ID H0Z495_TAEGU Unreviewed; 849 AA.
AC H0Z495;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN Name=ATP6V0A2 {ECO:0000313|Ensembl:ENSTGUP00000005390.2};
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000005390.2, ECO:0000313|Proteomes:UP000007754};
RN [1] {ECO:0000313|Ensembl:ENSTGUP00000005390.2, ECO:0000313|Proteomes:UP000007754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20360741; DOI=10.1038/nature08819;
RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E.,
RA Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P.,
RA Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O.,
RA Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L.,
RA McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C.,
RA Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K.,
RA Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z.,
RA Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T.,
RA Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A.,
RA Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L.,
RA Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT "The genome of a songbird.";
RL Nature 464:757-762(2010).
RN [2] {ECO:0000313|Ensembl:ENSTGUP00000005390.2}
RP IDENTIFICATION.
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 AlphaFoldDB; H0Z495; -.
DR STRING; 59729.ENSTGUP00000005390; -.
DR Ensembl; ENSTGUT00000005444.2; ENSTGUP00000005390.2; ENSTGUG00000005182.2.
DR GeneTree; ENSGT00950000182881; -.
DR HOGENOM; CLU_005230_0_0_1; -.
DR InParanoid; H0Z495; -.
DR OMA; TYVQLYI; -.
DR OrthoDB; 1967517at2759; -.
DR TreeFam; TF300346; -.
DR Proteomes; UP000007754; Chromosome 15.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:1902495; C:transmembrane transporter complex; IEA:Ensembl.
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 GO; GO:0036295; P:cellular response to increased oxygen levels; IEA:Ensembl.
DR GO; GO:0006879; P:intracellular iron ion homeostasis; IEA:Ensembl.
DR InterPro; IPR002490; V-ATPase_116kDa_su.
DR InterPro; IPR026028; V-type_ATPase_116kDa_su_euka.
DR PANTHER; PTHR11629:SF22; V-TYPE PROTON ATPASE 116 KDA SUBUNIT A 2; 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:UP000007754};
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 410..435
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 456..473
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 548..566
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 578..601
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 645..667
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 779..802
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT COILED 94..128
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 849 AA; 97272 MW; 4DF1F135B2605D34 CRC64;
MGALFRGEPV CLAQLFLQSG SAYECLSEVG ERGLAEFRDL NPNVSVFQRK YVNEVKKCEE
MERILGYLVQ EIKKADIPLP EGDVAPPAPL LKHILEIQEQ LQKLETELRE VTLNKEKLRK
NLLELTEYKY MLQITQNFVR RTPEYESHLH GNFEEFSSVE NEPLVDYNCT HRLSASLGFI
SGLVHIAKIE AFEKMLWRVC KGYPFLTYAE LDKDLEDPDT GKTTKWAVFL VSYWGEQIGQ
KVKKICDCYR CHVYPYPDTT EERQAVVEGL NVRIQDLETV LNKTEEYLHQ VLYKASESIY
TWVIQVKKMK AIYHVLNLCS FDVTNKCLIA EVWCPVADLQ NLRHALEEGS RKSGATISSF
MNTIPTTQPP PTLIRTNKFT SGFQNIVDAY GVGSYGEVNP ALYTIITFPF LFAVMFGDFG
HGLLMFIFAL LAIMYENHPR LKRAQDEIMK MLFEGRYVIL LMGLFSIYTG LIYNDCFSKS
INIFGSGWNV SAMYEKVWSD KDVESNRYLA LDPNVSGVYN GAYPFGIDPI WNLASNRLTF
LNSFKMKMSV IFGVTHMTFG VVLGLFNHLH FKKTYNIYLV FIPELLFMLC IFGYLVFMIF
FKWLAYSAEN STAAPSILIQ FINMFLFPSG ETQSFFNGQV PLQKFLLSVA FLCVPVMLLG
KPLYLYWLHS GGRGIRMYRS GYKLIRKESE EELCLLSCPD LEEGVSHSDS GHREGDAEEL
NFADVFMNQA IHTIEYCLGC ISNTASYLRL WALSLAHAQL SEVLWQMVMR VGLRVDTKYG
VLLLIPVMAF FAVLTVFILL VMEGLSAFLH AIRLHWVEFQ NKFYSGGGYK FTPFSFKHIS
LHFNKDGAL
//
