ID   VPP1_XENLA              Reviewed;         831 AA.
AC   Q8AVM5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=V-type proton ATPase 116 kDa subunit a1;
DE            Short=V-ATPase 116 kDa subunit a1;
DE   AltName: Full=Vacuolar proton translocating ATPase 116 kDa subunit a isoform 1;
GN   Name=atp6v0a1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2002) 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}.
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DR   EMBL; BC041732; AAH41732.1; -; mRNA.
DR   RefSeq; NP_001080294.1; NM_001086825.1.
DR   AlphaFoldDB; Q8AVM5; -.
DR   SMR; Q8AVM5; -.
DR   PRIDE; Q8AVM5; -.
DR   DNASU; 379986; -.
DR   GeneID; 379986; -.
DR   CTD; 379986; -.
DR   Xenbase; XB-GENE-959351; atp6v0a1.L.
DR   OrthoDB; 181796at2759; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   Bgee; 379986; Expressed in brain and 19 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:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
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..831
FT                   /note="V-type proton ATPase 116 kDa subunit a1"
FT                   /id="PRO_0000317418"
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..718
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        719..743
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        744..764
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        765..803
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        804..831
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   831 AA;  95556 MW;  4438B22808D506CA CRC64;
     MGELFRSEEM TLAQLFLQSE AAYCCVSELG ELGKVQFRDL NPDVNVFQRK FVNEVRRCEE
     MDRKLRFVEK EVKKANISIL DTGENPEVPF PRDIIDLEAN FEKIEIELKE INTNQEALKR
     NFLELTELKF ILRKTQQFFD EMADPDLLEE SSTLLEPSEM GRGAPLRLGF VAGVINRERI
     PTFERMLWRV CRGNVFLRQA QIENPLEDPV TGDSVHKSVF IIFFQGDQLK NRVKKICEGF
     RASLYPCPET PQERKEMATG VNTRIEDLQM VLNQTEDHRQ RVLQAAAKSL RVWFIKVRKM
     KAIYHTLNLC NIDVTQKCLI AEVWCPVADL DSIQFALRRG TEHSGSTVPS ILNRMQTNQT
     PPTYNKTNKF TYGFQNLVDA YGIGSYREIN PAPYTIITFP FLFAVMFGDF GHGILMTLFA
     VWMVVRESRI LSQKIDNELF SMMFSGRYII LLMGLFSTYT GLIYNDCFSK ALNLFGSSWS
     VRPMFTDTWS EDLLKHTSVL QLNPNVTGVF NGPYPFGIDP IWSLATNKLT FLNSFKMKMS
     VILGIIHMIF GVALSVLNHI YFKKPLNIYL SFIPEMIFMT TLFGYLVILI IYKWCAYDVS
     TSMVAPSLLI HFINMFLFSY QDTSLPMLYK GQMGLQCFLV VCAIICVPWM LVLKPLILRR
     QYLRRKHLGT HNFGGIRVGN GPTEEDAEII QHDQLSMHSD EEEEFDFGDT VVHQAIHTIE
     YCLGCISNTA SYLRLWALSL AHAQLSEVLW TMVMHIGLNI RSLGGGIALV FIFSAFATLT
     IAILLIMEGL SAFLHALRLH WVEFRNKFYM GTGFKFLPFS FETIWEGKFD D