VPP1_CAEEL
ID VPP1_CAEEL Reviewed; 905 AA.
AC P30628; Q23555; Q9GPJ3; Q9GPJ4; Q9GPJ5; Q9GPJ6; Q9GPJ7; Q9GPJ8;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2002, sequence version 3.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=V-type proton ATPase 116 kDa subunit a 1 {ECO:0000305};
DE Short=V-ATPase 116 kDa isoform a 1 {ECO:0000305};
DE AltName: Full=Uncoordinated protein 32 {ECO:0000312|WormBase:ZK637.8a};
DE AltName: Full=Vacuolar proton translocating ATPase 116 kDa subunit a 1 {ECO:0000305};
GN Name=unc-32 {ECO:0000303|PubMed:11110798, ECO:0000312|WormBase:ZK637.8a};
GN ORFNames=ZK637.8 {ECO:0000312|WormBase:ZK637.8a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B; C; D; E AND F), TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Bristol N2;
RX PubMed=11110798; DOI=10.1074/jbc.m009451200;
RA Pujol N., Bonnerot C., Ewbank J.J., Kohara Y., Thierry-Mieg D.;
RT "The Caenorhabditis elegans unc-32 gene encodes alternative forms of a
RT vacuolar ATPase a subunit.";
RL J. Biol. Chem. 276:11913-11921(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=1538779; DOI=10.1038/356037a0;
RA Sulston J., Du Z., Thomas K., Wilson R., Hillier L., Staden R.,
RA Halloran N., Green P., Thierry-Mieg J., Qiu L., Dear S., Coulson A.,
RA Craxton M., Durbin R., Berks M., Metzstein M., Hawkins T., Ainscough R.,
RA Waterston R.;
RT "The C. elegans genome sequencing project: a beginning.";
RL Nature 356:37-41(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [4]
RP INTERACTION WITH VHA-11, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=11441002; DOI=10.1074/jbc.m101652200;
RA Oka T., Toyomura T., Honjo K., Wada Y., Futai M.;
RT "Four subunit a isoforms of Caenorhabditis elegans vacuolar H+-ATPase.
RT Cell-specific expression during development.";
RL J. Biol. Chem. 276:33079-33085(2001).
RN [5]
RP FUNCTION.
RX PubMed=16005300; DOI=10.1016/j.cub.2005.05.057;
RA Syntichaki P., Samara C., Tavernarakis N.;
RT "The vacuolar H+ -ATPase mediates intracellular acidification required for
RT neurodegeneration in C. elegans.";
RL Curr. Biol. 15:1249-1254(2005).
RN [6]
RP FUNCTION.
RX PubMed=20148972; DOI=10.1111/j.1742-4658.2010.07573.x;
RA Levitte S., Salesky R., King B., Coe Smith S., Depper M., Cole M.,
RA Hermann G.J.;
RT "A Caenorhabditis elegans model of orotic aciduria reveals enlarged
RT lysosome-related organelles in embryos lacking umps-1 function.";
RL FEBS J. 277:1420-1439(2010).
RN [7]
RP FUNCTION.
RX PubMed=22426883; DOI=10.1534/genetics.112.139667;
RA Ernstrom G.G., Weimer R., Pawar D.R., Watanabe S., Hobson R.J.,
RA Greenstein D., Jorgensen E.M.;
RT "V-ATPase V1 sector is required for corpse clearance and neurotransmission
RT in Caenorhabditis elegans.";
RL Genetics 191:461-475(2012).
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). Regulates
CC the size of gut granules during embryonic development
CC (PubMed:20148972). In neurons, required for necrotic cell death by
CC promoting intracellular acidification (PubMed:16005300). Required for
CC cell death induced by hypoxia (PubMed:16005300). Required for
CC acidification of synaptic vesicles and the release of neurotransmitters
CC from adult neurons (PubMed:22426883). {ECO:0000250|UniProtKB:G5EGP4,
CC ECO:0000250|UniProtKB:P32563, ECO:0000250|UniProtKB:Q29466,
CC ECO:0000269|PubMed:16005300, ECO:0000269|PubMed:20148972,
CC ECO:0000269|PubMed:22426883}.
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 the accessory subunits vah-19/Ac45 and vah-20/PRR (By similarity).
CC Interacts with V-type proton ATPase subunit C vha-11 (PubMed:11441002).
CC {ECO:0000250|UniProtKB:Q29466, ECO:0000269|PubMed:11441002}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11441002}; Multi-
CC pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=a {ECO:0000312|WormBase:ZK637.8a}; Synonyms=A;
CC IsoId=P30628-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:ZK637.8b}; Synonyms=B;
CC IsoId=P30628-2; Sequence=VSP_000346, VSP_000348;
CC Name=c {ECO:0000312|WormBase:ZK637.8c}; Synonyms=C;
CC IsoId=P30628-3; Sequence=VSP_000347;
CC Name=d {ECO:0000312|WormBase:ZK637.8d}; Synonyms=D;
CC IsoId=P30628-4; Sequence=VSP_000348;
CC Name=e {ECO:0000312|WormBase:ZK637.8e}; Synonyms=E;
CC IsoId=P30628-5; Sequence=VSP_000347, VSP_000348;
CC Name=f {ECO:0000312|WormBase:ZK637.8f}; Synonyms=F;
CC IsoId=P30628-6; Sequence=VSP_000346;
CC -!- TISSUE SPECIFICITY: Ubiquitous expression in embryos. Expressed in
CC gonads, intestine, neurons in the head and motoneurons in the ventral
CC cord of larvae and adults (PubMed:11110798). Expressed in the vulvae
CC and spermathecal uterine valves (PubMed:11441002). Weakly expressed in
CC the pharynx (PubMed:11441002). {ECO:0000269|PubMed:11110798,
CC ECO:0000269|PubMed:11441002}.
