UniProtKB - P26360 (ATPG3_IPOBA)
ATP synthase subunit gamma, mitochondrial
ATPC
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 F1 domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha3beta3. Rotation of the central stalk against the surrounding alpha3beta3 subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
GO - Molecular functioni
- proton-transporting ATP synthase activity, rotational mechanism Source: InterPro
Keywordsi
Biological process | ATP synthesis, Hydrogen ion transport, Ion transport, Transport |
Names & Taxonomyi
Protein namesi | Recommended name: ATP synthase subunit gamma, mitochondrialAlternative name(s): F-ATPase gamma subunit |
Gene namesi | Name:ATPC |
Organismi | Ipomoea batatas (Sweet potato) (Convolvulus batatas) |
Taxonomic identifieri | 4120 [NCBI] |
Taxonomic lineagei | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliopsida › eudicotyledons › Gunneridae › Pentapetalae › asterids › lamiids › Solanales › Convolvulaceae › Ipomoeeae › Ipomoea |
Subcellular locationi
Mitochondrion
- Mitochondrion
- Mitochondrion inner membrane By similarity; Peripheral membrane protein By similarity
Mitochondrion
- mitochondrial inner membrane Source: UniProtKB-SubCell
Other locations
- proton-transporting ATP synthase complex, catalytic core F(1) Source: UniProtKB-KW
Keywords - Cellular componenti
CF(1), Membrane, Mitochondrion, Mitochondrion inner membranePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Transit peptidei | 1 – 45 | Mitochondrion1 PublicationAdd BLAST | 45 | |
ChainiPRO_0000002683 | 46 – 326 | ATP synthase subunit gamma, mitochondrialAdd BLAST | 281 |
Interactioni
Subunit structurei
F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. CF0 has three main subunits: a, b and c.
Family & Domainsi
Sequence similaritiesi
Keywords - Domaini
Transit peptideFamily and domain databases
CDDi | cd12151, F1-ATPase_gamma, 1 hit |
HAMAPi | MF_00815, ATP_synth_gamma_bact, 1 hit |
InterProi | View protein in InterPro IPR035968, ATP_synth_F1_ATPase_gsu IPR000131, ATP_synth_F1_gsu IPR023632, ATP_synth_F1_gsu_CS |
PANTHERi | PTHR11693, PTHR11693, 1 hit |
Pfami | View protein in Pfam PF00231, ATP-synt, 1 hit |
PRINTSi | PR00126, ATPASEGAMMA |
SUPFAMi | SSF52943, SSF52943, 1 hit |
TIGRFAMsi | TIGR01146, ATPsyn_F1gamma, 1 hit |
PROSITEi | View protein in PROSITE PS00153, ATPASE_GAMMA, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
10 20 30 40 50
MAMAALRREG RRLAAAPFTS PTPLNALRSS LVSPSEEIGL SGVRSISTQV
60 70 80 90 100
VRNRMKSVKN IQKITKAMKM VAASKLRAIQ TRAENSRGLW QPFTALLGDT
110 120 130 140 150
PSVDVKKNVI ITISSDKGLC GGINSTSVKT SRNIHKLNSG PEKENKYVIL
160 170 180 190 200
GEKAKAQLVR DSKKDIELII TELQKNPLNY TQVSVVADDI LKNVEFDALR
210 220 230 240 250
IVFNKFQSVV SFVPTMSTVL SPEVVERESE SGGKLGDLDS YEIEGAESKS
260 270 280 290 300
EVLQNLTEFQ FSSVLFNAVL ENACSEQGAR MSAMDSSSRN AGEMLDRLTL
310 320
TYNRTRQASI TTELIEIISG ASALEG
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 65 – 66 | TK → IS AA sequence (PubMed:2536736).Curated | 2 | |
Sequence conflicti | 74 | S → A AA sequence (PubMed:2536736).Curated | 1 | |
Sequence conflicti | 80 | Q → N AA sequence (PubMed:2536736).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D14699 mRNA Translation: BAA03526.1 |
PIRi | A47493 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D14699 mRNA Translation: BAA03526.1 |
PIRi | A47493 |
3D structure databases
SMRi | P26360 |
ModBasei | Search... |
Family and domain databases
CDDi | cd12151, F1-ATPase_gamma, 1 hit |
HAMAPi | MF_00815, ATP_synth_gamma_bact, 1 hit |
InterProi | View protein in InterPro IPR035968, ATP_synth_F1_ATPase_gsu IPR000131, ATP_synth_F1_gsu IPR023632, ATP_synth_F1_gsu_CS |
PANTHERi | PTHR11693, PTHR11693, 1 hit |
Pfami | View protein in Pfam PF00231, ATP-synt, 1 hit |
PRINTSi | PR00126, ATPASEGAMMA |
SUPFAMi | SSF52943, SSF52943, 1 hit |
TIGRFAMsi | TIGR01146, ATPsyn_F1gamma, 1 hit |
PROSITEi | View protein in PROSITE PS00153, ATPASE_GAMMA, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | ATPG3_IPOBA | |
Accessioni | P26360Primary (citable) accession number: P26360 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 1, 1992 |
Last sequence update: | June 1, 1994 | |
Last modified: | February 23, 2022 | |
This is version 101 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Plant Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Direct protein sequencingDocuments
- SIMILARITY comments
Index of protein domains and families