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Protein

NAD(P) transhydrogenase, mitochondrial

Gene

Nnt

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity).By similarity

Catalytic activityi

NADPH + NAD+ = NADP+ + NADH.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi229 – 25931NADBy similarityAdd
BLAST
Nucleotide bindingi965 – 9706NADPBy similarity
Nucleotide bindingi1007 – 10115NADPBy similarity
Nucleotide bindingi1042 – 10498NADPBy similarity
Nucleotide bindingi1068 – 10692NADPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
NAD(P) transhydrogenase, mitochondrial (EC:1.6.1.2)
Alternative name(s):
Nicotinamide nucleotide transhydrogenase
Pyridine nucleotide transhydrogenase
Gene namesi
Name:Nnt
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:109279. Nnt.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini44 – 474431Mitochondrial matrixAdd
BLAST
Transmembranei475 – 49319HelicalSequence analysisAdd
BLAST
Transmembranei501 – 52121HelicalSequence analysisAdd
BLAST
Transmembranei527 – 54620HelicalSequence analysisAdd
BLAST
Transmembranei558 – 57821HelicalSequence analysisAdd
BLAST
Topological domaini579 – 59517Mitochondrial matrixAdd
BLAST
Transmembranei596 – 61621HelicalSequence analysisAdd
BLAST
Transmembranei622 – 64221HelicalSequence analysisAdd
BLAST
Transmembranei646 – 66621HelicalSequence analysisAdd
BLAST
Transmembranei672 – 69120HelicalSequence analysisAdd
BLAST
Transmembranei702 – 72221HelicalSequence analysisAdd
BLAST
Topological domaini723 – 73917CytoplasmicAdd
BLAST
Transmembranei740 – 76021HelicalSequence analysisAdd
BLAST
Transmembranei778 – 79720HelicalSequence analysisAdd
BLAST
Transmembranei801 – 81919HelicalSequence analysisAdd
BLAST
Transmembranei833 – 85321HelicalSequence analysisAdd
BLAST
Transmembranei857 – 87923HelicalSequence analysisAdd
BLAST
Topological domaini880 – 1086207Mitochondrial matrixAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • mitochondrial inner membrane Source: MGI
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Disruption phenotypei

Higher levels of adrenocortical cell apoptosis and impaired glucocorticoid production are observed.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4343MitochondrionBy similarityAdd
BLAST
Chaini44 – 10861043NAD(P) transhydrogenase, mitochondrialPRO_0000001056Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei70 – 701N6-acetyllysineBy similarity
Modified residuei117 – 1171N6-succinyllysineCombined sources
Modified residuei224 – 2241N6-succinyllysineCombined sources
Modified residuei294 – 2941N6-succinyllysineCombined sources
Modified residuei331 – 3311N6-succinyllysineCombined sources
Modified residuei397 – 3971N6-acetyllysineBy similarity
Modified residuei1079 – 10791N6-succinyllysineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ61941.
MaxQBiQ61941.
PaxDbiQ61941.
PeptideAtlasiQ61941.
PRIDEiQ61941.

PTM databases

iPTMnetiQ61941.
PhosphoSiteiQ61941.

Expressioni

Tissue specificityi

Widely expressed with expression most readily detectable in adrenal, heart, kidney, thyroid and adipose tissues.1 Publication

Gene expression databases

CleanExiMM_NNT.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

MINTiMINT-1841613.
STRINGi10090.ENSMUSP00000096753.

Structurei

3D structure databases

ProteinModelPortaliQ61941.
SMRiQ61941. Positions 902-1083.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

In the N-terminal section; belongs to the AlaDH/PNT family.Curated
In the C-terminal section; belongs to the PNT beta subunit family.Curated

Keywords - Domaini

Transit peptide, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IEMU. Eukaryota.
ENOG410IRZN. Eukaryota.
COG1282. LUCA.
COG3288. LUCA.
HOVERGENiHBG006511.
InParanoidiQ61941.