CC -!- TISSUE SPECIFICITY: [Isoform c]: Specifically expressed in the nervous
CC system. {ECO:0000269|PubMed:11110798}.
CC -!- TISSUE SPECIFICITY: [Isoform f]: Specifically expressed in the nervous
CC system. {ECO:0000269|PubMed:11110798}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos, larvae and adult. Highest
CC level of expression is in early embryos (PubMed:11110798). Expressed in
CC the nerve ring and ventral nerve cord in L1 larvae (PubMed:11441002).
CC {ECO:0000269|PubMed:11110798, ECO:0000269|PubMed:11441002}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes embryonic
CC lethality at the 100-cell stage. {ECO:0000269|PubMed:11441002}.
CC -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; AF320899; AAG41432.1; -; mRNA.
DR EMBL; AF320900; AAG41433.1; -; mRNA.
DR EMBL; AF320901; AAG41434.1; -; mRNA.
DR EMBL; AF320902; AAG41435.1; -; mRNA.
DR EMBL; AF320903; AAG41436.1; -; mRNA.
DR EMBL; AF320904; AAG41437.1; -; mRNA.
DR EMBL; BX284603; CAA77448.2; -; Genomic_DNA.
DR EMBL; BX284603; CAA77453.2; -; Genomic_DNA.
DR EMBL; BX284603; CAD30450.1; -; Genomic_DNA.
DR EMBL; BX284603; CAD30451.1; -; Genomic_DNA.
DR EMBL; BX284603; CAD30452.1; -; Genomic_DNA.
DR EMBL; BX284603; CAD30453.1; -; Genomic_DNA.
DR PIR; S15795; S15795.
DR RefSeq; NP_001023017.1; NM_001027846.1. [P30628-1]
DR RefSeq; NP_001023018.1; NM_001027847.2. [P30628-2]
DR RefSeq; NP_001023019.1; NM_001027848.4. [P30628-3]
DR RefSeq; NP_001023020.1; NM_001027849.1. [P30628-4]
DR RefSeq; NP_001023021.1; NM_001027850.3. [P30628-5]
DR RefSeq; NP_001023022.1; NM_001027851.1. [P30628-6]
DR AlphaFoldDB; P30628; -.
DR BMRB; P30628; -.
DR SMR; P30628; -.
DR BioGRID; 41458; 7.
DR STRING; 6239.ZK637.8a; -.
DR TCDB; 3.A.2.2.7; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR iPTMnet; P30628; -.
DR EPD; P30628; -.
DR PaxDb; P30628; -.
DR PeptideAtlas; P30628; -.
DR PRIDE; P30628; -.
DR EnsemblMetazoa; ZK637.8a.1; ZK637.8a.1; WBGene00006768. [P30628-1]
DR EnsemblMetazoa; ZK637.8b.1; ZK637.8b.1; WBGene00006768. [P30628-2]
DR EnsemblMetazoa; ZK637.8c.1; ZK637.8c.1; WBGene00006768. [P30628-3]
DR EnsemblMetazoa; ZK637.8d.1; ZK637.8d.1; WBGene00006768. [P30628-4]
DR EnsemblMetazoa; ZK637.8e.1; ZK637.8e.1; WBGene00006768. [P30628-5]
DR EnsemblMetazoa; ZK637.8f.1; ZK637.8f.1; WBGene00006768. [P30628-6]
DR GeneID; 176257; -.
DR KEGG; cel:CELE_ZK637.8; -.
DR UCSC; ZK637.8e; c. elegans. [P30628-1]
DR CTD; 176257; -.
DR WormBase; ZK637.8a; CE30573; WBGene00006768; unc-32. [P30628-1]
DR WormBase; ZK637.8b; CE30574; WBGene00006768; unc-32. [P30628-2]
DR WormBase; ZK637.8c; CE30575; WBGene00006768; unc-32. [P30628-3]
DR WormBase; ZK637.8d; CE30576; WBGene00006768; unc-32. [P30628-4]
DR WormBase; ZK637.8e; CE30577; WBGene00006768; unc-32. [P30628-5]
DR WormBase; ZK637.8f; CE30578; WBGene00006768; unc-32. [P30628-6]
DR eggNOG; KOG2189; Eukaryota.
DR GeneTree; ENSGT00950000182881; -.
DR InParanoid; P30628; -.
DR OMA; FSYDRAR; -.
