VPP1_BOVIN
ID VPP1_BOVIN Reviewed; 838 AA.
AC Q29466;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=V-type proton ATPase 116 kDa subunit a 1;
DE Short=V-ATPase 116 kDa subunit a 1;
DE AltName: Full=Clathrin-coated vesicle/synaptic vesicle proton pump 116 kDa subunit;
DE AltName: Full=Vacuolar adenosine triphosphatase subunit Ac116;
DE AltName: Full=Vacuolar proton pump subunit 1;
DE AltName: Full=Vacuolar proton translocating ATPase 116 kDa subunit a isoform 1;
GN Name=ATP6V0A1; Synonyms=ATP6N1, VPP1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=8006034; DOI=10.1016/s0021-9258(17)32549-8;
RA Peng S.-B., Crider B.P., Xie X.-S., Stone D.K.;
RT "Alternative mRNA splicing generates tissue-specific isoforms of 116-kDa
RT polypeptide of vacuolar proton pump.";
RL J. Biol. Chem. 269:17262-17266(1994).
RN [2] {ECO:0007744|PDB:6XBW, ECO:0007744|PDB:6XBY}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.37 ANGSTROMS), FUNCTION, IDENTIFICATION
RP IN THE V-ATPASE COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND TISSUE SPECIFICITY.
RX PubMed=32764564; DOI=10.1038/s41467-020-17762-9;
RA Wang R., Long T., Hassan A., Wang J., Sun Y., Xie X.S., Li X.;
RT "Cryo-EM structures of intact V-ATPase from bovine brain.";
RL Nat. Commun. 11:3921-3921(2020).
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 (PubMed:32764564). 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 (PubMed:32764564). Required
CC for assembly and activity of the vacuolar ATPase (By similarity).
CC {ECO:0000250|UniProtKB:P32563, ECO:0000269|PubMed:32764564}.
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 (PubMed:32764564). The V1 complex consists of three
CC catalytic AB heterodimers that form a heterohexamer, three peripheral
CC stalks each consisting of EG heterodimers, one central rotor including
CC subunits D and F, and the regulatory subunits C and H
CC (PubMed:32764564). The proton translocation complex V0 consists of the
CC proton transport subunit a, a ring of proteolipid subunits c9c'',
CC rotary subunit d, subunits e and f, and the accessory subunits
CC ATP6AP1/Ac45 and ATP6AP2/PRR (PubMed:32764564). Interacts with SPAAR
CC (By similarity). {ECO:0000250|UniProtKB:Q93050,
CC ECO:0000269|PubMed:32764564}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
CC membrane {ECO:0000269|PubMed:32764564}; 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=I;
CC IsoId=Q29466-1; Sequence=Displayed;
CC Name=2; Synonyms=II;
CC IsoId=Q29466-2; Sequence=VSP_000341;
CC -!- TISSUE SPECIFICITY: [Isoform 1]: Expressed in brain (at protein level).
CC {ECO:0000269|PubMed:32764564, ECO:0000269|PubMed:8006034}.
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Expressed heart, kidney, liver,
CC spleen, and to a lesser extent in brain. {ECO:0000269|PubMed:8006034}.
CC -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; L31770; AAA21492.1; -; mRNA.
DR PIR; A54163; A54163.
DR RefSeq; NP_777179.1; NM_174754.2. [Q29466-1]
DR PDB; 6XBW; EM; 3.37 A; a=1-838.
DR PDB; 6XBY; EM; 3.79 A; a=1-838.
DR PDB; 7KHR; EM; 3.62 A; a=1-838.
DR PDBsum; 6XBW; -.
DR PDBsum; 6XBY; -.
DR PDBsum; 7KHR; -.
DR AlphaFoldDB; Q29466; -.
DR SMR; Q29466; -.
DR CORUM; Q29466; -.
DR STRING; 9913.ENSBTAP00000025588; -.
DR PaxDb; Q29466; -.
DR PeptideAtlas; Q29466; -.
DR PRIDE; Q29466; -.
DR GeneID; 286768; -.
DR KEGG; bta:286768; -.
DR CTD; 535; -.
DR eggNOG; KOG2189; Eukaryota.
DR InParanoid; Q29466; -.
