GPDA_HUMAN
ID GPDA_HUMAN Reviewed; 349 AA.
AC P21695; F8W1L5; Q8N1B0;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 4.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)], cytoplasmic {ECO:0000305};
DE Short=GPD-C;
DE Short=GPDH-C;
DE EC=1.1.1.8 {ECO:0000269|PubMed:7772607};
GN Name=GPD1 {ECO:0000312|HGNC:HGNC:4455};
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] (ISOFORM 1), VARIANT PRO-113, CATALYTIC
RP ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=7772607; DOI=10.1016/0167-4781(95)00069-s;
RA Menaya J., Gonzalez-Manchon C., Parrilla R., Ayuso M.S.;
RT "Molecular cloning, sequencing and expression of a cDNA encoding a human
RT liver NAD-dependent alpha-glycerol-3-phosphate dehydrogenase.";
RL Biochim. Biophys. Acta 1262:91-94(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Macrophage;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14.
RC TISSUE=Fetal liver;
RX PubMed=2398890; DOI=10.1128/mcb.10.10.5244-5256.1990;
RA Gwynn B., Lyford K.L., Birkenmeier E.H.;
RT "Sequence conservation and structural organization of the glycerol-3-
RT phosphate dehydrogenase promoter in mice and humans.";
RL Mol. Cell. Biol. 10:5244-5256(1990).
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 INVOLVEMENT IN HTGTI, AND VARIANTS VAL-54; LYS-124; ALA-197 AND ILE-223.
RX PubMed=22226083; DOI=10.1016/j.ajhg.2011.11.028;
RA Basel-Vanagaite L., Zevit N., Zahav A.H., Guo L., Parathath S.,
RA Pasmanik-Chor M., McIntyre A.D., Wang J., Albin-Kaplanski A., Hartman C.,
RA Marom D., Zeharia A., Badir A., Shoerman O., Simon A.J., Rechavi G.,
RA Shohat M., Hegele R.A., Fisher E.A., Shamir R.;
RT "Transient infantile hypertriglyceridemia, fatty liver, and hepatic
RT fibrosis caused by mutated GPD1, encoding glycerol-3-phosphate
RT dehydrogenase 1.";
RL Am. J. Hum. Genet. 90:49-60(2012).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, AND IDENTIFICATION BY
RP 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 [9] {ECO:0007744|PDB:6E8Y, ECO:0007744|PDB:6E8Z}
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH NAD, SUBUNIT, AND
RP ACTIVITY REGULATION.
RX PubMed=16460752; DOI=10.1016/j.jmb.2005.12.074;
RA Ou X., Ji C., Han X., Zhao X., Li X., Mao Y., Wong L.-L., Bartlam M.,
RA Rao Z.;
RT "Crystal structures of human glycerol 3-phosphate dehydrogenase 1 (GPD1).";
RL J. Mol. Biol. 357:858-869(2006).
RN [10]
RP VARIANT HTGTI PRO-229.
RX PubMed=24549054; DOI=10.1038/ejhg.2014.8;
RA Joshi M., Eagan J., Desai N.K., Newton S.A., Towne M.C., Marinakis N.S.,
RA Esteves K.M., De Ferranti S., Bennett M.J., McIntyre A., Beggs A.H.,
RA Berry G.T., Agrawal P.B.;
RT "A compound heterozygous mutation in GPD1 causes hepatomegaly,
RT steatohepatitis, and hypertriglyceridemia.";
RL Eur. J. Hum. Genet. 22:1229-1232(2014).
CC -!- FUNCTION: Has glycerol-3-phosphate dehydrogenase activity.
CC {ECO:0000269|PubMed:7772607}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate
CC + H(+) + NADH; Xref=Rhea:RHEA:11092, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642,
CC ChEBI:CHEBI:57945; EC=1.1.1.8; Evidence={ECO:0000269|PubMed:7772607};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11093;
CC Evidence={ECO:0000305|PubMed:7772607};
CC -!- ACTIVITY REGULATION: Inhibited by zinc ions and sulfate.
