NNTM_HUMAN
ID NNTM_HUMAN Reviewed; 1086 AA.
AC Q13423; Q16796; Q2TB60; Q8N3V4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 3.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=NAD(P) transhydrogenase, mitochondrial;
DE EC=7.1.1.1 {ECO:0000250|UniProtKB:Q2RSB2};
DE AltName: Full=Nicotinamide nucleotide transhydrogenase;
DE AltName: Full=Pyridine nucleotide transhydrogenase;
DE Flags: Precursor;
GN Name=NNT;
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].
RX PubMed=9524818; DOI=10.3109/10425179709034058;
RA Ware J., Zieger B.;
RT "Cloning and deduced amino acid sequence of human nicotinamide nucleotide
RT transhydrogenase.";
RL DNA Seq. 7:369-374(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RX PubMed=8616157; DOI=10.1016/0005-2728(95)00159-x;
RA Lagberg E.M., Betsholtz C., Rydstrom J.;
RT "The cDNA sequence of proton-pumping nicotinamide nucleotide
RT transhydrogenase from man and mouse.";
RL Biochim. Biophys. Acta 1273:203-205(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70 AND LYS-397, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
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 FUNCTION, TISSUE SPECIFICITY, AND VARIANTS GCCD4 ASN-193; ALA-357; PRO-365;
RP LEU-437; VAL-533; ARG-664; ARG-678; ASP-862; PRO-977; PRO-1008 AND
RP LYS-1009.
RX PubMed=22634753; DOI=10.1038/ng.2299;
RA Meimaridou E., Kowalczyk J., Guasti L., Hughes C.R., Wagner F.,
RA Frommolt P., Nurnberg P., Mann N.P., Banerjee R., Saka H.N., Chapple J.P.,
RA King P.J., Clark A.J., Metherell L.A.;
RT "Mutations in NNT encoding nicotinamide nucleotide transhydrogenase cause
RT familial glucocorticoid deficiency.";
RL Nat. Genet. 44:740-742(2012).
RN [8]
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 [9]
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 [10]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 880-1086 IN COMPLEX WITH NADP.
RX PubMed=10673423; DOI=10.1016/s0969-2126(00)00075-7;
RA White S.A., Peake S.J., McSweeney S., Leonard G., Cotton N.P.J.,
RA Jackson J.B.;
RT "The high-resolution structure of the NADP(H)-binding component (dIII) of
RT proton-translocating transhydrogenase from human heart mitochondria.";
RL Structure 8:1-12(2000).
RN [11] {ECO:0007744|PDB:1PT9}
RP X-RAY CRYSTALLOGRAPHY (2.42 ANGSTROMS) OF 880-1086 IN COMPLEX WITH
RP SUBSTRATE ANALOG.
RX PubMed=12791694; DOI=10.1074/jbc.m303061200;
RA Singh A., Venning J.D., Quirk P.G., van Boxel G.I., Rodrigues D.J.,
RA White S.A., Jackson J.B.;
RT "Interactions between transhydrogenase and thio-nicotinamide Analogues of
RT NAD(H) and NADP(H) underline the importance of nucleotide conformational
RT changes in coupling to proton translocation.";
RL J. Biol. Chem. 278:33208-33216(2003).
RN [12] {ECO:0007744|PDB:1U31}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 880-1086 IN COMPLEX WITH NADP.
RX PubMed=15323555; DOI=10.1021/bi0497594;
RA Mather O.C., Singh A., van Boxel G.I., White S.A., Jackson J.B.;
RT "Active-site conformational changes associated with hydride transfer in
RT proton-translocating transhydrogenase.";
RL Biochemistry 43:10952-10964(2004).
CC -!- FUNCTION: The transhydrogenation between NADH and NADP is coupled to
CC respiration and ATP hydrolysis and functions as a proton pump across
CC the membrane (By similarity). May play a role in reactive oxygen
CC species (ROS) detoxification in the adrenal gland (PubMed:22634753).
