VATA_MESAU
ID VATA_MESAU Reviewed; 174 AA.
AC P86205;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=V-type proton ATPase catalytic subunit A {ECO:0000250|UniProtKB:P50516};
DE Short=V-ATPase subunit A {ECO:0000250|UniProtKB:P50516};
DE EC=7.1.2.2 {ECO:0000250|UniProtKB:P50516};
DE AltName: Full=V-ATPase 69 kDa subunit {ECO:0000250|UniProtKB:P50516};
DE AltName: Full=Vacuolar proton pump subunit alpha {ECO:0000250|UniProtKB:P50516};
DE Flags: Fragments;
GN Name=ATP6V1A {ECO:0000250|UniProtKB:P50516};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20400973; DOI=10.1038/aja.2010.19;
RA Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.;
RT "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen
RT (GP96) are unique to hamster caput epididymal spermatozoa.";
RL Asian J. Androl. 12:344-355(2010).
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). In aerobic conditions, involved in intracellular iron
CC homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase
CC (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent
CC proteasomal degradation (By similarity). May play a role in neurite
CC development and synaptic connectivity (By similarity).
CC {ECO:0000250|UniProtKB:P38606}.
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, ECO:0000255|PROSITE-
CC ProRule:PRU10106};
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 ATP6AP1/Ac45 and ATP6AP2/PRR (By
CC similarity). Interacts with the V0 complex V-ATPase subunit a4 ATP6V0A4
CC (By similarity). Interacts with WFS1 (By similarity). Interacts with
CC alpha-crystallin B chain/CRYAB and with MTOR, forming a ternary complex
CC (By similarity). {ECO:0000250|UniProtKB:P38606,
CC ECO:0000250|UniProtKB:P50516}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P38606}.
CC Cytoplasm, cytosol {ECO:0000250|UniProtKB:P50516}. Cytoplasmic vesicle,
CC secretory vesicle {ECO:0000250|UniProtKB:P38606}. Cytoplasmic vesicle,
CC clathrin-coated vesicle membrane {ECO:0000250|UniProtKB:P31404};
CC Peripheral membrane protein {ECO:0000305}. Lysosome
CC {ECO:0000250|UniProtKB:P50516}. Note=Co-localizes with WFS1 in the
CC secretory granules in neuroblastoma cell lines.
CC {ECO:0000250|UniProtKB:P38606}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000255}.
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DR AlphaFoldDB; P86205; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0030133; C:transport vesicle; 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; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022878; V-ATPase_asu.
DR PANTHER; PTHR43607; PTHR43607; 2.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Cytoplasmic vesicle; Hydrogen ion transport;
KW Ion transport; Lysosome; Membrane; Nucleotide-binding; Reference proteome;
KW Translocase; Transport.
FT CHAIN <1..>174
FT /note="V-type proton ATPase catalytic subunit A"
FT /id="PRO_0000394297"
FT NON_CONS 12..13
FT /evidence="ECO:0000305"
FT NON_CONS 21..22
FT /evidence="ECO:0000305"
FT NON_CONS 29..30
FT /evidence="ECO:0000305"
FT NON_CONS 39..40
FT /evidence="ECO:0000305"
FT NON_CONS 51..52
FT /evidence="ECO:0000305"
FT NON_CONS 82..83
FT /evidence="ECO:0000305"
FT NON_CONS 110..111
FT /evidence="ECO:0000305"
FT NON_CONS 124..125
FT /evidence="ECO:0000305"
FT NON_CONS 141..142
FT /evidence="ECO:0000305"
FT NON_CONS 157..158
FT /evidence="ECO:0000305"
FT NON_TER 1
FT NON_TER 174
SQ SEQUENCE 174 AA; 19754 MW; 8FA463D76218B487 CRC64;
VGHSELVGEI IRGVNVSALS RHKIMLPPRF SMVQVWPVRL PANHPLLTGQ RRTALVANTS
NMPVAAREAS IYTGITLSEY FRWAEALREI SGRLAEMPAD SGYPAYLGAR KHFPSVNWLI
SYSKALDEYY DKHFTEFVPL RTVGMLSNMI SFYDMARIKA DYAQLLEDMQ NAFR