CC {ECO:0000269|PubMed:16460752}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=92 uM for glycerol 3-phosphate {ECO:0000269|PubMed:7772607};
CC KM=140 uM for NAD {ECO:0000269|PubMed:7772607};
CC KM=1070 mM for NADP {ECO:0000269|PubMed:7772607};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16460752}.
CC -!- INTERACTION:
CC P21695; B3EWG5: FAM25C; NbExp=3; IntAct=EBI-713346, EBI-14240149;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7772607}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P21695-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P21695-2; Sequence=VSP_045999;
CC -!- TISSUE SPECIFICITY: Expressed in liver (at protein level).
CC {ECO:0000269|PubMed:7772607}.
CC -!- DISEASE: Hypertriglyceridemia, transient infantile (HTGTI)
CC [MIM:614480]: An autosomal recessive disorder characterized by onset of
CC moderate to severe transient hypertriglyceridemia in infancy that
CC normalizes with age. The hypertriglyceridemia is associated with
CC hepatomegaly, moderately elevated transaminases, persistent fatty
CC liver, and the development of hepatic fibrosis.
CC {ECO:0000269|PubMed:22226083, ECO:0000269|PubMed:24549054}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; L34041; AAA92863.1; -; mRNA.
DR EMBL; AK130162; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC025154; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC032234; AAH32234.1; -; mRNA.
DR EMBL; M36917; AAA35925.1; -; Genomic_DNA.
DR CCDS; CCDS58229.1; -. [P21695-2]
DR CCDS; CCDS8799.1; -. [P21695-1]
DR PIR; S55920; S55920.
DR RefSeq; NP_001244128.1; NM_001257199.1. [P21695-2]
DR RefSeq; NP_005267.2; NM_005276.3. [P21695-1]
DR PDB; 1WPQ; X-ray; 2.50 A; A/B=1-349.
DR PDB; 1X0V; X-ray; 2.30 A; A/B=1-349.
DR PDB; 1X0X; X-ray; 2.75 A; A=1-349.
DR PDB; 6E8Y; X-ray; 1.85 A; A/B=1-349.
DR PDB; 6E8Z; X-ray; 2.10 A; A/B=1-349.
DR PDB; 6E90; X-ray; 2.05 A; A/B/C/D=1-349.
DR PDB; 6PYP; X-ray; 1.95 A; A/B=1-349.
DR PDBsum; 1WPQ; -.
DR PDBsum; 1X0V; -.
DR PDBsum; 1X0X; -.
DR PDBsum; 6E8Y; -.
DR PDBsum; 6E8Z; -.
DR PDBsum; 6E90; -.
DR PDBsum; 6PYP; -.
DR AlphaFoldDB; P21695; -.
DR SMR; P21695; -.
DR BioGRID; 109080; 21.
DR IntAct; P21695; 8.
DR STRING; 9606.ENSP00000301149; -.
DR DrugBank; DB00331; Metformin.
DR DrugBank; DB00157; NADH.
DR SwissLipids; SLP:000000645; -.
DR iPTMnet; P21695; -.
DR PhosphoSitePlus; P21695; -.
DR BioMuta; GPD1; -.
DR DMDM; 134047785; -.
DR jPOST; P21695; -.
DR MassIVE; P21695; -.
DR MaxQB; P21695; -.
DR PaxDb; P21695; -.
DR PeptideAtlas; P21695; -.
DR PRIDE; P21695; -.
DR ProteomicsDB; 29645; -.
DR ProteomicsDB; 53890; -. [P21695-1]
DR Antibodypedia; 26155; 345 antibodies from 33 providers.
DR DNASU; 2819; -.
DR Ensembl; ENST00000301149.8; ENSP00000301149.3; ENSG00000167588.13. [P21695-1]
DR Ensembl; ENST00000548814.1; ENSP00000446768.1; ENSG00000167588.13. [P21695-2]
DR GeneID; 2819; -.
DR KEGG; hsa:2819; -.
DR MANE-Select; ENST00000301149.8; ENSP00000301149.3; NM_005276.4; NP_005267.2.
