VATA_CHICK
ID VATA_CHICK Reviewed; 617 AA.
AC Q90647; Q90646;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 130.
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=ATP6V1A;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RX PubMed=7597085; DOI=10.1073/pnas.92.13.6087;
RA Hernando N., Bartkiewicz M., Collin-Osdoby P., Osdoby P., Baron R.;
RT "Alternative splicing generates a second isoform of the catalytic A subunit
RT of the vacuolar H(+)-ATPase.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:6087-6091(1995).
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};
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 two accessory subunits (By similarity).
CC {ECO:0000250|UniProtKB:P38606}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P38606}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=A1;
CC IsoId=Q90647-1; Sequence=Displayed;
CC Name=2; Synonyms=A2;
CC IsoId=Q90647-2; Sequence=VSP_024494;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed (both isoforms).
CC {ECO:0000269|PubMed:7597085}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000305}.
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DR EMBL; U22076; AAC59679.1; -; mRNA.
DR EMBL; U22077; AAC59680.1; -; mRNA.
DR PIR; I50715; I50715.
DR PIR; I50716; I50716.
DR RefSeq; NP_990305.1; NM_204974.1. [Q90647-2]
DR AlphaFoldDB; Q90647; -.
DR SMR; Q90647; -.
DR STRING; 9031.ENSGALP00000023849; -.
DR PaxDb; Q90647; -.
DR PRIDE; Q90647; -.
DR GeneID; 395821; -.
DR KEGG; gga:395821; -.
DR CTD; 523; -.
DR VEuPathDB; HostDB:geneid_395821; -.
DR eggNOG; KOG1352; Eukaryota.
DR InParanoid; Q90647; -.
DR PhylomeDB; Q90647; -.
DR PRO; PR:Q90647; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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 GO; GO:0006879; P:cellular iron ion homeostasis; ISS:UniProtKB.
DR GO; GO:0036295; P:cellular response to increased oxygen levels; ISS:UniProtKB.
DR GO; GO:1902600; P:proton transmembrane transport; IBA:GO_Central.
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 Alternative splicing; ATP-binding; Cytoplasm; Hydrogen ion transport;
KW Ion transport; Nucleotide-binding; Reference proteome; Translocase;
KW Transport.
FT CHAIN 1..617
FT /note="V-type proton ATPase catalytic subunit A"
FT /id="PRO_0000284400"
FT BINDING 250..257
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT VAR_SEQ 240..268
FT /note="CVQGGTTAIPGAFGCGKTVISQSLSKYSN -> KHILRWKRAVFEFLANQSP
FT FSLL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7597085"
FT /id="VSP_024494"
SQ SEQUENCE 617 AA; 68476 MW; AC4E578035B0D668 CRC64;
MDFSKLPKIR DEDREAFVGY VQGVSGPVVT ACNMAGAAMY ELVRVGHSEL VGEIIRLEGD
LATVQVYEET SGVSVGDPVL RTGKPLSVEL GPGIMGAIFD GIQRPLSDIS TLTKSIYIPR
GVNVSALSRD VKWDFTPSKN LRVGSHITGG DIYGVVNENS LIKHKIMLPP RNRGTVTYIA
PPGNYDTSDV VLELEFEGVK EKFTMVQVWP VRQVRPVTEK LPANHPLLTG QRVLDALFPC
VQGGTTAIPG AFGCGKTVIS QSLSKYSNSD VIIYVGCGER GNEMSEVLRD FPELTMEVDG
KVESIMKRTA LVANTSNMPV AAREASIYTG ITLSEYFRDM GYHVSMMADS TSRWAEALRE
ISGRLAEMPA DSGYPAYLGA RLASFYERAG RVKCLGNPER EGSVTIVGAV SPPGGDFSDP
VTSATLGIVQ VFWGLDKKLA QRKHFPSVNW LISYSKYTRA LDEYYDKHFT EFVPLRTKAK
EILQEEEDLA EIVQLVGKAS LAETDKITLE VAKLIKDDFL QQNGYTPYDR FCPFYKTVGM
LSNMIAFYDM RRRAVENTAQ SDNKITWSII RENMSEILYR LTSMKFKDPV KDGETKIKAD
YAQLFEDMQN AFRSLED
