AL1A2_HUMAN
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 03-AUG-2022, entry version 192.
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:0007744|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:0007744|PDB:6ALJ, ECO:0007744|PDB:6B5G, ECO:0007744|PDB:6B5H, ECO:0007744|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/";
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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 AlphaFoldDB; O94788; -.
DR SMR; O94788; -.
DR BioGRID; 114379; 75.
DR IntAct; O94788; 7.
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; 377 antibodies from 32 providers.
DR DNASU; 8854; -.
DR Ensembl; ENST00000249750.9; ENSP00000249750.4; ENSG00000128918.15. [O94788-1]
DR Ensembl; ENST00000347587.7; ENSP00000309623.3; ENSG00000128918.15. [O94788-2]
DR Ensembl; ENST00000537372.5; ENSP00000438296.1; ENSG00000128918.15. [O94788-3]
DR Ensembl; ENST00000559517.5; ENSP00000453408.1; ENSG00000128918.15. [O94788-4]
DR GeneID; 8854; -.
DR KEGG; hsa:8854; -.
DR MANE-Select; ENST00000249750.9; ENSP00000249750.4; NM_003888.4; NP_003879.2.
DR UCSC; uc002aew.4; human. [O94788-1]
DR CTD; 8854; -.
DR DisGeNET; 8854; -.
DR GeneCards; ALDH1A2; -.
DR HGNC; HGNC:15472; ALDH1A2.
DR HPA; ENSG00000128918; Tissue enhanced (endometrium, fallopian tube).
DR MIM; 603687; gene.
DR neXtProt; NX_O94788; -.
DR OpenTargets; ENSG00000128918; -.
DR PharmGKB; PA24693; -.
DR VEuPathDB; HostDB:ENSG00000128918; -.
DR eggNOG; KOG2450; Eukaryota.
DR GeneTree; ENSGT00940000158898; -.
DR HOGENOM; CLU_005391_0_0_1; -.
DR InParanoid; O94788; -.
DR OMA; RKAFEKW; -.
DR OrthoDB; 153834at2759; -.
DR PhylomeDB; O94788; -.
DR TreeFam; TF300455; -.
DR BioCyc; MetaCyc:HS05232-MON; -.
DR BRENDA; 1.2.1.36; 2681.
DR PathwayCommons; O94788; -.
DR Reactome; R-HSA-5365859; RA biosynthesis pathway.
DR SignaLink; O94788; -.
DR SIGNOR; O94788; -.
DR UniPathway; UPA00912; -.
DR BioGRID-ORCS; 8854; 8 hits in 1082 CRISPR screens.
DR ChiTaRS; ALDH1A2; human.
DR GeneWiki; ALDH1A2; -.
DR GenomeRNAi; 8854; -.
DR Pharos; O94788; Tchem.
DR PRO; PR:O94788; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; O94788; protein.
DR Bgee; ENSG00000128918; Expressed in germinal epithelium of ovary and 152 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:0008283; P:cell population proliferation; 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:1905562; P:regulation of vascular 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; Lipid metabolism; NAD;
KW Oxidoreductase; Phosphoprotein; Reference proteome.
FT CHAIN 1..518
FT /note="Retinal dehydrogenase 2"
FT /id="PRO_0000056422"
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 184..186
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:29240402,
FT ECO:0007744|PDB:4X2Q, ECO:0007744|PDB:6ALJ,
FT ECO:0007744|PDB:6B5G, ECO:0007744|PDB:6B5H"
FT BINDING 210..213
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:29240402,
FT ECO:0007744|PDB:4X2Q, ECO:0007744|PDB:6ALJ,
FT ECO:0007744|PDB:6B5G, ECO:0007744|PDB:6B5H"
FT BINDING 264..266
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:29240402,
FT ECO:0007744|PDB:6ALJ, ECO:0007744|PDB:6B5G,
FT ECO:0007744|PDB:6B5H"
FT BINDING 366..370
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:29240402,
FT ECO:0007744|PDB:6ALJ, ECO:0007744|PDB:6B5G,
FT ECO:0007744|PDB:6B5H"
FT BINDING 417
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:29240402,
FT ECO:0007744|PDB:6ALJ, ECO:0007744|PDB:6B5G,
FT ECO:0007744|PDB:6B5H"
FT SITE 187
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MOD_RES 168
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|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:0007829|PDB:6ALJ"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:6ALJ"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:6ALJ"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:6ALJ"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:6ALJ"
FT HELIX 74..87
FT /evidence="ECO:0007829|PDB:6ALJ"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:6ALJ"
FT HELIX 99..115
FT /evidence="ECO:0007829|PDB:6ALJ"
FT HELIX 117..128
FT /evidence="ECO:0007829|PDB:6ALJ"
FT HELIX 132..137
FT /evidence="ECO:0007829|PDB:6ALJ"
FT HELIX 139..151
FT /evidence="ECO:0007829|PDB:6ALJ"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:6ALJ"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:6ALJ"
FT STRAND 165..176
FT /evidence="ECO:0007829|PDB:6ALJ"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:6ALJ"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:6ALJ"
FT HELIX 189..202
FT /evidence="ECO:0007829|PDB:6ALJ"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:6ALJ"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:6B5I"
FT HELIX 217..229
FT /evidence="ECO:0007829|PDB:6ALJ"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:6ALJ"
FT TURN 243..245
FT /evidence="ECO:0007829|PDB:6ALJ"
FT HELIX 246..251
FT /evidence="ECO:0007829|PDB:6ALJ"
FT STRAND 258..263
FT /evidence="ECO:0007829|PDB:6ALJ"
FT HELIX 265..277
FT /evidence="ECO:0007829|PDB:6ALJ"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:6ALJ"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:6ALJ"
FT HELIX 301..313
FT /evidence="ECO:0007829|PDB:6ALJ"
FT HELIX 314..317
FT /evidence="ECO:0007829|PDB:6ALJ"
FT STRAND 325..329
FT /evidence="ECO:0007829|PDB:6ALJ"
FT HELIX 330..346
FT /evidence="ECO:0007829|PDB:6ALJ"
FT HELIX 365..380
FT /evidence="ECO:0007829|PDB:6ALJ"
FT STRAND 384..387
FT /evidence="ECO:0007829|PDB:6ALJ"
FT STRAND 393..396
FT /evidence="ECO:0007829|PDB:6ALJ"
FT STRAND 402..406
FT /evidence="ECO:0007829|PDB:6ALJ"
FT HELIX 412..415
FT /evidence="ECO:0007829|PDB:6ALJ"
FT STRAND 420..428
FT /evidence="ECO:0007829|PDB:6ALJ"
FT HELIX 431..439
FT /evidence="ECO:0007829|PDB:6ALJ"
FT STRAND 441..450
FT /evidence="ECO:0007829|PDB:6ALJ"
FT HELIX 454..463
FT /evidence="ECO:0007829|PDB:6ALJ"
FT STRAND 466..472
FT /evidence="ECO:0007829|PDB:6ALJ"
FT STRAND 479..481
FT /evidence="ECO:0007829|PDB:6B5I"
FT STRAND 490..492
FT /evidence="ECO:0007829|PDB:6ALJ"
FT HELIX 498..503
FT /evidence="ECO:0007829|PDB:6ALJ"
FT STRAND 504..512
FT /evidence="ECO:0007829|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