DR UCSC; uc001rvz.5; human. [P21695-1]
DR CTD; 2819; -.
DR DisGeNET; 2819; -.
DR GeneCards; GPD1; -.
DR HGNC; HGNC:4455; GPD1.
DR HPA; ENSG00000167588; Tissue enhanced (adipose tissue, skeletal muscle).
DR MalaCards; GPD1; -.
DR MIM; 138420; gene.
DR MIM; 614480; phenotype.
DR neXtProt; NX_P21695; -.
DR OpenTargets; ENSG00000167588; -.
DR Orphanet; 300293; Transient infantile hypertriglyceridemia and hepatosteatosis.
DR PharmGKB; PA28836; -.
DR VEuPathDB; HostDB:ENSG00000167588; -.
DR eggNOG; KOG2711; Eukaryota.
DR GeneTree; ENSGT00390000003114; -.
DR HOGENOM; CLU_033449_2_2_1; -.
DR InParanoid; P21695; -.
DR OMA; NRMFGNM; -.
DR PhylomeDB; P21695; -.
DR TreeFam; TF300836; -.
DR BioCyc; MetaCyc:HS09586-MON; -.
DR BRENDA; 1.1.1.8; 2681.
DR PathwayCommons; P21695; -.
DR Reactome; R-HSA-1483166; Synthesis of PA.
DR SABIO-RK; P21695; -.
DR SignaLink; P21695; -.
DR BioGRID-ORCS; 2819; 14 hits in 1075 CRISPR screens.
DR ChiTaRS; GPD1; human.
DR EvolutionaryTrace; P21695; -.
DR GenomeRNAi; 2819; -.
DR Pharos; P21695; Tbio.
DR PRO; PR:P21695; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P21695; protein.
DR Bgee; ENSG00000167588; Expressed in subcutaneous adipose tissue and 150 other tissues.
DR ExpressionAtlas; P21695; baseline and differential.
DR Genevisible; P21695; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:Ensembl.
DR GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase [NAD+] activity; IBA:GO_Central.
DR GO; GO:0051287; F:NAD binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR GO; GO:0006094; P:gluconeogenesis; IEA:Ensembl.
DR GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:InterPro.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0046486; P:glycerolipid metabolic process; IEA:Ensembl.
DR GO; GO:0006127; P:glycerophosphate shuttle; IEA:Ensembl.
DR GO; GO:0006116; P:NADH oxidation; IBA:GO_Central.
DR GO; GO:0045821; P:positive regulation of glycolytic process; IEA:Ensembl.
DR Gene3D; 1.10.1040.10; -; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR006168; G3P_DH_NAD-dep.
DR InterPro; IPR006109; G3P_DH_NAD-dep_C.
DR InterPro; IPR017751; G3P_DH_NAD-dep_euk.
DR InterPro; IPR011128; G3P_DH_NAD-dep_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF07479; NAD_Gly3P_dh_C; 1.
DR Pfam; PF01210; NAD_Gly3P_dh_N; 1.
DR PIRSF; PIRSF000114; Glycerol-3-P_dh; 1.
DR PRINTS; PR00077; GPDHDRGNASE.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR03376; glycerol3P_DH; 1.
DR PROSITE; PS00957; NAD_G3PDH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Disease variant; NAD;
KW Oxidoreductase; Phosphoprotein; Reference proteome.
