ID M7X534_RHOT1 Unreviewed; 859 AA.
AC M7X534;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN ORFNames=RHTO_02933 {ECO:0000313|EMBL:EMS25205.1};
OS Rhodotorula toruloides (strain NP11) (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1130832 {ECO:0000313|EMBL:EMS25205.1, ECO:0000313|Proteomes:UP000016926};
RN [1] {ECO:0000313|EMBL:EMS25205.1, ECO:0000313|Proteomes:UP000016926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NP11 {ECO:0000313|EMBL:EMS25205.1,
RC ECO:0000313|Proteomes:UP000016926};
RX PubMed=23047670; DOI=10.1038/ncomms2112;
RA Zhu Z., Zhang S., Liu H., Shen H., Lin X., Yang F., Zhou Y.J., Jin G.,
RA Ye M., Zou H., Zou H., Zhao Z.K.;
RT "A multi-omic map of the lipid-producing yeast Rhodosporidium toruloides.";
RL Nat. Commun. 3:1112-1112(2012).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB722643; EMS25205.1; -; Genomic_DNA.
DR RefSeq; XP_016276324.1; XM_016416605.1.
DR AlphaFoldDB; M7X534; -.
DR GeneID; 27366946; -.
DR eggNOG; KOG2189; Eukaryota.
DR HOGENOM; CLU_005230_0_0_1; -.
DR OrthoDB; 1967517at2759; -.
DR Proteomes; UP000016926; Unassembled WGS sequence.
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: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 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 436..459
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 480..499
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 562..581
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 593..615
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 654..673
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 790..814
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT REGION 696..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 104..138
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 859 AA; 96216 MW; AA7B674C96FAA3C8 CRC64;
MGDYEVTQYP SLLRSEHMTL VQLFCPIDVA HATVEALGEL ERIQFKDLNP DVNPFQRTYA
ERRLRFLTQQ IASQGIHIRP ASETLALLSG RSGPQALDDL DTRLSESESR VQAMNTSFEN
LEKRALELEE ARQVLRDTER FFLEAQGGRG APGDYRASFE QGEMEAPLLG DVEHAGPAGG
AGDAAAGGFE LEFVAGTIDR SRMATFERVL WRVLRGNLYM NSAEIADDVL PVPSTMQGTS
DSAGGEEKRL RKNAFVIFAH GQDLLDKIRK IAESMGATLF AIDSSSDKRS DKLREVTSRI
EDLHSVLYNT NQTRRAELLK IADSISAWWA LVRKEKVVFA TLNMWQWDQG RKTLVAEGWV
PTRDIPQVQA ALRRASENAG TSVSALLHEL RTTKTPPTFH RTNKFTEGFQ NIIDAYGIGS
YQEVNPGLFT VITFPFLFAV MFGDIGHGAL MMLSALVLIM LEKKFGKKGM GSEILDTFYF
GRYIIFLMGA FAIYTGIMYN DIFSLSLRLG PSQWHWPDEG SAGKAVEAIQ TSSRYWIGLD
PGWHGAENAL IFTNSLKMKM SIVLGVLHMS FAICLQVLNH LHFNRPELIW AEFLPQILFM
ESIFGYLVVC IVYKWSVDWE AAGRNPPNLL NMLIQMFLSP GNVNPDDQLY RGQAFVQVFL
LLLALVCVPW MLCTRPYLEY REMHKIKEQG YHGIQNGENG AHATDDETDT DGEGAHQGHA
VAMTEEAEEE GHDLGEVIIH QVIHTIEFCL GCISNTASYL RLWALSLAHA QLSEVLWNMT
IENAFGFEGV LAVVMLVFLF AMWFVLTIAI LCVMEGLSAF LHALRLHWVE FNSKFFIGAG
TAFDPLTFEG TDEIPEGVI
//