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NAD(P) transhydrogenase, mitochondrial (EC 1.6.1.2) (Nicotinamide nucleotide transhydrogenase) (Pyridine nucleotide transhydrogenase)

 NNTM_HUMAN              Reviewed;        1086 AA.
Q13423; Q16796; Q2TB60; Q8N3V4;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
16-AUG-2004, sequence version 3.
25-OCT-2017, entry version 177.
RecName: Full=NAD(P) transhydrogenase, mitochondrial;
EC=1.6.1.2;
AltName: Full=Nicotinamide nucleotide transhydrogenase;
AltName: Full=Pyridine nucleotide transhydrogenase;
Flags: Precursor;
Name=NNT;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9524818; DOI=10.3109/10425179709034058;
Ware J., Zieger B.;
"Cloning and deduced amino acid sequence of human nicotinamide
nucleotide transhydrogenase.";
DNA Seq. 7:369-374(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Heart;
PubMed=8616157; DOI=10.1016/0005-2728(95)00159-X;
Lagberg E.M., Betsholtz C., Rydstrom J.;
"The cDNA sequence of proton-pumping nicotinamide nucleotide
transhydrogenase from man and mouse.";
Biochim. Biophys. Acta 1273:203-205(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skeletal muscle;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70 AND LYS-397, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[7]
FUNCTION, TISSUE SPECIFICITY, AND VARIANTS GCCD4 ASN-193; ALA-357;
PRO-365; LEU-437; VAL-533; ARG-664; ARG-678; ASP-862; PRO-977;
PRO-1008 AND LYS-1009.
PubMed=22634753; DOI=10.1038/ng.2299;
Meimaridou E., Kowalczyk J., Guasti L., Hughes C.R., Wagner F.,
Frommolt P., Nurnberg P., Mann N.P., Banerjee R., Saka H.N.,
Chapple J.P., King P.J., Clark A.J., Metherell L.A.;
"Mutations in NNT encoding nicotinamide nucleotide transhydrogenase
cause familial glucocorticoid deficiency.";
Nat. Genet. 44:740-742(2012).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[10]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 880-1086 IN COMPLEX WITH
NADP.
PubMed=10673423; DOI=10.1016/S0969-2126(00)00075-7;
White S.A., Peake S.J., McSweeney S., Leonard G., Cotton N.P.J.,
Jackson J.B.;
"The high-resolution structure of the NADP(H)-binding component (dIII)
of proton-translocating transhydrogenase from human heart
mitochondria.";
Structure 8:1-12(2000).
-!- FUNCTION: The transhydrogenation between NADH and NADP is coupled
to respiration and ATP hydrolysis and functions as a proton pump
across the membrane. May play a role in reactive oxygen species
(ROS) detoxification in the adrenal gland.
{ECO:0000269|PubMed:22634753}.
-!- CATALYTIC ACTIVITY: NADPH + NAD(+) = NADP(+) + NADH.
-!- SUBUNIT: Homodimer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305};
Multi-pass membrane protein {ECO:0000305}; Matrix side
{ECO:0000305}.
-!- TISSUE SPECIFICITY: Widely expressed with expression most readily
detectable in adrenal, heart, kidney, thyroid and adipose tissues.
{ECO:0000269|PubMed:22634753}.
-!- DISEASE: Glucocorticoid deficiency 4 with or without
mineralocorticoid deficiency (GCCD4) [MIM:614736]: A rare,
potentially lethal, autosomal recessive disorder characterized by
resistance to ACTH action on the adrenal cortex, adrenal
insufficiency and an inability of the adrenal cortex to produce
cortisol. It usually presents in the neonatal period or in early
childhood with episodes of hypoglycemia and other symptoms related
to cortisol deficiency, including failure to thrive, recurrent
illnesses or infections, convulsions, and shock. In a small number
of patients hypoglycemia can be sufficiently severe and persistent
that it leads to serious long-term neurological damage or death.
The diagnosis is readily confirmed with a low plasma cortisol
measurement in the presence of an elevated ACTH level, and normal
aldosterone and plasma renin measurements.
{ECO:0000269|PubMed:22634753}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: In the N-terminal section; belongs to the AlaDH/PNT
family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the PNT beta
subunit family. {ECO:0000305}.