CC {ECO:0000250|UniProtKB:P07001, ECO:0000269|PubMed:22634753}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) + NAD(+) + NADPH = H(+)(out) + NADH + NADP(+);
CC Xref=Rhea:RHEA:47992, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:57945, ChEBI:CHEBI:58349; EC=7.1.1.1;
CC Evidence={ECO:0000250|UniProtKB:Q2RSB2};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P11024}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}; Matrix side {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Widely expressed with expression most readily
CC detectable in adrenal, heart, kidney, thyroid and adipose tissues.
CC {ECO:0000269|PubMed:22634753}.
CC -!- DISEASE: Glucocorticoid deficiency 4 with or without mineralocorticoid
CC deficiency (GCCD4) [MIM:614736]: A form of glucocorticoid deficiency, a
CC rare autosomal recessive disorder characterized by resistance to ACTH
CC action on the adrenal cortex, adrenal insufficiency and an inability of
CC the adrenal cortex to produce cortisol. It usually presents in the
CC neonatal period or in early childhood with episodes of hypoglycemia and
CC other symptoms related to cortisol deficiency, including failure to
CC thrive, recurrent illnesses or infections, convulsions, and shock. In a
CC small number of patients hypoglycemia can be sufficiently severe and
CC persistent that it leads to serious long-term neurological damage or
CC death. The diagnosis is readily confirmed with a low plasma cortisol
CC measurement in the presence of an elevated ACTH level, and normal
CC aldosterone and plasma renin measurements.
CC {ECO:0000269|PubMed:22634753}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: In the N-terminal section; belongs to the AlaDH/PNT family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the PNT beta subunit
CC family. {ECO:0000305}.
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DR EMBL; U40490; AAC51914.1; -; mRNA.
DR EMBL; Z50101; CAA90428.1; -; mRNA.
DR EMBL; AL831822; CAD38536.1; -; mRNA.
DR EMBL; BC110543; AAI10544.1; -; mRNA.
DR CCDS; CCDS3949.1; -.
DR PIR; G02257; G02257.
DR RefSeq; NP_036475.3; NM_012343.3.
DR RefSeq; NP_892022.2; NM_182977.2.
DR RefSeq; XP_005248331.1; XM_005248274.4.
DR RefSeq; XP_011512303.1; XM_011514001.2.
DR RefSeq; XP_016864782.1; XM_017009293.1.
DR PDB; 1DJL; X-ray; 2.00 A; A/B=880-1086.
DR PDB; 1PT9; X-ray; 2.42 A; A/B=880-1086.
DR PDB; 1U31; X-ray; 2.20 A; A/B=880-1086.
DR PDBsum; 1DJL; -.
DR PDBsum; 1PT9; -.
DR PDBsum; 1U31; -.
DR AlphaFoldDB; Q13423; -.
DR SMR; Q13423; -.
DR BioGRID; 117076; 178.
DR IntAct; Q13423; 33.
DR MINT; Q13423; -.
DR STRING; 9606.ENSP00000264663; -.
DR DrugBank; DB01763; 7-thionicotinamide-adenine-dinucleotide phosphate.
DR DrugBank; DB00157; NADH.
DR DrugBank; DB03461; Nicotinamide adenine dinucleotide phosphate.
DR DrugBank; DB09092; Xanthinol.
DR CarbonylDB; Q13423; -.
DR iPTMnet; Q13423; -.
DR MetOSite; Q13423; -.
DR PhosphoSitePlus; Q13423; -.
DR SwissPalm; Q13423; -.
DR BioMuta; NNT; -.
DR DMDM; 51338801; -.
DR EPD; Q13423; -.
DR jPOST; Q13423; -.
DR MassIVE; Q13423; -.
DR MaxQB; Q13423; -.
DR PaxDb; Q13423; -.
DR PeptideAtlas; Q13423; -.
DR PRIDE; Q13423; -.
DR ProteomicsDB; 59408; -.
