ID S7ZS22_PENO1 Unreviewed; 854 AA.
AC S7ZS22;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 22-FEB-2023, entry version 21.
DE RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN ORFNames=PDE_08482 {ECO:0000313|EMBL:EPS33520.1};
OS Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS33520.1, ECO:0000313|Proteomes:UP000019376};
RN [1] {ECO:0000313|EMBL:EPS33520.1, ECO:0000313|Proteomes:UP000019376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT "Genomic and secretomic analyses reveal unique features of the
RT lignocellulolytic enzyme system of Penicillium decumbens.";
RL PLoS ONE 8:E55185-E55185(2013).
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; KB644415; EPS33520.1; -; Genomic_DNA.
DR AlphaFoldDB; S7ZS22; -.
DR STRING; 933388.S7ZS22; -.
DR eggNOG; KOG2189; Eukaryota.
DR HOGENOM; CLU_005230_0_2_1; -.
DR OrthoDB; 1967517at2759; -.
DR PhylomeDB; S7ZS22; -.
DR Proteomes; UP000019376; 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 Reference proteome {ECO:0000313|Proteomes:UP000019376};
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..449
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 469..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 588..607
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 644..666
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 789..810
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT COILED 93..127
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 854 AA; 97055 MW; 17814F75E97EEDEB CRC64;
MASKDTFFRS SEMSLTQLYI ANEIGREVVS ALGELGQVQF RDLNPDTNAF QRTFTKEIRR
LDNVERQLRY FHAQMEKAAI PMRPSTDFSD TLAAPLASEI DELSERSESL EQRIVSLNDS
YETLKKREVE LTEWRWVLRE AGGFFDRAHT HTEDIRQSFD NDEAPLLRDV EQHAPRGTNG
DAQGQQSFSD MNIGFVAGVI PRDRIGAFER ILWRTLRGNL YMNQSEIPEV IIDPTNNEEI
HKNVFVIFAH GKGILAKIRK ISESLGASLY GVDENSELRR DQIHEVNTRL GDVSNVLRNT
KSTLDAELSQ IARSLAAWMI IVKKEKAVYD TLNKFSYDQA RKTLIAEAWC PTNSLGLIKT
TLQDVNDRAG LSVPTIVNQI RTNKTPPTYV RTNKFTEAFQ TIINSYGVPK YSEVNPGLYT
IVTFPFLFAV MFGDMGHGFI MALAASAMIL FEKKLLRTKL DELTYMAFYG RYIMLMMGLF
SIYTGFIYND IFSRALTIFP SQWEWPGDIK AGDSVEATLT DGYRFPIGLD WNWHEAENSL
LFSNSMKMKM SILLGWSHMT YALIHQYINA RHFKSKVDVL GNFVPGMLFF QCIFGYLAMT
ILYKWSVDWP AIGQDPPSLL NMLIFMFLSP GTLQGQLYSG QATVQVLLLL IAVIQVPIML
FLKPFWLRYE HNRARALGYR GLGEQSRVSA LDEDGDTNGG PRDSMASDGE GVAMIAQNID
DEEHEEFDFS DEMIHQVIHT IEFCLNCISH TASYLRLWAL SLAHQQLSIV LWNMTIGSAI
AMESHVTRVI LTVVCVYMFL VLSVAVLVTM EGVSAMLHSL RLHWVEAMSK HFMGEGIPFV
PFSFKTLLEE DPVD
//