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EMBL; U40490; AAC51914.1; -; mRNA.
EMBL; Z50101; CAA90428.1; -; mRNA.
EMBL; AL831822; CAD38536.1; -; mRNA.
EMBL; BC110543; AAI10544.1; -; mRNA.
CCDS; CCDS3949.1; -.
PIR; G02257; G02257.
RefSeq; NP_036475.3; NM_012343.3.
RefSeq; NP_892022.2; NM_182977.2.
RefSeq; XP_005248331.1; XM_005248274.4.
RefSeq; XP_011512303.1; XM_011514001.2.
RefSeq; XP_016864782.1; XM_017009293.1.
UniGene; Hs.482043; -.
PDB; 1DJL; X-ray; 2.00 A; A/B=880-1086.
PDB; 1PT9; X-ray; 2.42 A; A/B=880-1086.
PDB; 1U31; X-ray; 2.20 A; A/B=880-1086.
PDBsum; 1DJL; -.
PDBsum; 1PT9; -.
PDBsum; 1U31; -.
ProteinModelPortal; Q13423; -.
SMR; Q13423; -.
BioGrid; 117076; 54.
IntAct; Q13423; 19.
MINT; MINT-3027647; -.
STRING; 9606.ENSP00000264663; -.
DrugBank; DB03461; 2'-Monophosphoadenosine 5'-Diphosphoribose.
DrugBank; DB01763; 7-thionicotinamide-adenine-dinucleotide phosphate.
DrugBank; DB00157; NADH.
iPTMnet; Q13423; -.
PhosphoSitePlus; Q13423; -.
SwissPalm; Q13423; -.
BioMuta; NNT; -.
DMDM; 51338801; -.
EPD; Q13423; -.
MaxQB; Q13423; -.
PaxDb; Q13423; -.
PeptideAtlas; Q13423; -.
PRIDE; Q13423; -.
DNASU; 23530; -.
Ensembl; ENST00000264663; ENSP00000264663; ENSG00000112992.
Ensembl; ENST00000344920; ENSP00000343873; ENSG00000112992.
GeneID; 23530; -.
KEGG; hsa:23530; -.
UCSC; uc003joe.4; human.
CTD; 23530; -.
DisGeNET; 23530; -.
EuPathDB; HostDB:ENSG00000112992.16; -.
GeneCards; NNT; -.
H-InvDB; HIX0032203; -.
HGNC; HGNC:7863; NNT.
HPA; CAB004975; -.
HPA; HPA004829; -.
MalaCards; NNT; -.
MIM; 607878; gene.
MIM; 614736; phenotype.
neXtProt; NX_Q13423; -.
OpenTargets; ENSG00000112992; -.
Orphanet; 361; Familial glucocorticoid deficiency.
PharmGKB; PA31667; -.
eggNOG; ENOG410IEMU; Eukaryota.
eggNOG; COG1282; LUCA.
eggNOG; COG3288; LUCA.
GeneTree; ENSGT00390000004624; -.
HOGENOM; HOG000160623; -.
HOVERGEN; HBG006511; -.
InParanoid; Q13423; -.
KO; K00323; -.
OMA; KPGIPYK; -.
OrthoDB; EOG091G01NO; -.
PhylomeDB; Q13423; -.
TreeFam; TF300636; -.
BioCyc; MetaCyc:HS03639-MONOMER; -.
BRENDA; 1.6.1.2; 2681.
Reactome; R-HSA-71403; Citric acid cycle (TCA cycle).
ChiTaRS; NNT; human.
EvolutionaryTrace; Q13423; -.
GeneWiki; NNT_(gene); -.
GenomeRNAi; 23530; -.
PRO; PR:Q13423; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000112992; -.
CleanEx; HS_NNT; -.
ExpressionAtlas; Q13423; baseline and differential.
Genevisible; Q13423; HS.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005743; C:mitochondrial inner membrane; TAS:UniProtKB.
GO; GO:0005746; C:mitochondrial respiratory chain; TAS:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:LIFEdb.
GO; GO:0051287; F:NAD binding; TAS:UniProtKB.
GO; GO:0008750; F:NAD(P)+ transhydrogenase (AB-specific) activity; IBA:GO_Central.
GO; GO:0003957; F:NAD(P)+ transhydrogenase (B-specific) activity; TAS:UniProtKB.