DR OrthoDB; 181796at2759; -.
DR Proteomes; UP000009136; 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; IDA:UniProtKB.
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:0045851; P:pH reduction; IC:UniProtKB.
DR GO; GO:1902600; P:proton transmembrane transport; IC:UniProtKB.
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 3D-structure; Alternative splicing; Cytoplasmic vesicle;
KW Hydrogen ion transport; Ion transport; Membrane; Phosphoprotein;
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_0000119210"
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"
FT MOD_RES 250
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1G4"
FT MOD_RES 360
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q93050"
FT MOD_RES 364
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1G4"
FT VAR_SEQ 706..711
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8006034"
FT /id="VSP_000341"
FT STRAND 13..19
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 24..32
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 54..74
FT /evidence="ECO:0007829|PDB:6XBW"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 94..114
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 116..139
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 180..191
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 231..239
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:6XBW"
FT TURN 251..253
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 254..287
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 290..308
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 315..324
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 330..340
FT /evidence="ECO:0007829|PDB:6XBW"
FT TURN 341..345
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 351..354
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 372..381
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 392..406
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 410..425
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 427..432
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 438..445
FT /evidence="ECO:0007829|PDB:6XBW"
FT TURN 446..448
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 449..463
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 482..488
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 492..495
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 496..498
FT /evidence="ECO:0007829|PDB:6XBW"
FT TURN 507..510
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 516..518
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 522..525
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 526..528
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 529..558
FT /evidence="ECO:0007829|PDB:6XBW"
FT TURN 559..564
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 566..572
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 574..583
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 585..597
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 600..602
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 609..617
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 624..626
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 633..645
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 647..654
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 715..729
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 731..737
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 738..740
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 741..758
FT /evidence="ECO:0007829|PDB:6XBW"
FT TURN 759..761
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 762..765
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 768..770
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 774..789
FT /evidence="ECO:0007829|PDB:6XBW"
FT TURN 790..792
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 793..808
FT /evidence="ECO:0007829|PDB:6XBW"
FT TURN 809..814
FT /evidence="ECO:0007829|PDB:6XBW"
SQ SEQUENCE 838 AA; 96302 MW; 07F56C26C6DE6864 CRC64;
MGELFRSEEM TLAQLFLQSE AAYCCVSELG ELGKVQFRDL NPDVNVFQRK FVNEVRRCEE
MDRKLRFVEK EIRKANIPIM DTGENPEVPF PRDMIDLEAN FEKIENELKE INTNQEALKR
NFLELTELKF ILRKTQQFFD EMADPDLLEE SSSLLEPSEM GRGTPLRLGF VAGVINRERI
PTFERMLWRV CRGNVFLRQA EIENPLEDPV TGDYVHKSVF IIFFQGDQLK NRVKKICEGF
RASLYPCPET PQERKEMASG VNTRIDDLQM VLNQTEDHRQ RVLQAAAKNI RVWFIKVRKM
KAIYHTLNLC NIDVTQKCLI AEVWCPVTDL DSIQFALRRG TEHSGSTVPS ILNRMQTNQT
PPTYNKTNKF TYGFQNIVDA YGIGTYREIN PAPYTIITFP FLFAVMFGDL GHGILMTLFA
VWMVLKESRI LSQKNENEMF STIFSGRYII LLMGVFSIYT GLIYNDCFSK SLNIFGSSWS
VRPMFDIYNW TEETLRGNPV LQLNPAVTGV FGGPYPFGID PIWNIATNKL TFLNSFKMKM
SVILGIIHML FGVSLSLFNH TYFKKPLNIY FGFIPEIIFM TSLFGYLVIL IFYKWTAYNA
KTSEKAPSLL IHFINMFLFS YGDSGNSMLY SGQKGIQCFL VVVALLCVPW MLLFKPLVLR
RQYLRRKHLG TLNFGGIRVG NGPTEEDAEI IQHDQLSTHS EDAEEPTEDE VFDFGDTMVH
QAIHTIEYCL GCISNTASYL RLWALSLAHA QLSEVLWTMV IHIGLKVKSL AGGLALFFIF
AAFATLTVAI LLIMEGLSAF LHALRLHWVE FQNKFYSGTG FKFLPFSFEH IREGKFDD
