VPP1_RAT
ID VPP1_RAT Reviewed; 838 AA.
AC P25286;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 141.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS I AND II), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=1704894; DOI=10.1016/s0021-9258(19)67875-0;
RA Perin M.S., Fried V.A., Stone D.K., Xie X.-S., Suedhof T.C.;
RT "Structure of the 116-kDa polypeptide of the clathrin-coated
RT vesicle/synaptic vesicle proton pump.";
RL J. Biol. Chem. 266:3877-3881(1991).
RN [2] {ECO:0007744|PDB:6VQ6, ECO:0007744|PDB:6VQ7, ECO:0007744|PDB:6VQ8, ECO:0007744|PDB:6VQC, ECO:0007744|PDB:6VQG, ECO:0007744|PDB:6VQH, ECO:0007744|PDB:6VQI, ECO:0007744|PDB:6VQJ, ECO:0007744|PDB:6VQK}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS), FUNCTION, IDENTIFICATION
RP IN THE V-ATPASE COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND TISSUE SPECIFICITY.
RX PubMed=32165585; DOI=10.1126/science.aaz2924;
RA Abbas Y.M., Wu D., Bueler S.A., Robinson C.V., Rubinstein J.L.;
RT "Structure of V-ATPase from the mammalian brain.";
RL Science 367:1240-1246(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:32165585). 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:32165585). Required
CC for assembly and activity of the vacuolar ATPase (By similarity).
CC {ECO:0000250|UniProtKB:P32563, ECO:0000269|PubMed:32165585}.
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:32165585). 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:32165585). 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:32165585). Interacts with SPAAR
CC (By similarity). {ECO:0000250|UniProtKB:Q93050,
CC ECO:0000269|PubMed:32165585}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
CC membrane {ECO:0000269|PubMed:32165585}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle
CC membrane {ECO:0000269|PubMed:32165585}; Multi-pass membrane protein
CC {ECO:0000255}. Melanosome {ECO:0000250|UniProtKB:Q93050}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=I;
CC IsoId=P25286-1; Sequence=Displayed;
CC Name=II;
CC IsoId=P25286-2; Sequence=VSP_000344;
CC -!- TISSUE SPECIFICITY: [Isoform I]: Expressed in brain (at protein level).
CC {ECO:0000269|PubMed:1704894, ECO:0000269|PubMed:32165585}.
CC -!- TISSUE SPECIFICITY: [Isoform II]: Expressed in heart, kidney, liver,
CC spleen, and to a lesser extent in brain. {ECO:0000269|PubMed:1704894}.
CC -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; M58758; AAA41962.1; -; mRNA.
DR PIR; B38656; B38656.
DR RefSeq; NP_113792.2; NM_031604.2.
DR PDB; 6VQ6; EM; 3.90 A; a=1-838.
DR PDB; 6VQ7; EM; 4.00 A; a=1-838.
DR PDB; 6VQ8; EM; 3.90 A; a=1-838.
DR PDB; 6VQC; EM; 3.80 A; a=1-838.
DR PDB; 6VQG; EM; 4.20 A; a=1-838.
DR PDB; 6VQH; EM; 4.40 A; a=1-838.
DR PDB; 6VQI; EM; 4.30 A; a=1-838.
DR PDB; 6VQJ; EM; 5.70 A; a=1-838.
DR PDB; 6VQK; EM; 5.70 A; a=1-838.
DR PDBsum; 6VQ6; -.
DR PDBsum; 6VQ7; -.
DR PDBsum; 6VQ8; -.
DR PDBsum; 6VQC; -.
DR PDBsum; 6VQG; -.
DR PDBsum; 6VQH; -.
DR PDBsum; 6VQI; -.
DR PDBsum; 6VQJ; -.
DR PDBsum; 6VQK; -.
DR AlphaFoldDB; P25286; -.
DR SMR; P25286; -.
DR BioGRID; 248368; 5.
DR IntAct; P25286; 6.
DR MINT; P25286; -.
DR STRING; 10116.ENSRNOP00000052113; -.
DR iPTMnet; P25286; -.
DR PhosphoSitePlus; P25286; -.
DR jPOST; P25286; -.
DR PaxDb; P25286; -.
DR PRIDE; P25286; -.
DR GeneID; 29757; -.
DR KEGG; rno:29757; -.
DR UCSC; RGD:68405; rat. [P25286-1]
DR CTD; 535; -.
DR RGD; 68405; Atp6v0a1.
DR eggNOG; KOG2189; Eukaryota.
DR InParanoid; P25286; -.
DR OrthoDB; 181796at2759; -.
DR PhylomeDB; P25286; -.
DR Reactome; R-RNO-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-77387; Insulin receptor recycling.
DR Reactome; R-RNO-917977; Transferrin endocytosis and recycling.
DR Reactome; R-RNO-983712; Ion channel transport.
DR PRO; PR:P25286; -.
DR Proteomes; UP000002494; 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:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; IDA:SynGO.
DR GO; GO:0043229; C:intracellular organelle; ISO:RGD.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0008021; C:synaptic vesicle; IDA:SynGO.
DR GO; GO:0043195; C:terminal bouton; HDA:ParkinsonsUK-UCL.
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; ISS:UniProtKB.
DR GO; GO:0051117; F:ATPase binding; ISO:RGD.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0016241; P:regulation of macroautophagy; ISO:RGD.
DR GO; GO:1901998; P:toxin transport; ISO:RGD.
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_0000119214"
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 II)"
FT /evidence="ECO:0000303|PubMed:1704894"
FT /id="VSP_000344"
SQ SEQUENCE 838 AA; 96328 MW; D25FAD918638D7EE CRC64;
MGELFRSEEM TLAQLFLQSE AAYCCVSELE ELGKVQFRDL NPDVNVFQRK FVNEVRRCEE
MDRKLRFVEK EIRKANIPIM DTGENPEVPF PRDMIDLEAN FEKIENELKE INTNQEALKR
NFLELTELKF ILRKTQQFFD EMADPDLLEE SSSLLEPNEM GRGAPLRLGF VAGVINRERI
PTFERMLWRV CRGNVFLRQA EIENPLEDPV TGDYVHKSVF IIFFQGDQLK NRVKKICEGF
RASLYPCPET PQERKEMASG VNTRIDDLQM VLNQTEDHRQ RVLQAAAKNI RVWFIKVRKM
KAIYHTLNLC NIDVTQKCLI AEVWCPVTDL DSIQFALRRG TEHSGSTVPS ILNRMQTNQT
PPTYNKTNKF THGFQNIVDA YGIGTYREIN PAPYTVITFP FLFAVMFGDF GHGILMTLFA
VWMVLRESRI LSQKNENEMF SMVFSGRYII LLMGLFSIYT GLIYNDCFSK SLNIFGSSWS
VRPMFTIGNW TEETLLGSSV LQLNPAIPGV FGGPYPFGID PIWNIATNKL TFLNSFKMKM
SVILGIIHML FGVSLSLFNH IYFKKPLNIY FGFIPEIIFM SSLFGYLVIL IFYKWTAYDA
HSSRNAPSLL IHFINMFLFS YPESGNAMLY SGQKGIQCFL IVVAMLCVPW MLLFKPLILR
HQYLRKKHLG TLNFGGIRVG NGPTEEDAEI IQHDQLSTHS EDAEEPTEDE VFDFGDTMVH
QAIHTIEYCL GCISNTASYL RLWALSLAHA QLSEVLWTMV IHIGLHVRSL AGGLGLFFIF
AAFATLTVAI LLIMEGLSAF LHALRLHWVE FQNKFYTGTG FKFLPFSFEH IREGKFDE