GO; GO:0008746; F:NAD(P)+ transhydrogenase activity; EXP:Reactome.
GO; GO:0050661; F:NADP binding; IDA:UniProtKB.
GO; GO:0006740; P:NADPH regeneration; IBA:GO_Central.
GO; GO:0055114; P:oxidation-reduction process; TAS:UniProtKB.
GO; GO:0015992; P:proton transport; TAS:UniProtKB.
GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:UniProtKB.
GO; GO:0006099; P:tricarboxylic acid cycle; TAS:UniProtKB.
Gene3D; 3.40.50.1220; -; 1.
InterPro; IPR008143; Ala_DH/PNT_CS2.
InterPro; IPR008142; AlaDH/PNT_CS1.
InterPro; IPR007886; AlaDH/PNT_N.
InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR026255; NADP_transhyd_a.
InterPro; IPR024605; NADP_transhyd_a_C.
InterPro; IPR034300; PNTB-like.
Pfam; PF01262; AlaDh_PNT_C; 1.
Pfam; PF05222; AlaDh_PNT_N; 1.
Pfam; PF02233; PNTB; 1.
Pfam; PF12769; PNTB_4TM; 1.
SMART; SM01002; AlaDh_PNT_C; 1.
SMART; SM01003; AlaDh_PNT_N; 1.
SUPFAM; SSF51735; SSF51735; 1.
SUPFAM; SSF52467; SSF52467; 1.
TIGRFAMs; TIGR00561; pntA; 1.
PROSITE; PS00836; ALADH_PNT_1; 1.
PROSITE; PS00837; ALADH_PNT_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Disease mutation;
Membrane; Mitochondrion; Mitochondrion inner membrane; NAD; NADP;
Oxidoreductase; Reference proteome; Transit peptide; Transmembrane;
Transmembrane helix.
TRANSIT 1 43 Mitochondrion. {ECO:0000250}.
CHAIN 44 1086 NAD(P) transhydrogenase, mitochondrial.
/FTId=PRO_0000001055.
TOPO_DOM 44 474 Mitochondrial matrix.
TRANSMEM 475 493 Helical. {ECO:0000255}.
TRANSMEM 501 521 Helical. {ECO:0000255}.
TRANSMEM 527 546 Helical. {ECO:0000255}.
TRANSMEM 558 578 Helical. {ECO:0000255}.
TOPO_DOM 579 595 Mitochondrial matrix.
TRANSMEM 596 616 Helical. {ECO:0000255}.
TRANSMEM 622 642 Helical. {ECO:0000255}.
TRANSMEM 646 666 Helical. {ECO:0000255}.
TRANSMEM 672 691 Helical. {ECO:0000255}.
TRANSMEM 702 722 Helical. {ECO:0000255}.
TOPO_DOM 723 739 Cytoplasmic.
TRANSMEM 740 760 Helical. {ECO:0000255}.
TRANSMEM 778 797 Helical. {ECO:0000255}.
TRANSMEM 801 819 Helical. {ECO:0000255}.
TRANSMEM 833 853 Helical. {ECO:0000255}.
TRANSMEM 857 879 Helical. {ECO:0000255}.
TOPO_DOM 880 1086 Mitochondrial matrix.
NP_BIND 229 259 NAD. {ECO:0000250}.
NP_BIND 965 970 NADP. {ECO:0000269|PubMed:10673423}.
NP_BIND 1007 1011 NADP. {ECO:0000269|PubMed:10673423}.
NP_BIND 1042 1049 NADP. {ECO:0000269|PubMed:10673423}.
NP_BIND 1068 1069 NADP. {ECO:0000269|PubMed:10673423}.
BINDING 933 933 NADP; via amide nitrogen.
{ECO:0000269|PubMed:10673423}.
MOD_RES 70 70 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 117 117 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q61941}.
MOD_RES 224 224 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q61941}.
MOD_RES 294 294 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q61941}.
MOD_RES 331 331 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q61941}.
MOD_RES 397 397 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1079 1079 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q61941}.
VARIANT 193 193 S -> N (in GCCD4; dbSNP:rs867004061).
{ECO:0000269|PubMed:22634753}.
/FTId=VAR_068781.
