[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=9524818 [NCBI, ExPASy, EBI, Israel, Japan] 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; DOI=10.1016/0005-2728(95)00159-X; PubMed=8616157 [NCBI, ExPASy, EBI, Israel, Japan] 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; The German cDNA consortium; Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] 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]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 880-1086. DOI=10.1016/S0969-2126(00)00075-7; PubMed=10673423 [NCBI, ExPASy, EBI, Israel, Japan] 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).

Comments

FUNCTION: The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane.
CATALYTIC ACTIVITY: NADPH + NAD⁺ = NADP⁺ + NADH.
SUBUNIT: Homodimer (By similarity).
SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein; Matrix side (Potential).
SIMILARITY: In the N-terminal section; belongs to the AlaDH/PNT family.
SIMILARITY: In the C-terminal section; belongs to the PNT beta subunit family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U40490; AAC51914.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z50101; CAA90428.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL831822; CAD38536.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC110543; AAI10544.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

G02257; G02257.

RefSeq

NP_036475.3; -.
NP_892022.2; -.

UniGene

Hs.482043

3D structure databases

PDB

1DJL; X-ray; 2.00 A; A/B=880-1086.	[ExPASy / RCSB / EBI]
1PT9; X-ray; 2.42 A; A/B=880-1086.	[ExPASy / RCSB / EBI]
1U31; X-ray; 2.20 A; A/B=880-1086.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1DJL; -.
1PT9; -.
1U31; -.

ModBase

Q13423.

Protein-protein interaction databases

IntAct

Q13423; -.

PTM databases

PhosphoSite

Q13423; -.

Organism-specific databases

H-InvDB

HIX0019972; -.
HIX0032203; -.

HGNC

HGNC:7863; NNT.

GenAtlas

NNT.

HPA

CAB004975; -.
HPA004829; -.

MIM

607878; gene. [NCBI / EBI]

PharmGKB

PA31667; -.

GeneCards

Q13423.

Gene expression databases

ArrayExpress

Q13423; -.

CleanEx

HS_NNT; -.

GermOnline

ENSG00000112992; Homo sapiens.

Ontologies

GO:0005746;	Cellular component: mitochondrial respiratory chain (traceable author statement from UniProtKB).
GO:0051287;	Molecular function: NAD binding (traceable author statement from UniProtKB).
GO:0003957;	Molecular function: NAD(P)+ transhydrogenase (B-specific) activity (traceable author statement from UniProtKB).
GO:0050661;	Molecular function: NADP binding (inferred from direct assay from UniProtKB).
GO:0055114;	Biological process: oxidation reduction (traceable author statement from UniProtKB).
GO:0015992;	Biological process: proton transport (traceable author statement from UniProtKB).
GO:0006099;	Biological process: tricarboxylic acid cycle (traceable author statement from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR007698; Ala_DHase/PNT_C.
IPR008142; Ala_DHase/PNT_CS1.
IPR008143; Ala_DHase/PNT_CS2.
IPR007886; Ala_DHase/PNT_N.
IPR016040; NAD(P)-bd.
IPR004571; NADP_transhyd_a.
IPR004003; NADP_transhyd_b.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

Pfam

PF01262; AlaDh_PNT_C; 1.
PF05222; AlaDh_PNT_N; 1.
PF02233; PNTB; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR00561; pntA; 1.

PROSITE

PS00836; ALADH_PNT_1; 1.
PS00837; ALADH_PNT_2; 1.

BLOCKS

Q13423.

Proteomic databases

PeptideAtlas

Q13423; -.

Genome annotation databases

Ensembl

ENSG00000112992; Homo sapiens. [Contig view]

GeneID

23530; -.

KEGG

hsa:23530; -.

Phylogenomic databases

HOGENOM

Q13423; -.

HOVERGEN

Q13423; -.

Other

DB00157; NADH.

