ID Q5B1H4_EMENI Unreviewed; 852 AA.
AC Q5B1H4; C8VFZ6;
DT 26-APR-2005, integrated into UniProtKB/TrEMBL.
DT 26-APR-2005, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN ORFNames=ANIA_05606 {ECO:0000313|EMBL:CBF81569.1};
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321 {ECO:0000313|EMBL:CBF81569.1, ECO:0000313|Proteomes:UP000000560};
RN [1] {ECO:0000313|Proteomes:UP000000560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC {ECO:0000313|Proteomes:UP000000560};
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.J., Wortman J.R., Batzoglou S.,
RA Lee S.I., Basturkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M., Hynes M., Paoletti M., Fischer R., Miller B.,
RA Dyer P., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2] {ECO:0000313|Proteomes:UP000000560}
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC {ECO:0000313|Proteomes:UP000000560};
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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; BN001305; CBF81569.1; -; Genomic_DNA.
DR RefSeq; XP_663210.1; XM_658118.1.
DR AlphaFoldDB; Q5B1H4; -.
DR STRING; 227321.Q5B1H4; -.
DR EnsemblFungi; CBF81569; CBF81569; ANIA_05606.
DR GeneID; 2871898; -.
DR KEGG; ani:AN5606.2; -.
DR VEuPathDB; FungiDB:AN5606; -.
DR eggNOG; KOG2189; Eukaryota.
DR HOGENOM; CLU_005230_0_2_1; -.
DR InParanoid; Q5B1H4; -.
DR OMA; FYLWFFL; -.
DR OrthoDB; 1967517at2759; -.
DR Proteomes; UP000000560; Chromosome V.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IBA:GO_Central.
DR GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IBA:GO_Central.
DR GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR GO; GO:0051117; F:ATPase binding; IBA:GO_Central.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0007035; P:vacuolar acidification; IBA:GO_Central.
DR InterPro; IPR002490; V-ATPase_116kDa_su.
DR InterPro; IPR026028; V-type_ATPase_116kDa_su_euka.
DR PANTHER; PTHR11629:SF63; V-TYPE PROTON ATPASE SUBUNIT A; 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:UP000000560};
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 426..451
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 463..488
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 550..568
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 580..603
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 643..662
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 785..808
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT COILED 100..127
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 852 AA; 97292 MW; B55EAA51BB63203B CRC64;
MAPKDTFFRS SDMSLTQLYI ANEIGREVVS ALGELGQVQF RDLNPETNAF QKTFTKEIRR
LDNVERQLRY FHAQMDKAGI QMRPSSEFSD TLAAPLASEI DELAERSESL EQRIASLNDS
YETLKKREVE LTEWRWVLRE AGGFFDRAHT HTEEIRQSFD NDEAPLLRDV EQQNHRGANG
DAQGQQSFLE LNIGFVSGVI PRDRIGAFER ILWRTLRGNL YMNQAEIPDP IVDPTTNEET
QKMVFVIFAH GKNIIAKIRK ISESLGASLY SVDENSELRR DQIHEVNTRL SDVNNVLRNT
KNTLDAELSQ IARSLAAWMI IVKKEKAVYD TLNKCSYDQA RKTLIAEAWC PTNSLSLIKS
TLQDVNDRAG LSVPSIVNQI RTNKTPPTYV RTNKFTEAFQ TIVDAYGISK YSEVNPGLYT
VVTFPFLFAV MFGDFGHGFL MALAAAAMIF WERQLSKTKL DELTYMAFYG RYIMLMMGIF
SMYTGLIYND IFSKSFTVFS SSWKWPDNIE QGQSVEASLK GSYRFPFGLD WNWHEAENSL
LFTNSLKMKM SIILGWAHMT YALILQYVNA RHFKSKVDII GNFIPGIIFF QSIFGYLVLT
IIYKWSVDWP ARNQSPPGLL NMLIFMFLSP GNVEEELYPG QGGVQLCLLL LAVAQVPIML
FFKPFYLRRE HNRARALGYR GLGEQSRVSA LDEDGDLDGP RQSTASDGEG VAMIAQDLEE
EHEEFDFSEI MIHQVIHTIE FCLNCISHTA SYLRLWALSL AHQQLSIVLW DMTLGTAFDQ
EDGTIRTIMI IVTFYMWFTL TIAILCVMEG TSAMLHSLRL HWVEAMSKHF MGDGIPFAPF
SFKTLLEEDP VD
//