VATL1_CAEEL
ID VATL1_CAEEL Reviewed; 169 AA.
AC Q21898;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=V-type proton ATPase 16 kDa proteolipid subunit c 1 {ECO:0000305};
DE Short=V-ATPase 16 kDa proteolipid subunit c 1 {ECO:0000305};
DE AltName: Full=Vacuolar proton pump 16 kDa proteolipid subunit c 1 {ECO:0000305};
GN Name=vha-1 {ECO:0000312|WormBase:R10E11.8};
GN ORFNames=R10E11.8 {ECO:0000312|WormBase:R10E11.8};
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], AND TISSUE SPECIFICITY.
RX PubMed=9305897;
RA Oka T., Yamamoto R., Futai M.;
RT "Three vha genes encode proteolipids of Caenorhabditis elegans vacuolar-
RT type ATPase. Gene structures and preferential expression in an H-shaped
RT excretory cell and rectal cells.";
RL J. Biol. Chem. 272:24387-24392(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=9712884; DOI=10.1074/jbc.273.35.22570;
RA Oka T., Yamamoto R., Futai M.;
RT "Multiple genes for vacuolar-type ATPase proteolipids in Caenorhabditis
RT elegans: a new gene, vha-3, has a distinct cell-specific distribution.";
RL J. Biol. Chem. 273:22570-22576(1998).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15866168; DOI=10.1016/j.devcel.2005.02.018;
RA Kontani K., Moskowitz I.P.G., Rothman J.H.;
RT "Repression of cell-cell fusion by components of the C. elegans vacuolar
RT ATPase complex.";
RL Dev. Cell 8:787-794(2005).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16785323; DOI=10.1083/jcb.200511072;
RA Liegeois S., Benedetto A., Garnier J.M., Schwab Y., Labouesse M.;
RT "The V0-ATPase mediates apical secretion of exosomes containing Hedgehog-
RT related proteins in Caenorhabditis elegans.";
RL J. Cell Biol. 173:949-961(2006).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29168500; DOI=10.1038/nature24620;
RA Bohnert K.A., Kenyon C.;
RT "A lysosomal switch triggers proteostasis renewal in the immortal C.
RT elegans germ lineage.";
RL Nature 551:629-633(2017).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28581477; DOI=10.1038/ncb3539;
RA Sinclair J., Pinter K., Samuel T., Beardsley S., Yuan X., Zhang J.,
RA Meng K., Yun S., Krause M., Hamza I.;
RT "Inter-organ signalling by HRG-7 promotes systemic haem homeostasis.";
RL Nat. Cell Biol. 19:799-807(2017).
CC -!- FUNCTION: Proton-conducting pore forming of the V0 complex of
CC vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a
CC peripheral complex (V1) that hydrolyzes ATP and a membrane integral
CC complex (V0) that translocates protons (By similarity). V-ATPase is
CC responsible for acidifying and maintaining the pH of intracellular
CC compartments and in some cell types, is targeted to the plasma
CC membrane, where it is responsible for acidifying the extracellular
CC environment (By similarity). Required along with other vacuolar ATPase
CC components for the removal of protein aggregates which form in immature
CC oocytes in the distal gonad (PubMed:29168500). This removal occurs as
CC the oocytes mature and move to the proximal gonad, is triggered by the
CC introduction of sperm through mating and occurs before fertilization
CC (PubMed:29168500). The introduction of sperm triggers V-ATPase
CC accumulation in proximal oocytes and induces lysosomal acidification
CC which leads to engulfing of protein aggregates by lysosomes and
CC subsequent clearance of the aggregates (PubMed:29168500). Lysosomal
CC acidification also leads to changes in mitochondrial morphology and
CC function (PubMed:29168500). Mitochondria in distal immature oocytes are
CC fragmented, produce high levels of reactive oxygen species (ROS) and
CC have high membrane potential, indicative of metabolic inactivity
CC (PubMed:29168500). In contrast, mitochondria in proximal mature oocytes
CC are tubular with lower ROS levels and membrane potential, indicative of
CC an active metabolic state required for aggregate mobilization before
CC clearance (PubMed:29168500). Plays a role in the processing and
CC secretion of the aspartic protease hrg-7 from the intestine
CC (PubMed:28581477). During embryonic development, the V-ATPase is
CC required to repress fusion of epidermal cells probably by negatively
CC regulating eff-1-mediated cell fusion (PubMed:15866168). Involved in
CC receptor-mediated endocytosis (PubMed:16785323).
CC {ECO:0000250|UniProtKB:P23956, ECO:0000269|PubMed:15866168,
CC ECO:0000269|PubMed:16785323, ECO:0000269|PubMed:28581477,
CC ECO:0000269|PubMed:29168500}.
