VATA_CITUN
ID VATA_CITUN Reviewed; 623 AA.
AC Q9SM09;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=V-type proton ATPase catalytic subunit A;
DE Short=V-ATPase subunit A;
DE EC=7.1.2.2;
DE AltName: Full=V-ATPase 69 kDa subunit;
DE AltName: Full=Vacuolar proton pump subunit alpha;
OS Citrus unshiu (Satsuma mandarin) (Citrus nobilis var. unshiu).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=55188;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Miyagawa-Wase; TISSUE=Juice tissue;
RX PubMed=9804972; DOI=10.1016/s0005-2736(98)00148-5;
RA Takanokura Y., Komatsu A., Omura M., Akihama T.;
RT "Cloning and expression analysis of vacuolar H+-ATPase 69-kDa catalytic
RT subunit cDNA in citrus (Citrus unshiu Marc.).";
RL Biochim. Biophys. Acta 1414:265-272(1998).
CC -!- FUNCTION: Catalytic subunit of the peripheral V1 complex of vacuolar
CC ATPase. V-ATPase vacuolar ATPase is responsible for acidifying a
CC variety of intracellular compartments in eukaryotic cells.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate;
CC Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2;
CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral
CC catalytic V1 complex (main components: subunits A, B, C, D, E, and F)
CC attached to an integral membrane V0 proton pore complex (main
CC component: the proteolipid protein).
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000305}.
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DR EMBL; AB004247; BAA87891.1; -; mRNA.
DR AlphaFoldDB; Q9SM09; -.
DR SMR; Q9SM09; -.
DR PRIDE; Q9SM09; -.
DR GO; GO:0033180; C:proton-transporting V-type ATPase, V1 domain; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-EC.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR Gene3D; 1.10.1140.10; -; 1.
DR Gene3D; 2.40.30.20; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00309; ATP_synth_A_arch; 1.
DR InterPro; IPR031686; ATP-synth_a_Xtn.
DR InterPro; IPR023366; ATP_synth_asu-like_sf.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR024034; ATPase_F1/V1_b/a_C.
DR InterPro; IPR005725; ATPase_V1-cplx_asu.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022878; V-ATPase_asu.
DR PANTHER; PTHR43607; PTHR43607; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR Pfam; PF16886; ATP-synt_ab_Xtn; 1.
DR SUPFAM; SSF50615; SSF50615; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01042; V-ATPase_V1_A; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Hydrogen ion transport; Ion transport; Nucleotide-binding;
KW Translocase; Transport.
FT CHAIN 1..623
FT /note="V-type proton ATPase catalytic subunit A"
FT /id="PRO_0000144577"
FT BINDING 252..259
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 623 AA; 68681 MW; AF7BA1F9D29CD7E1 CRC64;
MPSVYGARLT TFEDEEKESE YGYVRKVSGP VVIADGMNGA AMYELVRVGH DNLIGEIIRL
EGDSATIQVY EETAGLMVND PVLRTHKPLS VELGPGILGN IFDGIQRPLK TIAIRSGDVY
IPRGVSVPAL DKDTLWEFQP KKIGEGDLLT GGDLYATVFE NSLMQHHVAL PPDAMGKVTY
VAPAGQYSLK DTVLELEFQG VKKSFTMLQA WPVRTPRPVS SKLAADTPLL TGQRVLDALF
PSVLGGTCAI PGAFGCGKTV ISQALSKYSN SDTVVYVGCG ERGNEMAEVL MDFPQLTMTL
PDGREESVMK RTTLVANTSN MPVAAREASI YTGITIAEYF RDMGYNVSMM ADSTSRWAEA
LREISGRLAE MPADSGYPAY LAARLASFYE RAGKVKCLGG PERTGSVTIV GAVSPPGGDF
SDPVTSATLS IVQVFWGLDK KLAQRKHFPS VNWLISYSKY STALESFYEQ FDPDFINIRT
KAREVLQRED DLNEIVQLVG KDALAEGDKI TLETAKLLRE DYLAQNAFTP YDKFCPFYKS
VWMMRNIIHF YNLANQAVEK GAGMDGQKIT YTLIKHRLGD LFYRLVSQKF EDPAEGEPAL
VAKFKKLHED LTAGFRALED ETR