Reviewed, UniProtKB/Swiss-Prot P91929 (NDUAA_DROME)

Names and origin

Protein names

Recommended name:
    NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial
Alternative name(s):
    NADH-ubiquinone oxidoreductase 42 kDa subunit
    Complex I-42kD
      Short name=CI-42kD

Gene names

Name:	ND42
ORF Names:	CG6343

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	407 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone By similarity.
Cofactor	Binds 1 FAD per subunit By similarity.
Subunit structure	Complex I is composed of 45 different subunits. This a component of the hydrophobic protein fraction By similarity.
Subcellular location	Mitochondrion matrix.
Sequence similarities	Belongs to the complex I NDUFA10 subunit family.

Ontologies

Keywords
Biological process	Electron transport Respiratory chain Transport
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	FAD Flavoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW nucleobase, nucleoside, nucleotide and nucleic acid metabolic process Inferred from electronic annotation. Source: InterPro transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell respiratory chain Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: InterPro phosphotransferase activity, alcohol group as acceptor Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	Q9VWF3	1	EBI-157155,EBI-157448

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 60	60	Mitochondrion Potential
	Chain	61 – 407	347	NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial		PRO_0000019990
Experimental info
	Sequence conflict	177	1	H → R in CAA71852. Ref.4
	Sequence conflict	198	1	M → L in CAA71852. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P91929-1 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: 4B5F4EC7DED9B8D4	FASTA	407	46,898
	10 20 30 40 50 60 MTAVFRVGLV RLVSRATQSP NLLQAQTNAL PAAFQQRCSI SGKTMRGGPR VPKAAPYPYK 70 80 90 100 110 120 TKKYSVFNAI FDKTSKRFDE NSKVICVEGP IAAGKSKFAK ELAEELDMEY YPAVDLDLIY 130 140 150 160 170 180 INSYGYDMRK LDPQLPPSCR SYDVRNFCLD PSHDLAAQFQ IRMYMLRYSQ YIDALQHVLS 190 200 210 220 230 240 TGQGVVLERS PYSDFVFMEA MFRQGYLSRG ARSVYNELRQ NTIGELLKPH LVIYLDLPVD 250 260 270 280 290 300 AVKKQIKARN VDYEVQSKVF SDAYLSDLEQ LYKQQYLKDI STHAELLIYD WTAGGETEVV 310 320 330 340 350 360 VEDIERIDFN QFEADIHNKK MLDWRFPLEA EWCEARIKYC HEKPDLMNYF NVPRFDVPEL 370 380 390 400 VRSADDGKVW RDVWFNAPGM KYRPGYNADM GDEGLLTKTK IGINQGI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[2]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[3]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[4]	"Identification of nuclear genes encoding mitochondrial proteins: isolation of a collection of D. melanogaster cDNAs homologous to sequences in the Human Gene Index database." Caggese C., Ragone G., Perrini B., Moschetti R., de Pinto V., Caizzi R., Barsanti P. Mol. Gen. Genet. 261:64-70(1999) [PubMed: 10071211] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 45-205. Tissue: Ovary.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE014297 Genomic DNA. Translation: AAF55947.1. AY051764 mRNA. Translation: AAK93188.1. Y10911 mRNA. Translation: CAA71852.1.
RefSeq	NP_524445.1. NP_732692.1.
UniGene	Dm.1653
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-21667N.
IntAct	P91929. 5 interactions.
STRING	P91929.
Genome annotation databases
Ensembl	FBtr0084172; FBpp0083570; FBgn0019957; Drosophila melanogaster. [Genome view] FBtr0084173; FBpp0083571; FBgn0019957; Drosophila melanogaster. [Genome view]
GeneID	42591.
KEGG	dme:Dmel_CG6343.
Organism-specific databases
CTD	42591.
FlyBase	FBgn0019957. ND42.
Phylogenomic databases
InParanoid	P91929.
OMA	HAELLIY.
OrthoDB	EOG9FJ8GW.
Enzyme and pathway databases
BioCyc	DMEL-XXX-02:DMEL-XXX-02-012754-MON. DMEL-XXX-02:DMEL-XXX-02-012755-MON.
Gene expression databases
ArrayExpress	P91929.
GermOnline	CG6343. Drosophila melanogaster.
Family and domain databases
InterPro	IPR002624. Deoxynucleoside_kinase. IPR015828. NADH_UbQ_OxRdtase_42KD_su. [Graphical view]
PANTHER	PTHR10513. dNK. 1 hit.
Pfam	PF01712. dNK. 1 hit. [Graphical view]
PIRSF	PIRSF000543. NADH_UQ_42KD. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	829575.

Entry information

Entry name

NDUAA_DROME

Accession

Primary (citable) accession number: P91929
Secondary accession number(s): Q9VD54

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	December 1, 2000
Last modified:	December 15, 2009
This is version 81 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project