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Protein

ATP synthase subunit f, mitochondrial

Gene

ATP5J2

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processATP synthesis, Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

ReactomeiR-BTA-163210. Formation of ATP by chemiosmotic coupling.
R-BTA-8949613. Cristae formation.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit f, mitochondrial
Gene namesi
Name:ATP5J2
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 25

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei55 – 72HelicalSequence analysisAdd BLAST18

Keywords - Cellular componenti

CF(0), Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity1 Publication
ChainiPRO_00001948232 – 88ATP synthase subunit f, mitochondrialAdd BLAST87

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei3PhosphoserineBy similarity1
Modified residuei16N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ28851.
PeptideAtlasiQ28851.
PRIDEiQ28851.

Expressioni

Gene expression databases

BgeeiENSBTAG00000002094.

Interactioni

Subunit structurei

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 MP68.1 Publication

Protein-protein interaction databases

IntActiQ28851. 1 interactor.
MINTiMINT-5007087.
STRINGi9913.ENSBTAP00000041308.

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase F chain family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4092. Eukaryota.
ENOG4111PBN. LUCA.
GeneTreeiENSGT00510000046986.
HOGENOMiHOG000034215.
HOVERGENiHBG002418.
InParanoidiQ28851.
KOiK02130.
OMAiHKYVQPK.
OrthoDBiEOG091G194E.
TreeFamiTF342865.

Family and domain databases

InterProiView protein in InterPro
IPR019344. F1F0-ATPsyn_F_prd.
PANTHERiPTHR13080. PTHR13080. 1 hit.
PfamiView protein in Pfam
PF10206. WRW. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q28851-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASVVPLKEK KLLEVKLGEL PSWILMRDFT PSGIAGAFQR GYYRYYNKYV
60 70 80
NVKKGSIAGL SMVLAAYVFL NYCRSYKELK HERLRKYH
Length:88
Mass (Da):10,297
Last modified:January 23, 2007 - v3
Checksum:iAC5D4BF93F53277B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti42Y → N in AAI08209 (Ref. 2) Curated1
Sequence conflicti60L → H in AAI08209 (Ref. 2) Curated1

Mass spectrometryi

Molecular mass is 10209.2 Da from positions 2 - 88. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S70447 mRNA. Translation: AAB31107.2.
BC108208 mRNA. Translation: AAI08209.1.
PIRiA54211.
RefSeqiNP_001107191.1. NM_001113719.2.
UniGeneiBt.59381.

Genome annotation databases

EnsembliENSBTAT00000043764; ENSBTAP00000041308; ENSBTAG00000002094.
GeneIDi506492.
KEGGibta:506492.

Similar proteinsi

Entry informationi

Entry nameiATPK_BOVIN
AccessioniPrimary (citable) accession number: Q28851
Secondary accession number(s): Q32P94
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: June 7, 2017
This is version 109 of the entry and version 3 of the sequence. See 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. SIMILARITY comments
    Index of protein domains and families