Family and domain databases

Gene3Di3.40.50.1220. 1 hit.
InterProiIPR008143. Ala_DH/PNT_CS2.
IPR008142. AlaDH/PNT_CS1.
IPR007886. AlaDH/PNT_N.
IPR007698. AlaDH/PNT_NAD(H)-bd.
IPR029035. DHS-like_NAD/FAD-binding_dom.
IPR016040. NAD(P)-bd_dom.
IPR012136. NADH_DH_b.
IPR026255. NADP_transhyd_a.
IPR024605. NADP_transhyd_a_C.
IPR030168. NADP_transhyd_mt.
[Graphical view]
PANTHERiPTHR10160:SF22. PTHR10160:SF22. 1 hit.
PfamiPF01262. AlaDh_PNT_C. 1 hit.
PF05222. AlaDh_PNT_N. 1 hit.
PF02233. PNTB. 1 hit.
PF12769. PNTB_4TM. 1 hit.
[Graphical view]
SMARTiSM01002. AlaDh_PNT_C. 1 hit.
SM01003. AlaDh_PNT_N. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF52467. SSF52467. 1 hit.
TIGRFAMsiTIGR00561. pntA. 1 hit.
PROSITEiPS00836. ALADH_PNT_1. 1 hit.
PS00837. ALADH_PNT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q61941-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAHLLKTVVA GCSCPFLSNL GSSKVLPGKR DFVRTLRTHQ ALWCKSPVKP
60 70 80 90 100
GIPYKQLTVG VPKEIFQNEK RVALSPAGVQ ALVKQGFNVV VESGAGEASK
110 120 130 140 150
FPDDLYRAAG AQIQGMKEVL ASDLVVKVRA PMVNPTLGAH EADFLKPSGT
160 170 180 190 200
LISFIYPAQN PDLLNKLSER KTTVLAMDQV PRVTIAQGYD ALSSMANISG
210 220 230 240 250
YKAVVLAANH FGRFFTGQIT AAGKVPPAKI LIVGGGVAGL ASAGAAKSMG
260 270 280 290 300
AVVRGFDTRA AALEQFKSLG AEPLEVDLKE SGEGQGGYAK EMSKEFIEAE
310 320 330 340 350
MKLFAQQCKE VDILISTALI PGKKAPVLFS KEMIESMKEG SVVVDLAAEA
360 370 380 390 400
GGNFETTKPG ELYVHKGITH IGYTDLPSRM ATQASTLYSN NITKLLKAIS
410 420 430 440 450
PDKDNFHFEV KDDFDFGTMS HVIRGTVVMK DGKVIFPAPT PKNIPEEAPV
460 470 480 490 500
KPKTVAELEA EKAGTVSMYT KTLTTASVYS AGLTGMLGLG IVAPNVAFSQ
510 520 530 540 550
MVTTFGLAGI IGYHTVWGVT PALHSPLMSV TNAISGLTAV GGLALMGGHF
560 570 580 590 600
YPSTTSQSLA ALATFISSVN IAGGFLVTQR MLDMFKRPTD PPEYNYLYLL
610 620 630 640 650
PGGTFVGGYL AALYGGYNIE EIMYLGSGLC CVGALGGLST QGTARLGNAL
660 670 680 690 700
GMIGVAGGLA ATLGGLKPDP QLLAQMSGAM AMGGTIGLTI AKRIQISDLP
710 720 730 740 750
QLVAAFHSLV GLAAVLTCMA EYIVEYPHFA MDATSNFTKI VAYLGTYIGG
760 770 780 790 800
VTFSGSLVAY GKLQGILKSA PLLLPGRHAL NAGLLAASVG GIIPFMADPS
810 820 830 840 850
FTTGITCLGS VSGLSTLMGV TLTAAIGGAD MPVVITVLNS YSGWALCAEG
860 870 880 890 900
FLLNNNLLTI VGALIGSSGA ILSYIMCVAM NRSLANVILG GYGTTSTAGG
910 920 930 940 950
KPMEISGTHT EINLDNAVEM IREANSIVIT PGYGLCAAKA QYPIADLVKM
960 970 980 990 1000
LTEQGKKVRF GIHPVAGRMP GQLNVLLAEA GVPYDIVLEM DEINSDFPDT
1010 1020 1030 1040 1050
DLVLVIGAND TVNSAAQEDP NSIIAGMPVL EVWKSKQVIV MKRSLGVGYA
1060 1070 1080
AVDNPIFYKP NTAMLLGDAK KTCDALQAKV RESYQK
Length:1,086
Mass (Da):113,838
Last modified:August 16, 2004 - v2
Checksum:iA023285169834D07
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti35 – 351T → M in CAA89065 (PubMed:8616157).Curated
Sequence conflicti775 – 7751P → L in CAA89065 (PubMed:8616157).Curated
Sequence conflicti813 – 8131G → A in CAA89065 (PubMed:8616157).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49204 mRNA. Translation: CAA89065.1.
AF257157
, AF257137, AF257138, AF257139, AF257140, AF257141, AF257142, AF257143, AF257144, AF257145, AF257146, AF257147, AF257148, AF257149, AF257150, AF257151, AF257152, AF257153, AF257154, AF257155, AF257156 Genomic DNA. Translation: AAF72982.2.
PIRiS54876.
UniGeneiMm.132584.
Mm.486065.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49204 mRNA. Translation: CAA89065.1.
AF257157
, AF257137, AF257138, AF257139, AF257140, AF257141, AF257142, AF257143, AF257144, AF257145, AF257146, AF257147, AF257148, AF257149, AF257150, AF257151, AF257152, AF257153, AF257154, AF257155, AF257156 Genomic DNA. Translation: AAF72982.2.
PIRiS54876.
UniGeneiMm.132584.
Mm.486065.

