ID H0VIY1_CAVPO Unreviewed; 834 AA.
AC H0VIY1;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN Name=ATP6V0A4 {ECO:0000313|Ensembl:ENSCPOP00000010188.3};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000010188.3, ECO:0000313|Proteomes:UP000005447};
RN [1] {ECO:0000313|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSCPOP00000010188.3}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000010188.3};
RG Ensembl;
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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {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 EMBL; AAKN02015503; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAKN02015504; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAKN02015505; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003475561.1; XM_003475513.2.
DR RefSeq; XP_013014078.1; XM_013158624.1.
DR RefSeq; XP_013014079.1; XM_013158625.1.
DR STRING; 10141.ENSCPOP00000025919; -.
DR Ensembl; ENSCPOT00000011438.3; ENSCPOP00000010188.3; ENSCPOG00000011332.4.
DR Ensembl; ENSCPOT00000044892.1; ENSCPOP00000025919.1; ENSCPOG00000011332.4.
DR GeneID; 100735854; -.
DR KEGG; cpoc:100735854; -.
DR CTD; 50617; -.
DR VEuPathDB; HostDB:ENSCPOG00000011332; -.
DR eggNOG; KOG2189; Eukaryota.
DR GeneTree; ENSGT00950000182881; -.
DR HOGENOM; CLU_005230_0_0_1; -.
DR OMA; YFRKTHN; -.
DR OrthoDB; 1967517at2759; -.
DR TreeFam; TF300346; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000011332; Expressed in adult mammalian kidney and 6 other cell types or tissues.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0031526; C:brush border membrane; IEA:Ensembl.
DR GO; GO:0005768; C:endosome; IEA:Ensembl.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR GO; GO:0051117; F:ATPase binding; IEA:Ensembl.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0001503; P:ossification; IEA:Ensembl.
DR GO; GO:0006885; P:regulation of pH; IEA:Ensembl.
DR GO; GO:0097254; P:renal tubular secretion; IEA:Ensembl.
DR GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
DR GO; GO:0097401; P:synaptic vesicle lumen acidification; IEA:Ensembl.
DR InterPro; IPR002490; V-ATPase_116kDa_su.
DR InterPro; IPR026028; V-type_ATPase_116kDa_su_euka.
DR PANTHER; PTHR11629:SF26; V-TYPE PROTON ATPASE 116 KDA SUBUNIT A 4; 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 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:UP000005447};
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 398..427
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 447..466
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 545..566
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 572..596
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 642..661
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 765..790
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT REGION 682..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 58..127
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 682..696
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 834 AA; 95648 MW; A65F41F36D7DC8A5 CRC64;
MASVFRSEEM CLSQLFLQVE AAYCCVAELG ELGLVQFKDL NASVNSFQRR FVNEVRRCES
LERILRFLED EMQNEITVHL PEKYPQIPLP REMIGLETTL EKLEGELQEA NQNHQALKKS
FLELTELKYL LKKTQDFFET EANLAEDFFT EDTSGLLELR AVPAFMAGKL GFMVGVINRE
RMASFERLLW RVCRGNIYLK FSEMDTPLED PVTREEIKKN IFIIFYQGEQ LRQKVKKICD
GFRATVYPCP EPAAERREML AGVNVRLEDL ITVITQTESH RQRLLQEAAA NWHCWATKVQ
KMKAIYHILN MCNIDVTQQC VIAEIWFPVA DTARIKRALE QGMELSGSSM APIMTEVQSR
TAPPTFNRTN KFTAGFQNIV DAYGVGSYRE MNPAPYTIIT FPFLFAVMFG DCGHGAVMLL
GALWMVLNEQ RLLSQKSSNE IWNTFFHGRY LILLMGIFSI YTGLIYNDCF SKSFNIFGSS
WSVQPMFRNG TWNAEIVETT PHLQLDPALP GVYSGNPYPF GIDPIWNLAS NKLTFLNSYK
MKMSVILGIV QMVFGVVLSL FNHIYFRKTY NIILQFIPEM IFILCLFGYL VFMIIFKWCQ
YDAHMSQSAP SILIHFINMF LFDYDSSSNV PLYEHQQEVQ TFFVVMALVS VPWMLLIKPF
FLRAKHRKSQ LQAFLVQENT TEDVEGGISS PSGSADTHEA QDDHEEEFNF GDVFVHQAIH
TIEYCLGCVS NTASYLRLWA LSLAHSELSE VLWTMVMNIG LRLQGWGGFI GVFVIFAVFA
VLTVAILLIM EGLSAFLHAL RLHWVEFQNK FYVGAGYKFS PFSFKNILEG TAEE
//