VPP1_XENTR
ID VPP1_XENTR Reviewed; 837 AA.
AC A1A5G6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
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 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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 -!- 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; BC128641; AAI28642.1; -; mRNA.
DR RefSeq; NP_001090714.1; NM_001097245.1.
DR AlphaFoldDB; A1A5G6; -.
DR SMR; A1A5G6; -.
DR PaxDb; A1A5G6; -.
DR PRIDE; A1A5G6; -.
DR GeneID; 100036694; -.
DR KEGG; xtr:100036694; -.
DR CTD; 535; -.
DR Xenbase; XB-GENE-959346; atp6v0a1.
DR eggNOG; KOG2189; Eukaryota.
DR HOGENOM; CLU_005230_0_0_1; -.
DR InParanoid; A1A5G6; -.
DR OMA; FSYDRAR; -.
DR OrthoDB; 181796at2759; -.
DR TreeFam; TF300346; -.
DR Reactome; R-XTR-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-XTR-6798695; Neutrophil degranulation.
DR Reactome; R-XTR-77387; Insulin receptor recycling.
DR Reactome; R-XTR-917977; Transferrin endocytosis and recycling.
DR Reactome; R-XTR-983712; Ion channel transport.
DR Proteomes; UP000008143; Chromosome 10.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000007635; Expressed in brain and 12 other tissues.
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 2: Evidence at transcript level;
KW Cytoplasmic vesicle; Hydrogen ion transport; Ion transport; Membrane;
KW Reference proteome; Synapse; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..837
FT /note="V-type proton ATPase 116 kDa subunit a 1"
FT /id="PRO_0000317419"
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..534
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 535..554
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 555..572
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 573..593
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 594..638
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 639..658
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 659..724
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 725..749
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 750..770
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 771..809
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 810..837
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 837 AA; 96016 MW; 310874E8724C5A65 CRC64;
MGELFRSEEM TLAQLFLQSE AAYCCVSELG ELGKVQFRDL NPDVNVFQRK FVNEVRRCEE
MDRKLRFVEK EVKKANISIL DTGENPEVPF PRDMIDLEAN FEKIEIELKE INTNQEALKR
NFLELTELKF ILRKTQQFFD EMADPDLLEE SSSLLEPSEM GRGAPLRLGF VAGVINRERI
PTFERMLWRV CRGNVFLRQA EIENPLEDPV TGDSVHKSVF IIFFQGDQLK NRVKKICEGF
RASLYPCPET PQERKEMATG VNTRIEDLQM VLNQTEDHRQ RVLQAAAKSL RVWFIKVRKM
KAIYHTLNLC NIDVTQKCLI AEVWCPVADL DSIQFALRRG TEHSGSTVPS ILNRMQTNQT
PPTYNKTNKF TYGFQNLVDA YGIGSYREIN PAPYTIITFP FLFAVMFGDF GHGILMTLFA
VWMVVRESRI LSQKIDNELF TMMFSGRYII LLMGLFSIYT GLIYNDCFSK ALNLFGSSWS
VRPMFTDTWS EDLLKHTSVL QLNPNVTGVF NGPYPFGIDP IWSLATNKLT FLNSFKMKMS
VVLGIIHMTF GVALSLLNHI YFKKPLNIYL GFIPEMIFMT TLFGYLVILI IYKWCAYDAS
TSMVAPSLLI HFINMFLFSY QDTSLPMLYK GQMGLQCFLV VCAIICVPWM LVVKPLILRR
QYLRRKHLGT HNFGGIRVGN GPTEEDAEII QHDQLSMHSE EGEEPAMEEV FDFGDTVVHQ
AIHTIEYCLG CISNTASYLR LWALSLAHAQ LSEVLWTMVM HVGLSIRSLG GGIALVFVFS
AFATLTIAIL LIMEGLSAFL HALRLHWVEF QNKFYMGTGF KFLPFSFENI REGKFDE