FT CHAIN 1..349
FT /note="Glycerol-3-phosphate dehydrogenase [NAD(+)],
FT cytoplasmic"
FT /id="PRO_0000138079"
FT ACT_SITE 204
FT /note="Proton acceptor"
FT /evidence="ECO:0000305"
FT BINDING 10..15
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:16460752"
FT BINDING 41
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:16460752"
FT BINDING 97
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:16460752"
FT BINDING 120
FT /ligand="substrate"
FT BINDING 153
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:16460752"
FT BINDING 269..270
FT /ligand="substrate"
FT BINDING 269
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:16460752"
FT BINDING 296
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:16460752"
FT BINDING 298
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:16460752"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 289
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P13707"
FT MOD_RES 326
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O35077"
FT VAR_SEQ 74..96
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045999"
FT VARIANT 54
FT /note="I -> V (in dbSNP:rs2232202)"
FT /evidence="ECO:0000269|PubMed:22226083"
FT /id="VAR_029492"
FT VARIANT 113
FT /note="A -> P (in dbSNP:rs1128867)"
FT /evidence="ECO:0000269|PubMed:7772607"
FT /id="VAR_029493"
FT VARIANT 124
FT /note="E -> K (in dbSNP:rs34783513)"
FT /evidence="ECO:0000269|PubMed:22226083"
FT /id="VAR_067425"
FT VARIANT 197
FT /note="V -> A (in dbSNP:rs2232207)"
FT /evidence="ECO:0000269|PubMed:22226083"
FT /id="VAR_049220"
FT VARIANT 223
FT /note="T -> I (in dbSNP:rs200251017)"
FT /evidence="ECO:0000269|PubMed:22226083"
FT /id="VAR_067426"
FT VARIANT 229
FT /note="R -> P (in HTGTI; dbSNP:rs199673455)"
FT /evidence="ECO:0000269|PubMed:24549054"
FT /id="VAR_071967"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:6E8Y"
FT HELIX 13..28
FT /evidence="ECO:0007829|PDB:6E8Y"
FT STRAND 32..39
FT /evidence="ECO:0007829|PDB:6E8Y"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:1X0V"
FT HELIX 51..57
FT /evidence="ECO:0007829|PDB:6E8Y"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:6E8Y"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:6E8Y"
FT HELIX 79..83
FT /evidence="ECO:0007829|PDB:6E8Y"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:6E8Y"
FT HELIX 95..105
FT /evidence="ECO:0007829|PDB:6E8Y"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:6E8Y"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:6E8Y"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:6E8Y"
FT HELIX 132..140
FT /evidence="ECO:0007829|PDB:6E8Y"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:6E8Y"
FT HELIX 153..157
FT /evidence="ECO:0007829|PDB:6E8Y"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:6E8Y"
FT HELIX 171..181
FT /evidence="ECO:0007829|PDB:6E8Y"
FT STRAND 186..192
FT /evidence="ECO:0007829|PDB:6E8Y"
FT HELIX 194..216
FT /evidence="ECO:0007829|PDB:6E8Y"
FT HELIX 221..242
FT /evidence="ECO:0007829|PDB:6E8Y"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:1X0V"
FT HELIX 249..253
FT /evidence="ECO:0007829|PDB:6E8Y"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:6E8Y"
FT HELIX 258..266
FT /evidence="ECO:0007829|PDB:6E8Y"
FT HELIX 269..280
FT /evidence="ECO:0007829|PDB:6E8Y"
FT HELIX 284..292
FT /evidence="ECO:0007829|PDB:6E8Y"
FT HELIX 298..312
FT /evidence="ECO:0007829|PDB:6E8Y"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:6E8Y"
FT HELIX 320..330
FT /evidence="ECO:0007829|PDB:6E8Y"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:6E8Y"
FT HELIX 339..342
FT /evidence="ECO:0007829|PDB:6E8Y"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:6E8Y"
SQ SEQUENCE 349 AA; 37568 MW; CE7B7681103076EF CRC64;
MASKKVCIVG SGNWGSAIAK IVGGNAAQLA QFDPRVTMWV FEEDIGGKKL TEIINTQHEN
VKYLPGHKLP PNVVAVPDVV QAAEDADILI FVVPHQFIGK ICDQLKGHLK ANATGISLIK
GVDEGPNGLK LISEVIGERL GIPMSVLMGA NIASEVADEK FCETTIGCKD PAQGQLLKEL
MQTPNFRITV VQEVDTVEIC GALKNVVAVG AGFCDGLGFG DNTKAAVIRL GLMEMIAFAK
LFCSGPVSSA TFLESCGVAD LITTCYGGRN RKVAEAFART GKSIEQLEKE LLNGQKLQGP
ETARELYSIL QHKGLVDKFP LFMAVYKVCY EGQPVGEFIH CLQNHPEHM