DR OrthoDB; 181796at2759; -.
DR PhylomeDB; P30628; -.
DR Reactome; R-CEL-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-77387; Insulin receptor recycling.
DR Reactome; R-CEL-917977; Transferrin endocytosis and recycling.
DR Reactome; R-CEL-9639288; Amino acids regulate mTORC1.
DR Reactome; R-CEL-983712; Ion channel transport.
DR PRO; PR:P30628; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00006768; Expressed in pharyngeal muscle cell (C elegans) and 9 other tissues.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IPI:WormBase.
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:0050830; P:defense response to Gram-positive bacterium; IGI:UniProtKB.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0040011; P:locomotion; IMP:WormBase.
DR GO; GO:0040013; P:negative regulation of locomotion; NAS:UniProtKB.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0001956; P:positive regulation of neurotransmitter secretion; IMP:UniProtKB.
DR GO; GO:0043068; P:positive regulation of programmed cell death; IMP:WormBase.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; NAS:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; IMP:WormBase.
DR GO; GO:0007271; P:synaptic transmission, cholinergic; IMP:WormBase.
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 Alternative splicing; Hydrogen ion transport; Ion transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..905
FT /note="V-type proton ATPase 116 kDa subunit a 1"
FT /id="PRO_0000119221"
FT TOPO_DOM 1..424
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 425..443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 444..445
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 446..462
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 463..477
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 478..507
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 508..572
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 573..592
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 593..610
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 611..631
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 632..699
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 700..719
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 720..788
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 789..813
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 814..834
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 835..873
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 874..905
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT VAR_SEQ 154..205
FT /note="VDHDRWRILEGGSGRRGRSTEREETRPLIDIGDMDDDSAARMSAQAAMLRLG
FT -> HEDMIASSAESSGIGEVLSADEEELSGRFSDAMSPLKLQLR (in isoform c
FT and isoform e)"
FT /evidence="ECO:0000303|PubMed:11110798"
FT /id="VSP_000347"
FT VAR_SEQ 154..204
FT /note="VDHDRWRILEGGSGRRGRSTEREETRPLIDIGDMDDDSAARMSAQAAMLRL
FT -> AGTGEMLPPAAVESEEGLELTQHAAAGGATMFANF (in isoform b and
FT isoform f)"
FT /evidence="ECO:0000303|PubMed:11110798"
FT /id="VSP_000346"
FT VAR_SEQ 694..740
FT /note="ATIEIILVVLALVQVPIMLFAKPYFLYRRDKQQSRYSTLTAESNQHQ -> S
FT FFETIFVLVAIACVPVMLFGKPYFLWKEEKERREGGHRQL (in isoform b,
FT isoform d and isoform e)"
FT /evidence="ECO:0000303|PubMed:11110798"
FT /id="VSP_000348"
SQ SEQUENCE 905 AA; 103401 MW; 2B6647EB521A9FBC CRC64;
MGDYVTPGEE PPQPGIYRSE QMCLAQLYLQ SDASYQCVAE LGELGLVQFR DLNPDVSSFQ
RKYVNEVRRC DEMERKLRYL EREIKKDQIP MLDTGENPDA PLPREMIDLE ATFEKLENEL
REVNKNEETL KKNFSELTEL KHILRKTQTF FEEVDHDRWR ILEGGSGRRG RSTEREETRP
LIDIGDMDDD SAARMSAQAA MLRLGFVAGV IQRERLPAFE RLLWRACRGN VFLRTSEIDD
VLNDTVTGDP VNKCVFIIFF QGDHLKTKVK KICEGFRATL YPCPDTPQER REMSIGVMTR
IEDLKTVLGQ TQDHRHRVLV AASKNVRMWL TKVRKIKSIY HTLNLFNIDV TQKCLIAEVW
CPIAELDRIK MALKRGTDES GSQVPSILNR METNEAPPTY NKTNKFTKGF QNIVDAYGIA
TYREINPAPY TMISFPFLFA VMFGDMGHGA IMLLAALFFI LKEKQLEAAR IKDEIFQTFF
GGRYVIFLMG AFSIYTGFMY NDVFSKSINT FGSSWQNTIP ESVIDYYLDD EKRSESQLIL
PPETAFDGNP YPIGVDPVWN LAEGNKLSFL NSMKMKMSVL FGIAQMTFGV LLSYQNFIYF
KSDLDIKYMF IPQMIFLSSI FIYLCIQILS KWLFFGAVGG TVLGYKYPGS NCAPSLLIGL
INMFMMKSRN AGFVDDSGET YPQCYLSTWY PGQATIEIIL VVLALVQVPI MLFAKPYFLY
RRDKQQSRYS TLTAESNQHQ SVRADINQDD AEVVHAPEQT PKPSGHGHGH GDGPLEMGDV
MVYQAIHTIE FVLGCVSHTA SYLRLWALSL AHAQLSDVLW TMVFRNAFVL DGYTGAIATY
ILFFIFGSLS VFILVLMEGL SAFLHALRLH WVEFQSKFYG GLGYEFAPFS FEKILAEERE
AEENL