DR Antibodypedia; 1369; 163 antibodies from 29 providers.
DR DNASU; 23530; -.
DR Ensembl; ENST00000264663.9; ENSP00000264663.5; ENSG00000112992.18.
DR Ensembl; ENST00000344920.9; ENSP00000343873.4; ENSG00000112992.18.
DR Ensembl; ENST00000653251.1; ENSP00000499281.1; ENSG00000112992.18.
DR Ensembl; ENST00000656666.1; ENSP00000499249.1; ENSG00000112992.18.
DR Ensembl; ENST00000662525.1; ENSP00000499639.1; ENSG00000112992.18.
DR Ensembl; ENST00000669601.1; ENSP00000499527.1; ENSG00000112992.18.
DR Ensembl; ENST00000670904.1; ENSP00000499611.1; ENSG00000112992.18.
DR Ensembl; ENST00000671668.1; ENSP00000499494.1; ENSG00000112992.18.
DR GeneID; 23530; -.
DR KEGG; hsa:23530; -.
DR MANE-Select; ENST00000344920.9; ENSP00000343873.4; NM_182977.3; NP_892022.2.
DR UCSC; uc003joe.4; human.
DR CTD; 23530; -.
DR DisGeNET; 23530; -.
DR GeneCards; NNT; -.
DR HGNC; HGNC:7863; NNT.
DR HPA; ENSG00000112992; Tissue enhanced (skeletal muscle, tongue).
DR MalaCards; NNT; -.
DR MIM; 607878; gene.
DR MIM; 614736; phenotype.
DR neXtProt; NX_Q13423; -.
DR OpenTargets; ENSG00000112992; -.
DR Orphanet; 361; Familial glucocorticoid deficiency.
DR PharmGKB; PA31667; -.
DR VEuPathDB; HostDB:ENSG00000112992; -.
DR eggNOG; ENOG502QQ0A; Eukaryota.
DR GeneTree; ENSGT00390000004624; -.
DR HOGENOM; CLU_003376_1_0_1; -.
DR InParanoid; Q13423; -.
DR OMA; NPAFTTM; -.
DR OrthoDB; 1152704at2759; -.
DR PhylomeDB; Q13423; -.
DR TreeFam; TF300636; -.
DR BioCyc; MetaCyc:HS03639-MON; -.
DR BRENDA; 1.6.1.2; 2681.
DR BRENDA; 7.1.1.1; 2681.
DR PathwayCommons; Q13423; -.
DR Reactome; R-HSA-71403; Citric acid cycle (TCA cycle).
DR SignaLink; Q13423; -.
DR BioGRID-ORCS; 23530; 12 hits in 1084 CRISPR screens.
DR ChiTaRS; NNT; human.
DR EvolutionaryTrace; Q13423; -.
DR GeneWiki; NNT_(gene); -.
DR GenomeRNAi; 23530; -.
DR Pharos; Q13423; Tbio.
DR PRO; PR:Q13423; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q13423; protein.
DR Bgee; ENSG00000112992; Expressed in heart right ventricle and 192 other tissues.
DR ExpressionAtlas; Q13423; baseline and differential.
DR Genevisible; Q13423; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:UniProtKB.
DR GO; GO:0005746; C:mitochondrial respirasome; TAS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:LIFEdb.
DR GO; GO:0051287; F:NAD binding; IBA:GO_Central.
DR GO; GO:0003957; F:NAD(P)+ transhydrogenase (B-specific) activity; TAS:UniProtKB.
DR GO; GO:0008746; F:NAD(P)+ transhydrogenase activity; IBA:GO_Central.
DR GO; GO:0050661; F:NADP binding; IDA:UniProtKB.
DR GO; GO:0006740; P:NADPH regeneration; IBA:GO_Central.
DR GO; GO:1902600; P:proton transmembrane transport; TAS:UniProtKB.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:UniProtKB.
DR GO; GO:0006099; P:tricarboxylic acid cycle; TAS:UniProtKB.