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 {ECO:0000250|UniProtKB:P23956}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Adult H-shaped excretory cell and rectum.
CC {ECO:0000269|PubMed:9305897, ECO:0000269|PubMed:9712884}.
CC -!- DEVELOPMENTAL STAGE: High levels during embryogenesis, moderate levels
CC during L1 and adult stages and very low levels during L2-L4 stages.
CC {ECO:0000269|PubMed:9712884}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes embryonic
CC lethality (PubMed:16785323). RNAi-mediated knockdown results in
CC increased protein aggregation in the oocytes of sperm-deficient young
CC adult females which is not eliminated by mating (PubMed:29168500).
CC RNAi-mediated knockdown causes hyperfusion of embryonic epidermal cells
CC (PubMed:15866168). RNAi-mediated knockdown results in the accumulation
CC of the aspartic protease hrg-7 in its immature uncleaved form and in
CC the intestine (PubMed:28581477). Causes defects in alae formation in
CC the few surviving larvae and impairs yolk uptake by the oocytes from
CC the pseudoceolomic cavities (PubMed:16785323). Causes an increase in
CC the section of the excretory canal, which often has multiple lumens and
CC abnormal whorls (PubMed:16785323). {ECO:0000269|PubMed:15866168,
CC ECO:0000269|PubMed:16785323, ECO:0000269|PubMed:28581477,
CC ECO:0000269|PubMed:29168500}.
CC -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC {ECO:0000305}.
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DR EMBL; AB000917; BAA22595.1; -; mRNA.
DR EMBL; BX284603; CAA82354.1; -; Genomic_DNA.
DR PIR; T37235; T37235.
DR RefSeq; NP_499165.1; NM_066764.5.
DR AlphaFoldDB; Q21898; -.
DR SMR; Q21898; -.
DR BioGRID; 41578; 4.
DR DIP; DIP-25947N; -.
DR STRING; 6239.R10E11.8.2; -.
DR TCDB; 3.A.2.2.7; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR EPD; Q21898; -.
DR PaxDb; Q21898; -.
DR PeptideAtlas; Q21898; -.
DR EnsemblMetazoa; R10E11.8.1; R10E11.8.1; WBGene00006910.
DR GeneID; 176383; -.
DR KEGG; cel:CELE_R10E11.8; -.
DR UCSC; R10E11.8.3; c. elegans.
DR CTD; 176383; -.
DR WormBase; R10E11.8; CE06291; WBGene00006910; vha-1.
DR eggNOG; KOG0232; Eukaryota.
DR HOGENOM; CLU_085752_1_2_1; -.
DR InParanoid; Q21898; -.
DR OMA; DPESAMY; -.
DR OrthoDB; 1534092at2759; -.
DR PhylomeDB; Q21898; -.
DR PRO; PR:Q21898; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00006910; Expressed in larva and 7 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0045121; C:membrane raft; HDA:WormBase.
DR GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0007042; P:lysosomal lumen acidification; IMP:UniProtKB.
DR GO; GO:0030728; P:ovulation; IMP:WormBase.
DR GO; GO:1902600; P:proton transmembrane transport; NAS:UniProtKB.
DR GO; GO:0060142; P:regulation of syncytium formation by plasma membrane fusion; IMP:WormBase.
DR Gene3D; 1.20.120.610; -; 1.
DR InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR InterPro; IPR000245; ATPase_proteolipid_csu.
DR InterPro; IPR011555; ATPase_proteolipid_su_C_euk.
DR InterPro; IPR035921; F/V-ATP_Csub_sf.
DR Pfam; PF00137; ATP-synt_C; 2.
DR PRINTS; PR00122; VACATPASE.
DR SUPFAM; SSF81333; SSF81333; 2.
DR TIGRFAMs; TIGR01100; V_ATP_synt_C; 1.
PE 2: Evidence at transcript level;
KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..169
FT /note="V-type proton ATPase 16 kDa proteolipid subunit c 1"
FT /id="PRO_0000071757"
FT TOPO_DOM 1..23
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..66
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 88..106
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..145
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 167..169
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT SITE 153
FT /note="Essential for proton translocation"
FT /evidence="ECO:0000250|UniProtKB:P63081"
SQ SEQUENCE 169 AA; 16954 MW; 65D6D23037D08187 CRC64;
MSTDTKQIIA DALLKNEQAM YGPFFGSLGV TSAMAFAAAG SAYGTAKAGT GIASMAVARP
DLVMKAIIPV VMAGIVAIYG LVVAVIVSGK VEPAGANYTI NNAFSQFAGG LVCGLCGLGA
GYAIGIAGDA GVRALSQQPR MFVGMILILI FAEVLGLYGM IVALILGAT
