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Protein

ATP synthase subunit g, mitochondrial

Gene

ATP5L

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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

  • proton transmembrane transporter activity Source: InterPro
  • transmembrane transporter activity Source: UniProtKB

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit g, mitochondrial
Short name:
ATPase subunit g
Gene namesi
Name:ATP5L
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

EuPathDBiHostDB:ENSG00000167283.7
HGNCiHGNC:14247 ATP5L
MIMi617473 gene
neXtProtiNX_O75964

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

Keywords - Cellular componenti

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

Pathology & Biotechi

Organism-specific databases

DisGeNETi10632
OpenTargetsiENSG00000167283
PharmGKBiPA25143

Polymorphism and mutation databases

BioMutaiATP5L

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000716912 – 103ATP synthase subunit g, mitochondrialAdd BLAST102

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei11N6-acetyllysineBy similarity1
Modified residuei24N6-acetyllysineCombined sources1
Modified residuei35N6-acetyllysineBy similarity1
Modified residuei54N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiO75964
MaxQBiO75964
PaxDbiO75964
PeptideAtlasiO75964
PRIDEiO75964
ProteomicsDBi50328
TopDownProteomicsiO75964

PTM databases

CarbonylDBiO75964
iPTMnetiO75964
PhosphoSitePlusiO75964
SwissPalmiO75964

Expressioni

Gene expression databases

BgeeiENSG00000167283
CleanExiHS_ATP5L
ExpressionAtlasiO75964 baseline and differential
GenevisibleiO75964 HS

Organism-specific databases

HPAiHPA044629

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, ATP5MC1, ATP5F1E, ATP5H, ATP5ME, ATP5J, ATP5J2, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5O, ATP5L, USMG5 and MP68 (By similarity).By similarity

Protein-protein interaction databases

BioGridi115876, 59 interactors
CORUMiO75964
IntActiO75964, 27 interactors
MINTiO75964
STRINGi9606.ENSP00000300688

Structurei

3D structure databases

ProteinModelPortaliO75964
SMRiO75964
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase g subunit family.Curated

Phylogenomic databases

eggNOGiKOG4103 Eukaryota
ENOG4111TZ1 LUCA
GeneTreeiENSGT00390000009724
HOGENOMiHOG000007506
HOVERGENiHBG050614
InParanoidiO75964
KOiK02140
OMAiWQYAKVE
OrthoDBiEOG091G16ZZ
PhylomeDBiO75964
TreeFamiTF313978

Family and domain databases

InterProiView protein in InterPro
IPR006808 ATP_synth_F0_gsu_mt
IPR016702 ATP_synth_su_G_mt_met
PANTHERiPTHR12386 PTHR12386, 1 hit
PfamiView protein in Pfam
PF04718 ATP-synt_G, 1 hit
PIRSFiPIRSF017835 ATP-synth_g_mitoch_animal, 1 hit

Sequencei

Sequence statusi: Complete.

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

O75964-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQFVRNLVE KTPALVNAAV TYSKPRLATF WYYAKVELVP PTPAEIPRAI
60 70 80 90 100
QSLKKIVNSA QTGSFKQLTV KEAVLNGLVA TEVLMWFYVG EIIGKRGIIG

YDV
Length:103
Mass (Da):11,428
Last modified:April 26, 2005 - v3
Checksum:i03D484BCF836E6C2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti2A → G in AAC61597 (Ref. 1) Curated1
Sequence conflicti48R → K in AAC61597 (Ref. 1) Curated1
Sequence conflicti57V → A in AAH15128 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF092124 mRNA Translation: AAC61597.1
AF087846 mRNA Translation: AAP97159.1
AF070655 mRNA Translation: AAD20961.1
AL050277 mRNA Translation: CAB43378.1
CR533494 mRNA Translation: CAG38525.1
CR542211 mRNA Translation: CAG47007.1
AK289568 mRNA Translation: BAF82257.1
CH471065 Genomic DNA Translation: EAW67376.1
BC015128 mRNA Translation: AAH15128.1
BC070165 mRNA Translation: AAH70165.1
CCDSiCCDS8397.1
PIRiT08727
RefSeqiNP_006467.4, NM_006476.4
UniGeneiHs.486360

Genome annotation databases

EnsembliENST00000300688; ENSP00000300688; ENSG00000167283
GeneIDi10632
KEGGihsa:10632
UCSCiuc001psx.4 human

Similar proteinsi

Entry informationi

Entry nameiATP5L_HUMAN
AccessioniPrimary (citable) accession number: O75964
Secondary accession number(s): A8K0K3, Q96BV6, Q9UBZ7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: April 26, 2005
Last modified: July 18, 2018
This is version 163 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

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