VARIANT 357 357 T -> A (in GCCD4).
{ECO:0000269|PubMed:22634753}.
/FTId=VAR_068782.
VARIANT 365 365 H -> P (in GCCD4).
{ECO:0000269|PubMed:22634753}.
/FTId=VAR_068783.
VARIANT 437 437 P -> L (in GCCD4; dbSNP:rs781183677).
{ECO:0000269|PubMed:22634753}.
/FTId=VAR_068784.
VARIANT 533 533 A -> V (in GCCD4; dbSNP:rs387907232).
{ECO:0000269|PubMed:22634753}.
/FTId=VAR_068785.
VARIANT 664 664 G -> R (in GCCD4; dbSNP:rs371979800).
{ECO:0000269|PubMed:22634753}.
/FTId=VAR_068786.
VARIANT 678 678 G -> R (in GCCD4).
{ECO:0000269|PubMed:22634753}.
/FTId=VAR_068787.
VARIANT 862 862 G -> D (in GCCD4).
{ECO:0000269|PubMed:22634753}.
/FTId=VAR_068788.
VARIANT 977 977 L -> P (in GCCD4; dbSNP:rs387907233).
{ECO:0000269|PubMed:22634753}.
/FTId=VAR_068789.
VARIANT 1008 1008 A -> P (in GCCD4; dbSNP:rs387907234).
{ECO:0000269|PubMed:22634753}.
/FTId=VAR_068790.
VARIANT 1009 1009 N -> K (in GCCD4; dbSNP:rs370273690).
{ECO:0000269|PubMed:22634753}.
/FTId=VAR_068791.
CONFLICT 176 176 A -> T (in Ref. 2; CAA90428).
{ECO:0000305}.
CONFLICT 212 212 G -> E (in Ref. 3; CAD38536).
{ECO:0000305}.
CONFLICT 246 246 A -> E (in Ref. 1; AAC51914).
{ECO:0000305}.
CONFLICT 262 262 A -> S (in Ref. 1; AAC51914).
{ECO:0000305}.
CONFLICT 706 706 F -> S (in Ref. 1; AAC51914).
{ECO:0000305}.
CONFLICT 731 731 T -> P (in Ref. 1; AAC51914).
{ECO:0000305}.
CONFLICT 810 810 S -> A (in Ref. 2; CAA90428).
{ECO:0000305}.
CONFLICT 824 824 A -> P (in Ref. 2; CAA90428).
{ECO:0000305}.
CONFLICT 871 871 I -> P (in Ref. 1; AAC51914).
{ECO:0000305}.
CONFLICT 929 929 I -> F (in Ref. 1; AAC51914).
{ECO:0000305}.
CONFLICT 1059 1059 K -> R (in Ref. 3; CAD38536).
{ECO:0000305}.
HELIX 914 923 {ECO:0000244|PDB:1DJL}.
STRAND 925 931 {ECO:0000244|PDB:1DJL}.
HELIX 933 938 {ECO:0000244|PDB:1DJL}.
HELIX 941 953 {ECO:0000244|PDB:1DJL}.
STRAND 957 962 {ECO:0000244|PDB:1DJL}.
STRAND 967 969 {ECO:0000244|PDB:1DJL}.
HELIX 972 979 {ECO:0000244|PDB:1DJL}.
HELIX 984 986 {ECO:0000244|PDB:1DJL}.
STRAND 987 989 {ECO:0000244|PDB:1DJL}.
HELIX 990 993 {ECO:0000244|PDB:1DJL}.
HELIX 994 999 {ECO:0000244|PDB:1DJL}.
STRAND 1001 1007 {ECO:0000244|PDB:1DJL}.
HELIX 1010 1012 {ECO:0000244|PDB:1DJL}.
HELIX 1015 1018 {ECO:0000244|PDB:1DJL}.
TURN 1023 1026 {ECO:0000244|PDB:1DJL}.
HELIX 1032 1034 {ECO:0000244|PDB:1DJL}.
STRAND 1035 1045 {ECO:0000244|PDB:1DJL}.
HELIX 1055 1058 {ECO:0000244|PDB:1DJL}.
STRAND 1062 1067 {ECO:0000244|PDB:1DJL}.
HELIX 1069 1081 {ECO:0000244|PDB:1DJL}.
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


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