DR InterPro; IPR008143; Ala_DH/PNT_CS2.
DR InterPro; IPR008142; AlaDH/PNT_CS1.
DR InterPro; IPR007886; AlaDH/PNT_N.
DR InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR026255; NADP_transhyd_a.
DR InterPro; IPR024605; NADP_transhyd_a_C.
DR InterPro; IPR034300; PNTB-like.
DR Pfam; PF01262; AlaDh_PNT_C; 1.
DR Pfam; PF05222; AlaDh_PNT_N; 1.
DR Pfam; PF02233; PNTB; 1.
DR Pfam; PF12769; PNTB_4TM; 1.
DR SMART; SM01002; AlaDh_PNT_C; 1.
DR SMART; SM01003; AlaDh_PNT_N; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF52467; SSF52467; 1.
DR TIGRFAMs; TIGR00561; pntA; 1.
DR PROSITE; PS00836; ALADH_PNT_1; 1.
DR PROSITE; PS00837; ALADH_PNT_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Disease variant; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; NAD; NADP; Nucleotide-binding;
KW Reference proteome; Transit peptide; Translocase; Transmembrane;
KW Transmembrane helix.
FT TRANSIT 1..43
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P11024"
FT CHAIN 44..1086
FT /note="NAD(P) transhydrogenase, mitochondrial"
FT /id="PRO_0000001055"
FT TOPO_DOM 44..474
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P11024"
FT TRANSMEM 475..493
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 501..521
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 527..546
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 558..578
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 579..595
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P11024"
FT TRANSMEM 596..616
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 622..642
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 646..666
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 672..691
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 702..722
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 723..739
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P11024"
FT TRANSMEM 740..760
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 778..797
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 801..819
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 833..853
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 857..879
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 880..1086
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P11024"
FT BINDING 182..184
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P07001"
FT BINDING 237
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P07001"
FT BINDING 257..259
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P07001"
FT BINDING 287
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:W5PFI3"
FT BINDING 300
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P07001"
FT BINDING 319
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P07001"
FT BINDING 933
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:10673423,
FT ECO:0000269|PubMed:12791694, ECO:0000269|PubMed:15323555,
FT ECO:0007744|PDB:1DJL, ECO:0007744|PDB:1PT9,
FT ECO:0007744|PDB:1U31"
FT BINDING 965..970
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:10673423,
