ID A0A103XGI9_CYNCS Unreviewed; 817 AA.
AC A0A103XGI9;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN ORFNames=Ccrd_007636 {ECO:0000313|EMBL:KVH90358.1};
OS Cynara cardunculus var. scolymus (Globe artichoke) (Cynara scolymus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Carduoideae; Cardueae;
OC Carduinae; Cynara.
OX NCBI_TaxID=59895 {ECO:0000313|EMBL:KVH90358.1, ECO:0000313|Proteomes:UP000243975};
RN [1] {ECO:0000313|EMBL:KVH90358.1, ECO:0000313|Proteomes:UP000243975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2C {ECO:0000313|EMBL:KVH90358.1};
RX PubMed=26786968; DOI=10.1038/srep19427;
RA Scaglione D., Reyes-Chin-Wo S., Acquadro A., Froenicke L., Portis E.,
RA Beitel C., Tirone M., Mauro R., Lo Monaco A., Mauromicale G., Faccioli P.,
RA Cattivelli L., Rieseberg L., Michelmore R., Lanteri S.;
RT "The genome sequence of the outbreeding globe artichoke constructed de novo
RT incorporating a phase-aware low-pass sequencing strategy of F1 progeny.";
RL Sci. Rep. 6:19427-19427(2016).
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:KVH90358.1}.
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DR EMBL; LEKV01005106; KVH90358.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A103XGI9; -.
DR STRING; 59895.A0A103XGI9; -.
DR EnsemblPlants; KVH90358; KVH90358; Ccrd_007636.
DR Gramene; KVH90358; KVH90358; Ccrd_007636.
DR OMA; TYVQLYI; -.
DR OrthoDB; 1967517at2759; -.
DR Proteomes; UP000243975; 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:SF72; V-TYPE PROTON ATPASE SUBUNIT A1; 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:UP000243975};
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 421..444
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 465..483
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 546..568
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 589..616
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 636..653
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 754..775
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT COILED 99..126
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 817 AA; 93066 MW; 5AD0246D4E938364 CRC64;
MELLKNLPEM DLMRSEKMTF VQLIIPVESA HRAISYLGEL GLLQFRDLND DKSPFQRTFV
NQVKRCAEMS RKLRFFKDQI HKAGLLSSAL PTLQPDVDLE ALEIQLAEHE HELIEMNANS
EKLQQTYNEL LEFKMVLQKA GGFLISGKSY ETAEGRELDE NVYPSDYPES ASLLEQATQP
GPSNLAGLRF ISGIIPKSKV LLFERMLFRA TRGNLLFNQA PADDLIMDPV SSEMVEKTVF
VVFFSGEQAK TKILKICEAF GANCYPVPED MTKQSQITQE VLSRLSELET TLDVGIRQRN
AALHSIGFHL TIWMNMVKRE KAVFDTLNML NFDVTKKCLV GEGWCPIFAK PQIQEALQRA
TFDSNSQVGI IFHVMDAVES PPTYFRTNKF TNAYQEIVDA YGVAKYQEAN PAVYTVITFP
FLFAVMFGDW GHGICLLLGA MVLIAREGKL GSQKLGSFME MLFGGRYVLL LMSLFSIYCG
LIYNEFFSVP YHIFGSSAYR CRDAACSEAH TVGLIKYRDA YPFGVDPSWR GSRSELPFLN
SLKMKMSILF GIAQMNLGII LSYFNSIFFS SSIDIRYQFV PQMIFLNSLF GYLSLLIIIK
WCTGSQADLY HVMIYMFLSP FDDLGENELF WGQRPLQIIL LLSALVAVPW MLFPKPFILR
KLHSERFQGR AYGILRSSEM DTDSEPGSAR HHEEEFNFSE VFVHQMIHSI EFVLGSVSNT
ASYLRLWALS LAHSELSTVF YEKVLLLAWG YENIIIRMVG LAVFAFATAF ILLMMETLSA
FLHALRLHWV EFQNKFYHGD GYKFKPFSFA AIADDED
//