VATA_MANSE
ID VATA_MANSE Reviewed; 617 AA.
AC P31400;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=V-type proton ATPase catalytic subunit A;
DE Short=V-ATPase subunit A;
DE EC=7.1.2.2 {ECO:0000250|UniProtKB:P50516};
DE AltName: Full=V-ATPase 69 kDa subunit;
DE AltName: Full=Vacuolar proton pump subunit alpha;
GN Name=VHAA;
OS Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Sphingidae; Sphinginae; Sphingini; Manduca.
OX NCBI_TaxID=7130;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Midgut;
RX PubMed=1532941; DOI=10.1016/0014-5793(92)80177-i;
RA Graf R., Novak F.J., Harvey W.R., Wieczorek H.;
RT "Cloning and sequencing of cDNA encoding the putative insect plasma
RT membrane V-ATPase subunit A.";
RL FEBS Lett. 300:119-122(1992).
CC -!- FUNCTION: Catalytic subunit of the V1 complex of vacuolar(H+)-ATPase
CC (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1)
CC that hydrolyzes ATP and a membrane integral complex (V0) that
CC translocates protons (By similarity). V-ATPase is responsible for
CC acidifying and maintaining the pH of intracellular compartments and in
CC some cell types, is targeted to the plasma membrane, where it is
CC responsible for acidifying the extracellular environment (By
CC similarity). {ECO:0000250|UniProtKB:P38606,
CC ECO:0000250|UniProtKB:P50516}.
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 Evidence={ECO:0000250|UniProtKB:P50516};
CC -!- ACTIVITY REGULATION: ATP hydrolysis occurs at the interface between the
CC nucleotide-binding domains of subunits A and B (By similarity). ATP
CC hydrolysis triggers a conformational change in the subunits D and F,
CC which induces a shift of subunit d (By similarity). The c-ring is
CC subsequently rotated and results in a continuous proton translocation
CC across the membrane (By similarity). {ECO:0000250|UniProtKB:P31404}.
CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme made up of two
CC complexes: the ATP-hydrolytic V1 complex and the proton translocation
CC V0 complex (By similarity). The V1 complex consists of three catalytic
CC AB heterodimers that form a heterohexamer, three peripheral stalks each
CC consisting of EG heterodimers, one central rotor including subunits D
CC and F, and the regulatory subunits C and H (By similarity). The proton
CC translocation complex V0 consists of the proton transport subunit a, a
CC ring of proteolipid subunits c9c'', rotary subunit d, subunits e and f,
CC and the accessory subunits VhaAC45 and ATP6AP2 (By similarity).
CC {ECO:0000250|UniProtKB:P38606}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000305}.
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DR EMBL; X64233; CAA45537.1; -; mRNA.
DR PIR; S21107; S21107.
DR AlphaFoldDB; P31400; -.
DR SMR; P31400; -.
DR DIP; DIP-61386N; -.
DR IntAct; P31400; 1.
DR PRIDE; P31400; -.
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..617
FT /note="V-type proton ATPase catalytic subunit A"
FT /id="PRO_0000144568"
FT BINDING 250..257
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P38606"
SQ SEQUENCE 617 AA; 68166 MW; E373F806017C49D0 CRC64;
MASKGGLKTI ANEENEERFG YVFAVSGPVV TAEKMSGSAM YELVRVGYNE LVGEIIRLEG
DMATIQVYEE TSGVTVGDPV LRTGKPLSVE LGPGILGSIF DGIQRPLKDI NELTQSIYIP
KGVNVPSLAR EVDWEFNPLN VKVGSHITGG DLYGIVHENT LVKHKMLMPP RAKGTVTYIA
PAGNYKVTDV VLETEFDGEK AQYTMLQVWP VRQPRPVTEK LPANHPLLTG QRVLDSLFPC
VQGGTTAIPG AFGCGKTVIS QALSKYSNSD VIIYVGCGER GNEMSEVLRD FPELTVEIEG
VTESIMKRTA LVANTSNMPV AAREASIYTG ITLSEYFRDM GYNVSMMADS TSRWAEALRE
ISGRLAEMPA DSGYPAYLGA RLASFYERAG RVKCLGNPDR EGSVSIVGAV SPPGGDFSDP
VTAATLGIVQ VFWGLDKKLA QRKHFPSINW LISYSKYMRA LDDFYEKNYP EFVPLRTKVK
EILQEEEDLS EIVQLVGKAS LAETDKITLE VAKLLKDDFL QQNSYSSYDR FCPFYKTVGM
LKNIISFYDM SRHAVESTAQ SDNKVTWNVI RDAMGNVLYQ LSSMKFKDPV KDGEAKIKAD
FDQLLEDMSA AFRNLED