FT ECO:0000269|PubMed:12791694, ECO:0000269|PubMed:15323555,
FT ECO:0007744|PDB:1DJL, ECO:0007744|PDB:1PT9,
FT ECO:0007744|PDB:1U31"
FT BINDING 1007..1011
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:10673423,
FT ECO:0000269|PubMed:12791694, ECO:0000269|PubMed:15323555,
FT ECO:0007744|PDB:1DJL, ECO:0007744|PDB:1PT9,
FT ECO:0007744|PDB:1U31"
FT BINDING 1026..1027
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:10673423,
FT ECO:0000269|PubMed:15323555, ECO:0007744|PDB:1DJL,
FT ECO:0007744|PDB:1U31"
FT BINDING 1042..1049
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:10673423,
FT ECO:0000269|PubMed:12791694, ECO:0000269|PubMed:15323555,
FT ECO:0007744|PDB:1DJL, ECO:0007744|PDB:1PT9,
FT ECO:0007744|PDB:1U31"
FT BINDING 1068..1069
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:10673423,
FT ECO:0000269|PubMed:12791694, ECO:0000269|PubMed:15323555,
FT ECO:0007744|PDB:1DJL, ECO:0007744|PDB:1PT9,
FT ECO:0007744|PDB:1U31"
FT MOD_RES 70
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 117
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q61941"
FT MOD_RES 224
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q61941"
FT MOD_RES 294
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q61941"
FT MOD_RES 331
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q61941"
FT MOD_RES 397
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1079
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q61941"
FT VARIANT 193
FT /note="S -> N (in GCCD4; dbSNP:rs867004061)"
FT /evidence="ECO:0000269|PubMed:22634753"
FT /id="VAR_068781"
FT VARIANT 357
FT /note="T -> A (in GCCD4; dbSNP:rs1447408865)"
FT /evidence="ECO:0000269|PubMed:22634753"
FT /id="VAR_068782"
FT VARIANT 365
FT /note="H -> P (in GCCD4)"
FT /evidence="ECO:0000269|PubMed:22634753"
FT /id="VAR_068783"
FT VARIANT 437
FT /note="P -> L (in GCCD4; dbSNP:rs781183677)"
FT /evidence="ECO:0000269|PubMed:22634753"
FT /id="VAR_068784"
FT VARIANT 533
FT /note="A -> V (in GCCD4; dbSNP:rs387907232)"
FT /evidence="ECO:0000269|PubMed:22634753"
FT /id="VAR_068785"
FT VARIANT 664
FT /note="G -> R (in GCCD4; dbSNP:rs371979800)"
FT /evidence="ECO:0000269|PubMed:22634753"
FT /id="VAR_068786"
FT VARIANT 678
FT /note="G -> R (in GCCD4)"
FT /evidence="ECO:0000269|PubMed:22634753"
FT /id="VAR_068787"
FT VARIANT 862
FT /note="G -> D (in GCCD4; dbSNP:rs1474421419)"
FT /evidence="ECO:0000269|PubMed:22634753"
FT /id="VAR_068788"
FT VARIANT 977
FT /note="L -> P (in GCCD4; dbSNP:rs387907233)"
FT /evidence="ECO:0000269|PubMed:22634753"
FT /id="VAR_068789"
FT VARIANT 1008
FT /note="A -> P (in GCCD4; dbSNP:rs387907234)"
FT /evidence="ECO:0000269|PubMed:22634753"
FT /id="VAR_068790"
FT VARIANT 1009
FT /note="N -> K (in GCCD4; dbSNP:rs370273690)"
FT /evidence="ECO:0000269|PubMed:22634753"
FT /id="VAR_068791"
FT CONFLICT 176
FT /note="A -> T (in Ref. 2; CAA90428)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="G -> E (in Ref. 3; CAD38536)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="A -> E (in Ref. 1; AAC51914)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="A -> S (in Ref. 1; AAC51914)"
