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Database: UniProt
Entry: A0A2P7YTC4_9ASCO
LinkDB: A0A2P7YTC4_9ASCO
Original site: A0A2P7YTC4_9ASCO 
ID   A0A2P7YTC4_9ASCO        Unreviewed;       796 AA.
AC   A0A2P7YTC4;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   22-FEB-2023, entry version 15.
DE   RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN   ORFNames=C7M61_001827 {ECO:0000313|EMBL:PSK39224.1};
OS   [Candida] pseudohaemulonii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC   Candida/Metschnikowiaceae.
OX   NCBI_TaxID=418784 {ECO:0000313|EMBL:PSK39224.1, ECO:0000313|Proteomes:UP000241107};
RN   [1] {ECO:0000313|EMBL:PSK39224.1, ECO:0000313|Proteomes:UP000241107}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B12108 {ECO:0000313|EMBL:PSK39224.1,
RC   ECO:0000313|Proteomes:UP000241107};
RA   Munoz J.F., Gade L.G., Chow N.A., Litvintseva A.P., Loparev V.N.,
RA   Cuomo C.A.;
RT   "Candida pseudohaemulonii genome assembly and annotation.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PSK39224.1}.
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DR   EMBL; PYFQ01000003; PSK39224.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P7YTC4; -.
DR   STRING; 418784.A0A2P7YTC4; -.
DR   EnsemblFungi; C7M61_001827_t1; PSK39224.1; C7M61_001827.
DR   VEuPathDB; FungiDB:C7M61_001827; -.
DR   OrthoDB; 1967517at2759; -.
DR   Proteomes; UP000241107; Unassembled WGS sequence.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IEA:EnsemblFungi.
DR   GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IEA:EnsemblFungi.
DR   GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IEA:EnsemblFungi.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:EnsemblFungi.
DR   GO; GO:0071474; P:cellular hyperosmotic response; IEA:EnsemblFungi.
DR   GO; GO:0071469; P:cellular response to alkaline pH; IEA:EnsemblFungi.
DR   GO; GO:0006797; P:polyphosphate metabolic process; IEA:EnsemblFungi.
DR   GO; GO:0065003; P:protein-containing complex assembly; IEA:EnsemblFungi.
DR   GO; GO:0007035; P:vacuolar acidification; IEA:EnsemblFungi.
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:UP000241107};
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        383..407
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        428..449
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        508..528
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        534..561
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        599..621
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        700..719
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        731..754
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   COILED          85..112
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   796 AA;  90412 MW;  C171858F654449B7 CRC64;
     MALVEVYVPS EESRHILHEI GNLGLMQFKD LNSGVNEFQR AFVQELRTLD NIERQYSFLK
     SALDKKGISL NAHPYETNDV QVSDIDEYAQ NAALLESRVH QLSNSADGLQ EKKLELIQYR
     SAIKTVDNFF ATGDSREVLP PSVVDESLNS GSKFVTGTID REKIGILQQI LWRALRGNMY
     FYTEEIPQLV FDPKRGCDVP KNVFIIFSHG LLIHHRILKI AESLDAKVFD VNMGSDERLR
     QIAHLDGELR DLNVVLKETD NALCSELIAV SRDLPKWWEV IAKEKRVYQV MNLCNYDILR
     KTLIAEGWVP EDEIQSLTAK VRSLSSSESV PTIVSILETS KTPPTYHRTN KFTSAFQSIC
     DTYGIASYQE INPGLPTIIT FPFMFAIMFG DLGHGFLMFL AALILVLKEE HISALKRDEI
     FDMAFSGRYI LLMMGAFSMY TGLMYNDIFS KSLTLFSSGW QWPSEFNDGE LVTATQVGVY
     PFGLDWAWHG SENSLLFSNS YKMKLSVLMG YLHMTYSYFF SLLNAIYFGS MIDIIGNFVP
     GLLFMQSIFG YLSLCIVYKW SVDWVKSQEQ PPGLLNMLIT MFLSPGTVVE PLYSHQSVVQ
     LTLLLIALIC VPWLVFVKPF YLKHKMSLKE SSDTYEAIIN EETDFTNPAD ESRLTSLQGG
     ESLVTDELEE EEGFGDIMIH QVIHTIEFCL NCVSHTASYL RLWALSLAHA QLSTVLWTMT
     LENAFGPTGA LGVIMTVFLF GMWFCLTVVI LVIMEGTSAM LHSLRLHWVE SMSKFFVGEG
     YLYQPFEFGQ ILENRL
//
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