VPP1_CHICK
ID VPP1_CHICK Reviewed; 838 AA.
AC Q9I8D0;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=V-type proton ATPase 116 kDa subunit a 1;
DE Short=V-ATPase 116 kDa subunit a 1;
DE AltName: Full=Vacuolar proton translocating ATPase 116 kDa subunit a isoform 1;
GN Name=ATP6V0A1;
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], IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10866814; DOI=10.1046/j.1432-1327.2000.01445.x;
RA Mattsson J.P., Li X., Peng S.-B., Nilsson F., Andersen P., Lundberg L.G.,
RA Stone D.K., Keeling D.J.;
RT "Properties of three isoforms of the 116-kDa subunit of vacuolar H+-ATPase
RT from a single vertebrate species. Cloning, gene expression and protein
RT characterization of functionally distinct isoforms in Gallus gallus.";
RL Eur. J. Biochem. 267:4115-4126(2000).
CC -!- FUNCTION: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase),
CC a multisubunit enzyme composed of a peripheral complex (V1) that
CC hydrolyzes ATP and a membrane integral complex (V0) that translocates
CC protons (By similarity). V-ATPase is responsible for acidifying and
CC maintaining the pH of intracellular compartments and in some cell
CC types, is targeted to the plasma membrane, where it is responsible for
CC acidifying the extracellular environment (By similarity). Required for
CC assembly and activity of the vacuolar ATPase (By similarity).
CC {ECO:0000250|UniProtKB:G5EGP4, ECO:0000250|UniProtKB:P32563,
CC ECO:0000250|UniProtKB:Q29466}.
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:Q29466}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
CC membrane {ECO:0000250|UniProtKB:P25286}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle
CC membrane {ECO:0000250|UniProtKB:P25286}; Multi-pass membrane protein
CC {ECO:0000255}. Melanosome {ECO:0000250|UniProtKB:Q93050}.
CC -!- TISSUE SPECIFICITY: Detected in brain (at protein level). Highest
CC expression in brain, intermediate levels in kidney, and relatively low
CC levels in bone and liver. {ECO:0000269|PubMed:10866814}.
CC -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ289019; CAB93527.1; -; mRNA.
DR RefSeq; NP_990055.1; NM_204724.2.
DR AlphaFoldDB; Q9I8D0; -.
DR SMR; Q9I8D0; -.
DR STRING; 9031.ENSGALP00000005145; -.
DR BindingDB; Q9I8D0; -.
DR ChEMBL; CHEMBL2683; -.
DR PaxDb; Q9I8D0; -.
DR GeneID; 395474; -.
DR KEGG; gga:395474; -.
DR CTD; 535; -.
DR VEuPathDB; HostDB:geneid_395474; -.
DR eggNOG; KOG2189; Eukaryota.
DR InParanoid; Q9I8D0; -.
DR OrthoDB; 181796at2759; -.
DR PhylomeDB; Q9I8D0; -.
DR PRO; PR:Q9I8D0; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IBA:GO_Central.
DR GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR GO; GO:0051117; F:ATPase binding; IBA:GO_Central.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0007035; P:vacuolar acidification; IBA:GO_Central.
DR InterPro; IPR002490; V-ATPase_116kDa_su.
DR InterPro; IPR026028; V-type_ATPase_116kDa_su_euka.
DR PANTHER; PTHR11629; PTHR11629; 1.
DR Pfam; PF01496; V_ATPase_I; 1.
DR PIRSF; PIRSF001293; ATP6V0A1; 1.
PE 1: Evidence at protein level;
KW Cytoplasmic vesicle; Hydrogen ion transport; Ion transport; Membrane;
KW Reference proteome; Synapse; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..838
FT /note="V-type proton ATPase 116 kDa subunit a 1"
FT /id="PRO_0000318901"
FT TOPO_DOM 1..388
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..407
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 408..409
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 410..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 427..441
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 442..471
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 472..535
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 536..555
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 556..573
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 574..594
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 595..639
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 640..659
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 660..725
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 726..750
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 751..771
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 772..810
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 811..838
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 838 AA; 95984 MW; F629DAA90759C66F CRC64;
MGELFRSEEM TLAQLFLQSE AAYCCVSELG ELGKVQFRDL NPDVNVFQRK FVNEVRRCEE
MDRKLRFVEK EIKKANIPIM DTGENPEVPF PRDMIDLEAN FEKIENELKE INTNQEALKR
NFLELTELKF ILRKTQQFFD EMADPDLLEE SSSLLEPSEM GRGAPLRLGF VAGVINRERI
PTFERMLWRV CRGNVFLRQA EIENPLEDPV TGDYVHKSVF IIFFQGDQLK NRVKKICEGF
RASLYPCPET PQERKEMASG VNTRIDDLQM VLNQTEDHRQ RVLQAAAKNI RVWFIKVRKM
KAIYHTLNLC NIDVTQKCLS AEVWCPVADL DSIQFALRRG TEHSGSTVPS ILNRMQTNQT
PPTYNKTNKF TCGFQNIVDA YGIGTYREIN PAPYTIITFP FLFAVMFGDF GHGILMTLIA
IWMVLRESRI LSQKSDNEMF STVFSGRYII LLMGLFSTYT GLIYNDCFSK SLNMFGSSWS
VRPMFSKANW SDELLKTTPL LQLDPAEAGV FGGPYPFGID PIWNIANNKL AFLNSFKMKM
SVILGIIHML FGVMLSLLNH IYFKKPLNIY LGFIPEMIFM SSLFGYLVIL IFYKWTAYDA
HTSKEAPSPL IHFINMFLFS YGDTSNKMLY RGQKGIQCFL VVVALLCVPW MLVAKPLVLR
HQYLRRKHLG THNFGGIRVG NGPTEEDAEI IQHDQLSTHS EEGEEPTEDE VFDFADTVVY
QAIHTIEYCL GCISNTASYL RLWALSLAHA QLSEVLWTMV IHTGLSVRSL AGGFGLVFIF
AAFATLTVAI LLVMEGLSAF LHALRLHWIE FQNKFYTGTG FKFLPFSFDP IREGKFDD