3D structure databases

ProteinModelPortaliQ61941.
SMRiQ61941. Positions 902-1083.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1841613.
STRINGi10090.ENSMUSP00000096753.

PTM databases

iPTMnetiQ61941.
PhosphoSiteiQ61941.

Proteomic databases

EPDiQ61941.
MaxQBiQ61941.
PaxDbiQ61941.
PeptideAtlasiQ61941.
PRIDEiQ61941.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:109279. Nnt.

Phylogenomic databases

eggNOGiENOG410IEMU. Eukaryota.
ENOG410IRZN. Eukaryota.
COG1282. LUCA.
COG3288. LUCA.
HOVERGENiHBG006511.
InParanoidiQ61941.

Miscellaneous databases

ChiTaRSiNnt. mouse.
PROiQ61941.
SOURCEiSearch...

Gene expression databases

CleanExiMM_NNT.

Family and domain databases

Gene3Di3.40.50.1220. 1 hit.
InterProiIPR008143. Ala_DH/PNT_CS2.
IPR008142. AlaDH/PNT_CS1.
IPR007886. AlaDH/PNT_N.
IPR007698. AlaDH/PNT_NAD(H)-bd.
IPR029035. DHS-like_NAD/FAD-binding_dom.
IPR016040. NAD(P)-bd_dom.
IPR012136. NADH_DH_b.
IPR026255. NADP_transhyd_a.
IPR024605. NADP_transhyd_a_C.
IPR030168. NADP_transhyd_mt.
[Graphical view]
PANTHERiPTHR10160:SF22. PTHR10160:SF22. 1 hit.
PfamiPF01262. AlaDh_PNT_C. 1 hit.
PF05222. AlaDh_PNT_N. 1 hit.
PF02233. PNTB. 1 hit.
PF12769. PNTB_4TM. 1 hit.
[Graphical view]
SMARTiSM01002. AlaDh_PNT_C. 1 hit.
SM01003. AlaDh_PNT_N. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF52467. SSF52467. 1 hit.
TIGRFAMsiTIGR00561. pntA. 1 hit.
PROSITEiPS00836. ALADH_PNT_1. 1 hit.
PS00837. ALADH_PNT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The cDNA sequence of proton-pumping nicotinamide nucleotide transhydrogenase from man and mouse."
    Lagberg E.M., Betsholtz C., Rydstrom J.
    Biochim. Biophys. Acta 1273:203-205(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6 X CBA.
    Tissue: Liver.
  2. "Characterization of a nicotinamide nucleotide transhydrogenase gene from the green alga Acetabularia acetabulum and comparison of its structure with those of the corresponding genes in mouse and Caenorhabditis elegans."
    Arkblad E.L., Betsholtz C., Mandoli D., Rydstrom J.
    Biochim. Biophys. Acta 1520:115-123(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/SvJ.
  3. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 72-84; 214-224; 268-279; 367-379; 434-442; 769-777 AND 940-949, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  5. "Mutations in NNT encoding nicotinamide nucleotide transhydrogenase cause familial glucocorticoid deficiency."
    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.
    Nat. Genet. 44:740-742(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
  6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-117; LYS-224; LYS-294; LYS-331 AND LYS-1079, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiNNTM_MOUSE
AccessioniPrimary (citable) accession number: Q61941
Secondary accession number(s): Q9JK70
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 16, 2004
Last modified: July 6, 2016
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.