[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=Hereford; TISSUE=Uterus; NIH - Mammalian Gene Collection (MGC) project; Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [MRNA] OF 1-75. DOI=10.1016/S0006-291X(88)80005-6; PubMed=3196335 [NCBI, ExPASy, EBI, Israel, Japan] Yamaguchi M., Hatefi Y., Trach K., Hoch J.A.; "Amino acid sequence of the signal peptide of mitochondrial nicotinamide nucleotide transhydrogenase as determined from the sequence of its messenger RNA."; Biochem. Biophys. Res. Commun. 157:24-29(1988).
[3]	NUCLEOTIDE SEQUENCE [MRNA] OF 52-1086, AND PROTEIN SEQUENCE OF 44-58. PubMed=3277960 [NCBI, ExPASy, EBI, Israel, Japan] Yamaguchi M., Hatefi Y., Trach K., Hoch J.A.; "The primary structure of the mitochondrial energy-linked nicotinamide nucleotide transhydrogenase deduced from the sequence of cDNA clones."; J. Biol. Chem. 263:2761-2767(1988).
[4]	PROTEIN SEQUENCE OF 280-290 AND 1044-1049. PubMed=3325062 [NCBI, ExPASy, EBI, Israel, Japan] Wakabayashi S., Hatefi Y.; "Characterization of the substrate-binding sites of the mitochondrial nicotinamide nucleotide transhydrogenase."; Biochem. Int. 15:915-924(1987).
[5]	PROTEIN SEQUENCE OF 291-302. PubMed=3426633 [NCBI, ExPASy, EBI, Israel, Japan] Wakabayashi S., Hatefi Y.; "Amino acid sequence of the NAD (H)-binding region of the mitochondrial nicotinamide nucleotide transhydrogenase modified by N,N'-dicyclohexylcarbodiimide."; Biochem. Int. 15:667-675(1987).
[6]	TOPOLOGY. PubMed=2005110 [NCBI, ExPASy, EBI, Israel, Japan] Yamaguchi M., Hatefi Y.; "Mitochondrial energy-linked nicotinamide nucleotide transhydrogenase. Membrane topography of the bovine enzyme."; J. Biol. Chem. 266:5728-5735(1991).
[7]	X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 903-1086. DOI=10.1038/70067; PubMed=10581554 [NCBI, ExPASy, EBI, Israel, Japan] Prasad G.S., Sridhar V., Yamaguchi M., Hatefi Y., Stout C.D.; "Crystal structure of transhydrogenase domain III at 1.2 A resolution."; Nat. Struct. Biol. 6:1126-1131(1999).

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.
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

BC114660; AAI14661.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
J03534; AAA30660.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M22754; AAA30717.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L02543; AAA21440.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A31670; DEBOXM.

NP_776368.1; -.

3D structure databases

PDB

1D4O; X-ray; 1.21 A; A=903-1086.

[ExPASy / RCSB / EBI]

PDBsum

1D4O; -.

ModBase

P11024.

Ontologies

GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005743;	Cellular component: mitochondrial inner membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0008750;	Molecular function: NAD(P)+ transhydrogenase (AB-specific) activity (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0015992;	Biological process: proton transport (inferred from electronic annotation from InterPro).
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.

Genome annotation databases

Ensembl

ENSBTAG00000011885; Bos taurus. [Contig view]

GeneID

280878; -.

KEGG

bta:280878; -.

Phylogenomic databases

HOVERGEN

P11024; -.

Other

ProtoNet

P11024.

UniRef

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

Keywords

3D-structure; Direct protein sequencing; 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.`
`CHAIN`	`44 1086`	`1043`	`NAD(P) transhydrogenase, mitochondrial.`	`PRO_0000001054`
`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).`
`HELIX`	`914 923`	`10`
`STRAND`	`925 931`	`7`
`HELIX`	`933 937`	`5`
`TURN`	`938 940`	`3`
`HELIX`	`941 953`	`13`
`STRAND`	`957 962`	`6`
`STRAND`	`967 969`	`3`
`HELIX`	`972 980`	`9`
`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`	`1038 1045`	`8`
`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: 113854 Da [This is the MW of the unprocessed precursor]

CRC64: E3663B533B8E7E35 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MANLLKTVVT GCSCPFLSNL GSCKVLPGKK NFLRTFHTHR ILWCSAPVKP GIPYKQLTVG 

        70         80         90        100        110        120 
VPKEIFQNEK RVALSPAGVQ ALVKQGFNVV VESGAGEASK FSDDHYRAAG AQIQGAKEVL 

       130        140        150        160        170        180 
ASDLVVKVRA PMLNPTLGVH EADLLKTSGT LISFIYPAQN PDLLNKLSKR 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 PGKKAPILFN KEMIESMKEG SVVVDLAAEA GGNFETTKPG 

       370        380        390        400        410        420 
ELYVHKGITH IGYTDLPSRM ATQASTLYSN NITKLLKAIS PDKDNFYFEV KDDFDFGTMG 

       430        440        450        460        470        480 
HVIRGTVVMK DGQVIFPAPT PKNIPQGAPV KQKTVAELEA EKAATITPFR KTMTSASVYT 

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

       550        560        570        580        590        600 
GGLVLMGGHL YPSTTSQGLA ALATFISSVN IAGGFLVTQR MLDMFKRPTD PPEYNYLYLL 

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

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

       730        740        750        760        770        780 
EYIIEYPHFA TDAAANLTKI VAYLGTYIGG VTFSGSLVAY GKLQGILKSA PLLLPGRHLL 

       790        800        810        820        830        840 
NAGLLAGSVG GIIPFMMDPS 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 LSEQGKKVRF 

       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

P11024 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