NNT; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Membrane; Mitochondrion; Mitochondrion inner membrane; NAD; NADP; Oxidoreductase; Transit peptide; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 43`	`43`	`Mitochondrion (By similarity).`
`CHAIN`	`44 1086`	`1043`	`NAD(P) transhydrogenase, mitochondrial.`	`PRO_0000001055`
`TOPO_DOM`	`44 474`	`431`	`Mitochondrial matrix.`
`TRANSMEM`	`475 493`	`19`	`Potential.`
`TRANSMEM`	`501 521`	`21`	`Potential.`
`TRANSMEM`	`527 546`	`20`	`Potential.`
`TRANSMEM`	`558 578`	`21`	`Potential.`
`TOPO_DOM`	`579 595`	`17`	`Mitochondrial matrix.`
`TRANSMEM`	`596 616`	`21`	`Potential.`
`TRANSMEM`	`622 642`	`21`	`Potential.`
`TRANSMEM`	`646 666`	`21`	`Potential.`
`TRANSMEM`	`672 691`	`20`	`Potential.`
`TRANSMEM`	`702 722`	`21`	`Potential.`
`TOPO_DOM`	`723 739`	`17`	`Cytoplasmic.`
`TRANSMEM`	`740 760`	`21`	`Potential.`
`TRANSMEM`	`778 797`	`20`	`Potential.`
`TRANSMEM`	`801 819`	`19`	`Potential.`
`TRANSMEM`	`833 853`	`21`	`Potential.`
`TRANSMEM`	`857 879`	`23`	`Potential.`
`TOPO_DOM`	`880 1086`	`207`	`Mitochondrial matrix.`
`NP_BIND`	`229 259`	`31`	`NAD (By similarity).`
`CONFLICT`	`176 176`		`A -> T (in Ref. 2; CAA90428).`
`CONFLICT`	`212 212`		`G -> E (in Ref. 3; CAD38536).`
`CONFLICT`	`246 246`		`A -> E (in Ref. 1; AAC51914).`
`CONFLICT`	`262 262`		`A -> S (in Ref. 1; AAC51914).`
`CONFLICT`	`706 706`		`F -> S (in Ref. 1; AAC51914).`
`CONFLICT`	`731 731`		`T -> P (in Ref. 1; AAC51914).`
`CONFLICT`	`810 810`		`S -> A (in Ref. 2; CAA90428).`
`CONFLICT`	`824 824`		`A -> P (in Ref. 2; CAA90428).`
`CONFLICT`	`871 871`		`I -> P (in Ref. 1; AAC51914).`
`CONFLICT`	`929 929`		`I -> F (in Ref. 1; AAC51914).`
`CONFLICT`	`1059 1059`		`K -> R (in Ref. 3; CAD38536).`
`STRAND`	`904 912`	`9`
`HELIX`	`914 923`	`10`
`STRAND`	`925 931`	`7`
`HELIX`	`933 938`	`6`
`HELIX`	`941 953`	`13`
`STRAND`	`957 962`	`6`
`STRAND`	`967 969`	`3`
`HELIX`	`972 979`	`8`
`HELIX`	`984 986`	`3`
`STRAND`	`987 989`	`3`
`HELIX`	`990 993`	`4`
`HELIX`	`994 999`	`6`
`STRAND`	`1001 1007`	`7`
`HELIX`	`1010 1012`	`3`
`HELIX`	`1015 1018`	`4`
`TURN`	`1023 1026`	`4`
`HELIX`	`1032 1034`	`3`
`STRAND`	`1035 1045`	`11`
`HELIX`	`1055 1058`	`4`
`STRAND`	`1062 1067`	`6`
`HELIX`	`1069 1081`	`13`

Sequence information

Length: 1086 AA [This is the length of the unprocessed precursor]

Molecular weight: 113896 Da [This is the MW of the unprocessed precursor]

CRC64: 8A437658CA0EB41B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MANLLKTVVT GCSCPLLSNL GSCKGLRVKK DFLRTFYTHQ ELWCKAPVKP GIPYKQLTVG 

        70         80         90        100        110        120 
VPKEIFQNEK RVALSPAGVQ NLVKQGFNVV VESGAGEASK FSDDHYRVAG AQIQGAKEVL 

       130        140        150        160        170        180 
ASDLVVKVRA PMVNPTLGVH EADLLKTSGT LISFIYPAQN PELLNKLSQR KTTVLAMDQV 

       190        200        210        220        230        240 
PRVTIAQGYD ALSSMANIAG YKAVVLAANH FGRFFTGQIT AAGKVPPAKI LIVGGGVAGL 

       250        260        270        280        290        300 
ASAGAAKSMG AIVRGFDTRA AALEQFKSLG AEPLEVDLKE SGEGQGGYAK EMSKEFIEAE 

       310        320        330        340        350        360 
MKLFAQQCKE VDILISTALI PGKKAPVLFN KEMIESMKEG SVVVDLAAEA GGNFETTKPG 

       370        380        390        400        410        420 
ELYIHKGITH IGYTDLPSRM ATQASTLYSN NITKLLKAIS PDKDNFYFDV KDDFDFGTMG 

       430        440        450        460        470        480 
HVIRGTVVMK DGKVIFPAPT PKNIPQGAPV KQKTVAELEA EKAATITPFR KTMSTASAYT 

       490        500        510        520        530        540 
AGLTGILGLG IAAPNLAFSQ MVTTFGLAGI VGYHTVWGVT PALHSPLMSV TNAISGLTAV 

       550        560        570        580        590        600 
GGLALMGGHL YPSTTSQGLA ALAAFISSVN IAGGFLVTQR MLDMFKRPTD PPEYNYLYLL 

       610        620        630        640        650        660 
PAGTFVGGYL AALYSGYNIE QIMYLGSGLC CVGALAGLST QGTARLGNAL GMIGVAGGLA 

       670        680        690        700        710        720 
ATLGVLKPGP ELLAQMSGAM ALGGTIGLTI AKRIQISDLP QLVAAFHSLV GLAAVLTCIA 

       730        740        750        760        770        780 
EYIIEYPHFA TDAAANLTKI VAYLGTYIGG VTFSGSLIAY GKLQGLLKSA PLLLPGRHLL 

       790        800        810        820        830        840 
NAGLLAASVG GIIPFMVDPS FTTGITCLGS VSALSAVMGV TLTAAIGGAD MPVVITVLNS 

       850        860        870        880        890        900 
YSGWALCAEG FLLNNNLLTI VGALIGSSGA ILSYIMCVAM NRSLANVILG GYGTTSTAGG 

       910        920        930        940        950        960 
KPMEISGTHT EINLDNAIDM IREANSIIIT PGYGLCAAKA QYPIADLVKM LTEQGKKVRF 

       970        980        990       1000       1010       1020 
GIHPVAGRMP GQLNVLLAEA GVPYDIVLEM DEINHDFPDT DLVLVIGAND TVNSAAQEDP 

      1030       1040       1050       1060       1070       1080 
NSIIAGMPVL EVWKSKQVIV MKRSLGVGYA AVDNPIFYKP NTAMLLGDAK KTCDALQAKV 


RESYQK

Q13423 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools