P56135 (ATPK_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP synthase subunit f, mitochondrial

Gene names

Name:

Atp5j2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	88 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	Mitochondrial membrane ATP synthase (F1F0 ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F1 - containing the extramembraneous catalytic core and F0 - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F0 domain. Minor subunit located with subunit a in the membrane.
Subunit structure	F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF0 seems to have nine subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L). Component of an ATP synthase complex composed of ATP5F1, ATP5G1, ATP5E, ATP5H, ATP5I, ATP5J, ATP5J2, MT-ATP6, MT-ATP8, ATP5A1, ATP5B, ATP5D, ATP5C1, ATP5O, ATP5L, USMG5 and MP68 By similarity.
Subcellular location	Mitochondrion. Mitochondrion inner membrane; Single-pass membrane protein Potential.
Sequence similarities	Belongs to the ATPase F chain family.

Ontologies

Keywords
Biological process	ATP synthesis Hydrogen ion transport Ion transport Transport
Cellular component	CF(0) Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transmembrane Transmembrane helix
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ATP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW proton transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial proton-transporting ATP synthase complex Inferred from sequence or structural similarity. Source: UniProtKB proton-transporting ATP synthase complex, coupling factor F(o) Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATPase activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 88	87	ATP synthase subunit f, mitochondrial		PRO_0000194825
Regions
	Transmembrane	57 – 76	20	Helical; Potential
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P56135 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 89526C72EC436E48	FASTA	88	10,344
	10 20 30 40 50 60 MASLVPLKEK KLMEVKLGEL PSWIMMRDFT PSGIAGAFRR GYDRYYNKYI NVRKGSISGI 70 80 SMVLAAYVVF SYCISYKELK HERRRKYH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Growth suppression of Escherichia coli by induction of expression of mammalian genes with transmembrane or ATPase domains." Inoue S., Sano H., Ohta M. Biochem. Biophys. Res. Commun. 268:553-561(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and DBA/2. Tissue: Bone marrow, Embryo and Kidney.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Czech II. Tissue: Mammary gland.
[4]	Lubec G., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 17-39, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB030192 mRNA. Translation: BAA92756.1. AK002519 mRNA. Translation: BAB22157.1. AK003235 mRNA. Translation: BAB22660.1. AK003817 mRNA. Translation: BAB23014.1. AK013130 mRNA. Translation: BAB28667.1. AK151737 mRNA. Translation: BAE30651.1. AK168095 mRNA. Translation: BAE40067.1. BC029226 mRNA. Translation: AAH29226.1.
IPI	IPI00271986.
RefSeq	NP_065607.1. NM_020582.2.
UniGene	Mm.133551.
3D structure databases
ProteinModelPortal	P56135.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-1843047.
PTM databases
PhosphoSite	P56135.
Proteomic databases
PaxDb	P56135.
PRIDE	P56135.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000161741; ENSMUSP00000125504; ENSMUSG00000038690.
GeneID	57423.
KEGG	mmu:57423.
UCSC	uc009amk.1. mouse.
Organism-specific databases
CTD	9551.
MGI	MGI:1927558. Atp5j2.
Phylogenomic databases
eggNOG	NOG292892.
GeneTree	ENSGT00510000046986.
HOGENOM	HOG000034215.
HOVERGEN	HBG002418.
InParanoid	P56135.
KO	K02130.
OMA	QLTVASM.
OrthoDB	EOG4NVZMX.
Gene expression databases
ArrayExpress	P56135.
Bgee	P56135.
Genevestigator	P56135.
GermOnline	ENSMUSG00000038690. Mus musculus.
Family and domain databases
InterPro	IPR019344. F1F0-ATPsyn_F_prd. [Graphical view]
PANTHER	PTHR13080. PTHR13080. 1 hit.
Pfam	PF10206. WRW. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ATP5J2. mouse.
NextBio	313776.
SOURCE	Search...

Entry information

Entry name

ATPK_MOUSE

Accession

Primary (citable) accession number: P56135
Secondary accession number(s): Q3THX9, Q9JMF4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 88 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program