FT /evidence="ECO:0000305"
FT CONFLICT 706
FT /note="F -> S (in Ref. 1; AAC51914)"
FT /evidence="ECO:0000305"
FT CONFLICT 731
FT /note="T -> P (in Ref. 1; AAC51914)"
FT /evidence="ECO:0000305"
FT CONFLICT 810
FT /note="S -> A (in Ref. 2; CAA90428)"
FT /evidence="ECO:0000305"
FT CONFLICT 824
FT /note="A -> P (in Ref. 2; CAA90428)"
FT /evidence="ECO:0000305"
FT CONFLICT 871
FT /note="I -> P (in Ref. 1; AAC51914)"
FT /evidence="ECO:0000305"
FT CONFLICT 929
FT /note="I -> F (in Ref. 1; AAC51914)"
FT /evidence="ECO:0000305"
FT CONFLICT 1059
FT /note="K -> R (in Ref. 3; CAD38536)"
FT /evidence="ECO:0000305"
FT HELIX 914..923
FT /evidence="ECO:0007829|PDB:1DJL"
FT STRAND 925..931
FT /evidence="ECO:0007829|PDB:1DJL"
FT HELIX 933..938
FT /evidence="ECO:0007829|PDB:1DJL"
FT HELIX 941..953
FT /evidence="ECO:0007829|PDB:1DJL"
FT STRAND 957..962
FT /evidence="ECO:0007829|PDB:1DJL"
FT STRAND 967..969
FT /evidence="ECO:0007829|PDB:1DJL"
FT HELIX 972..979
FT /evidence="ECO:0007829|PDB:1DJL"
FT HELIX 984..986
FT /evidence="ECO:0007829|PDB:1DJL"
FT STRAND 987..989
FT /evidence="ECO:0007829|PDB:1DJL"
FT HELIX 990..993
FT /evidence="ECO:0007829|PDB:1DJL"
FT HELIX 994..999
FT /evidence="ECO:0007829|PDB:1DJL"
FT STRAND 1001..1007
FT /evidence="ECO:0007829|PDB:1DJL"
FT HELIX 1010..1012
FT /evidence="ECO:0007829|PDB:1DJL"
FT HELIX 1015..1018
FT /evidence="ECO:0007829|PDB:1DJL"
FT TURN 1023..1026
FT /evidence="ECO:0007829|PDB:1DJL"
FT HELIX 1032..1034
FT /evidence="ECO:0007829|PDB:1DJL"
FT STRAND 1035..1045
FT /evidence="ECO:0007829|PDB:1DJL"
FT HELIX 1055..1058
FT /evidence="ECO:0007829|PDB:1DJL"
FT STRAND 1062..1067
FT /evidence="ECO:0007829|PDB:1DJL"
FT HELIX 1069..1081
FT /evidence="ECO:0007829|PDB:1DJL"
SQ SEQUENCE 1086 AA; 113896 MW; 8A437658CA0EB41B CRC64;
MANLLKTVVT GCSCPLLSNL GSCKGLRVKK DFLRTFYTHQ ELWCKAPVKP GIPYKQLTVG
VPKEIFQNEK RVALSPAGVQ NLVKQGFNVV VESGAGEASK FSDDHYRVAG AQIQGAKEVL
ASDLVVKVRA PMVNPTLGVH EADLLKTSGT LISFIYPAQN PELLNKLSQR KTTVLAMDQV
PRVTIAQGYD ALSSMANIAG YKAVVLAANH FGRFFTGQIT AAGKVPPAKI LIVGGGVAGL
ASAGAAKSMG AIVRGFDTRA AALEQFKSLG AEPLEVDLKE SGEGQGGYAK EMSKEFIEAE
MKLFAQQCKE VDILISTALI PGKKAPVLFN KEMIESMKEG SVVVDLAAEA GGNFETTKPG
ELYIHKGITH IGYTDLPSRM ATQASTLYSN NITKLLKAIS PDKDNFYFDV KDDFDFGTMG
HVIRGTVVMK DGKVIFPAPT PKNIPQGAPV KQKTVAELEA EKAATITPFR KTMSTASAYT
AGLTGILGLG IAAPNLAFSQ MVTTFGLAGI VGYHTVWGVT PALHSPLMSV TNAISGLTAV
GGLALMGGHL YPSTTSQGLA ALAAFISSVN IAGGFLVTQR MLDMFKRPTD PPEYNYLYLL
PAGTFVGGYL AALYSGYNIE QIMYLGSGLC CVGALAGLST QGTARLGNAL GMIGVAGGLA
ATLGVLKPGP ELLAQMSGAM ALGGTIGLTI AKRIQISDLP QLVAAFHSLV GLAAVLTCIA
EYIIEYPHFA TDAAANLTKI VAYLGTYIGG VTFSGSLIAY GKLQGLLKSA PLLLPGRHLL
NAGLLAASVG GIIPFMVDPS FTTGITCLGS VSALSAVMGV TLTAAIGGAD MPVVITVLNS
YSGWALCAEG FLLNNNLLTI VGALIGSSGA ILSYIMCVAM NRSLANVILG GYGTTSTAGG
KPMEISGTHT EINLDNAIDM IREANSIIIT PGYGLCAAKA QYPIADLVKM LTEQGKKVRF
GIHPVAGRMP GQLNVLLAEA GVPYDIVLEM DEINHDFPDT DLVLVIGAND TVNSAAQEDP
NSIIAGMPVL EVWKSKQVIV MKRSLGVGYA AVDNPIFYKP NTAMLLGDAK KTCDALQAKV
RESYQK
