ID A0A3Q7RKJ9_VULVU Unreviewed; 838 AA.
AC A0A3Q7RKJ9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN Name=ATP6V0A1 {ECO:0000313|RefSeq:XP_025842816.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025842816.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025842816.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025842816.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025842816.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Essential component of the vacuolar proton pump (V-ATPase), a
CC multimeric enzyme that catalyzes the translocation of protons across
CC the membranes. Required for assembly and activity of the V-ATPase.
CC {ECO:0000256|RuleBase:RU361189}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
CC membrane {ECO:0000256|ARBA:ARBA00029431}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00029431}. Cytoplasmic vesicle, secretory
CC vesicle, synaptic vesicle membrane {ECO:0000256|ARBA:ARBA00004644};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004644}. Melanosome
CC {ECO:0000256|ARBA:ARBA00004223}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00009904, ECO:0000256|RuleBase:RU361189}.
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DR RefSeq; XP_025842816.1; XM_025987031.1.
DR AlphaFoldDB; A0A3Q7RKJ9; -.
DR Proteomes; UP000286640; Unplaced.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR InterPro; IPR002490; V-ATPase_116kDa_su.
DR InterPro; IPR026028; V-type_ATPase_116kDa_su_euka.
DR PANTHER; PTHR11629:SF68; V-TYPE PROTON ATPASE 116 KDA SUBUNIT A 1; 1.
DR PANTHER; PTHR11629; VACUOLAR PROTON ATPASES; 1.
DR Pfam; PF01496; V_ATPase_I; 1.
DR PIRSF; PIRSF001293; ATP6V0A1; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781,
KW ECO:0000256|RuleBase:RU361189};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU361189};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361189};
KW Reference proteome {ECO:0000313|Proteomes:UP000286640};
KW Synapse {ECO:0000256|ARBA:ARBA00023018};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361189};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361189};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU361189}.
FT TRANSMEM 401..425
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 445..464
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 542..563
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 569..593
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 634..658
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 742..765
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 771..794
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT COILED 94..128
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 838 AA; 96392 MW; 3FC0DFF97E612556 CRC64;
MGELFRSEEM TLAQLFLQSE AAYCCVSELG ELGKVQFRDL NPDVNVFQRK FVNEVRRCEE
MDRKLRFVEK EIRKANIPIM DTGENPEVPF PRDMIDLEAN FEKIENELKE INTNQEALKR
NFLELTELKF ILRKTQQFFD EMADPDLLEE SSSLLEPSEM GRGTPLRLGF VAGVINRERI
PTFERMLWRV CRGNVFLRQA EIENPLEDPV TGDYVHKSVF IIFFQGDQLK NRVKKICEGF
RASLYPCPET PQERKEMASG VNTRIDDLQM VLNQTEDHRQ RVLQAAAKNI RVWFIKVRKM
KAIYHTLNLC NIDVTQKCLI AEVWCPVTDL DSIQFALRRG TEHSGSTVPS ILNRMQTNQT
PPTYNKTNKF TYGFQNIVDA YGIGTYREIN PAPYTIITFP FLFAVMFGDF GHGILMTLFA
VWMVLRESRI LSQKNENEMF STVFSGRYII LLMGVFSIYT GLIYNDCFSK SLNIFGSSWS
VRPMFTIYNW TEETLRGNPV LQLNPSVRGV FGGPYPFGID PIWNIATNKL TFLNSFKMKT
SVILGIIHMM FGVTLSLFNH IYFKKPLNIY FGFIPEIIFM TSLFGYLVIL IFYKWTAYNA
DTSEKAPSLL IHFINMFLFS YGDSSNSMLY SGQKGIQCFL VVVALLCVPW MLLFKPLVLR
HQYLRRKHLG TLNFGGIRVG NGPTEEDAEI IQHDQLSTHS EDAEEPTEDE VFDFGDTMVH
QAIHTIEYCL GCISNTASYL RLWALSLAHA QLSEVLWTMV IHIGLSVKSL AGGLALFFIF
AAFATLTVAI LLIMEGLSAF LHALRLHWVE FQNKFYSGTG FKFLPFSFEH IREGKFDE
//