396
FT                   /evidence="ECO:0000244|PDB:6ALJ"
FT   STRAND          402..406
FT                   /evidence="ECO:0000244|PDB:6ALJ"
FT   HELIX           412..415
FT                   /evidence="ECO:0000244|PDB:6ALJ"
FT   STRAND          420..428
FT                   /evidence="ECO:0000244|PDB:6ALJ"
FT   HELIX           431..439
FT                   /evidence="ECO:0000244|PDB:6ALJ"
FT   STRAND          441..450
FT                   /evidence="ECO:0000244|PDB:6ALJ"
FT   HELIX           454..463
FT                   /evidence="ECO:0000244|PDB:6ALJ"
FT   STRAND          466..472
FT                   /evidence="ECO:0000244|PDB:6ALJ"
FT   STRAND          479..481
FT                   /evidence="ECO:0000244|PDB:6B5I"
FT   STRAND          490..492
FT                   /evidence="ECO:0000244|PDB:6ALJ"
FT   HELIX           498..503
FT                   /evidence="ECO:0000244|PDB:6ALJ"
FT   STRAND          504..512
FT                   /evidence="ECO:0000244|PDB:6ALJ"
SQ   SEQUENCE   518 AA;  56724 MW;  AAEE7A886951373F CRC64;
     MTSSKIEMPG EVKADPAALM ASLHLLPSPT PNLEIKYTKI FINNEWQNSE SGRVFPVYNP
     ATGEQVCEVQ EADKADIDKA VQAARLAFSL GSVWRRMDAS ERGRLLDKLA DLVERDRAVL
     ATMESLNGGK PFLQAFYVDL QGVIKTFRYY AGWADKIHGM TIPVDGDYFT FTRHEPIGVC
     GQIIPWNFPL LMFAWKIAPA LCCGNTVVIK PAEQTPLSAL YMGALIKEAG FPPGVINILP
     GYGPTAGAAI ASHIGIDKIA FTGSTEVGKL IQEAAGRSNL KRVTLELGGK SPNIIFADAD
     LDYAVEQAHQ GVFFNQGQCC TAGSRIFVEE SIYEEFVRRS VERAKRRVVG SPFDPTTEQG
     PQIDKKQYNK ILELIQSGVA EGAKLECGGK GLGRKGFFIE PTVFSNVTDD MRIAKEEIFG
     PVQEILRFKT MDEVIERANN SDFGLVAAVF TNDINKALTV SSAMQAGTVW INCYNALNAQ
     SPFGGFKMSG NGREMGEFGL REYSEVKTVT VKIPQKNS
//
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