VATA_ENCCU
ID VATA_ENCCU Reviewed; 607 AA.
AC Q8SQU9;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 126.
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:P17255};
DE AltName: Full=Vacuolar proton pump subunit alpha;
GN Name=VMA1; OrderedLocusNames=ECU11_1280i;
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP DEVELOPMENTAL STAGE.
RX PubMed=16691553; DOI=10.1002/pmic.200500796;
RA Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
RT "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi
RT (microsporidia): a reference map for proteins expressed in late sporogonial
RT stages.";
RL Proteomics 6:3625-3635(2006).
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 (By
CC similarity). {ECO:0000250|UniProtKB:P17255}.
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:P17255};
CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral
CC catalytic V1 complex (components A to H) attached to an integral
CC membrane V0 proton pore complex (components: a, c, c', c'', d, e, f and
CC VOA1). {ECO:0000250|UniProtKB:P17255}.
CC -!- SUBCELLULAR LOCATION: Endomembrane system
CC {ECO:0000250|UniProtKB:P17255}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Vacuole membrane
CC {ECO:0000250|UniProtKB:P17255}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Membranes of
CC various intracellular acidic compartments.
CC {ECO:0000250|UniProtKB:P17255}.
CC -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
CC {ECO:0000269|PubMed:16691553}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000305}.
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DR EMBL; AL590450; CAD26038.1; -; Genomic_DNA.
DR RefSeq; NP_586434.1; NM_001042267.1.
DR AlphaFoldDB; Q8SQU9; -.
DR SMR; Q8SQU9; -.
DR STRING; 284813.Q8SQU9; -.
DR PRIDE; Q8SQU9; -.
DR GeneID; 860088; -.
DR KEGG; ecu:ECU11_1280i; -.
DR VEuPathDB; MicrosporidiaDB:ECU11_1280i; -.
DR HOGENOM; CLU_008162_3_1_1; -.
DR InParanoid; Q8SQU9; -.
DR OMA; RIVKTFW; -.
DR OrthoDB; 241249at2759; -.
DR Proteomes; UP000000819; Chromosome XI.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; ISS:UniProtKB.
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 1: Evidence at protein level;
KW ATP-binding; Hydrogen ion transport; Ion transport; Membrane;
KW Nucleotide-binding; Reference proteome; Translocase; Transport; Vacuole.
FT CHAIN 1..607
FT /note="V-type proton ATPase catalytic subunit A"
FT /id="PRO_0000382909"
FT BINDING 251..258
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00499"
SQ SEQUENCE 607 AA; 67306 MW; 5310E6E1C23B0BFA CRC64;
MNVVQQTFAE LSIGEPEKRV EGRVYSVSGP VVVGCNMIGC AMYELVKVGS EGLAGEIIKI
DKDQATIQVY EDTSGLCVGD TIVRTGLPLC AELGPGLFES IYDGIQRPLR EIRESSGGIF
IPKGVNIPAL DREREYEFVP AVSAGDYVVG GDVFGKVYEN SLIETKILVP PKKSGKVAFI
ACRGNYTLKD VVMELETGKG KEEMFMYHTW PVRIPRPIEE KKNATHPLFT GQRILDSLFP
CVQGGTTAIP GAFGCGKTVI SQSLSKYSNS DAIVYVGCGE RGNEMSEVLM EFPKLTVGGK
DDSIMKRTVL VANTSNMPVA AREASIYTGI TISEYLRDQG MNVSMMADST SRWAEALREI
SGRLAEMPAD SGYPAYLGAK LAFFYERAGS VVCLGSPRRT GSVTIVGAVS PPGGDFSDPV
TSATLGIVQV FWGLDKKLAQ RKHFPSINWN LSYSKYFSNL EPYYEEVDPG FIVNRTKCRE
ILQLDDDLSE IVQLVGKNAL SETEKLILDI SKLIKEDFLQ QNGYSRYDNY CPFTKTRLML
RNIILYFDNS KNAITNYKLS WSTIRKETED VFYGLMKMKF VMADKEMEPK LNKLKREIEG
VFLKMLG
