ID   VATA1_ACEAT             Reviewed;         613 AA.
AC   Q38676;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=V-type proton ATPase catalytic subunit A isoform 1;
DE            Short=V-ATPase subunit A 1;
DE            EC=7.1.2.2;
DE   AltName: Full=V-ATPase 69 kDa subunit 1;
DE   AltName: Full=Vacuolar proton pump subunit alpha 1;
OS   Acetabularia acetabulum (Mermaid's wine glass) (Acetabularia mediterranea).
OC   Eukaryota; Viridiplantae; Chlorophyta; Ulvophyceae; TCBD clade;
OC   Dasycladales; Polyphysaceae; Acetabularia.
OX   NCBI_TaxID=35845;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Konishi K., Moritani C., Rahman H., Kadowaki H., Ohmori S., de Groot E.J.,
RA   Oesterhelt D., Ikeda M.;
RT   "Molecular cloning of cDNAs encoding Acetabularia acetabulum V type ATPase,
RT   A subunit.";
RL   (er) Plant Gene Register PGR95-042(1995).
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; D50528; BAA09097.1; -; mRNA.
DR   AlphaFoldDB; Q38676; -.
DR   SMR; Q38676; -.
DR   PRIDE; Q38676; -.
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..613
FT                   /note="V-type proton ATPase catalytic subunit A isoform 1"
FT                   /id="PRO_0000144572"
FT   BINDING         240..247
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   613 AA;  67366 MW;  5E5166A33056BC27 CRC64;
     MSKAKEGDYG SIKKVSGPVV VADNMGGSAM YELVRVGTGE LIGEIIRLEG DTATIQVYEE
     TSGLTVGDGV LRTKQPLSVD LGPGILGNIF DGIQRPLKAI ADVSGDVFIP RGVNVPSLDQ
     TKQWEFRPSA FKVGDRVTGG DIIGIVPENS LLDHKVMLLP QAKGTVTYIA APGNYTINEK
     IIEVEFQGAK YEYSMKQSWP VRSPRPVVEK LLADTPLLTG QRVLDSLFPG VRGGTCAIPG
     AFGCGKTVIS QALSKYSNSD GIVYVGCGER GNEMAEVLMD FPQLTMTMPD GREESIMKRT
     TLVANTSNMP VAAREASIYT GITLSEYFRD MGYNFAMMAD STSRWAEALR EISGRLAEMP
     ADSGYPAYLG ARLASFYERS GRVACIGSPE REGSVTIVGA VSPPGGDFSD PVTSATLGIV
     QVFWGLDKKL AQRKHFPSVN WLISYSKYLN ALEPFYEKFD SDFVTLRQVA REVLQKEDEL
     NEIVQLVGKD ALAESDKIIL ETARFLKEDY LQQNSFTKYD KYCPFYKSVG MMRNIVTFHR
     LATQAIERTA AGNVDGQKIT FNIIKAKLGD LLYKVSSQKF EDPSDGEGVV TAHLNELNEE
     LKEKFRALED EYR