VATL2_CAEEL
ID VATL2_CAEEL Reviewed; 161 AA.
AC C0HLB3; P34546; P83577;
DT 12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT 12-SEP-2018, sequence version 1.
DT 03-AUG-2022, entry version 20.
DE RecName: Full=V-type proton ATPase 16 kDa proteolipid subunit c 2 {ECO:0000305};
DE Short=V-ATPase 16 kDa proteolipid subunit c 2 {ECO:0000305};
DE AltName: Full=Vacuolar proton pump 16 kDa proteolipid subunit c 2 {ECO:0000305};
GN Name=vha-2 {ECO:0000312|WormBase:R10E11.2};
GN ORFNames=R10E11.2 {ECO:0000312|WormBase:R10E11.2};
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 FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22157748; DOI=10.1038/emboj.2011.447;
RA Troulinaki K., Tavernarakis N.;
RT "Endocytosis and intracellular trafficking contribute to necrotic
RT neurodegeneration in C. elegans.";
RL EMBO J. 31:654-666(2012).
RN [5]
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).
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). Involved in necrotic cell death
CC (PubMed:22157748). Required along with other vacuolar ATPase components
CC for the removal of protein aggregates which form in immature oocytes in
CC the distal gonad (PubMed:29168500). This removal occurs as the oocytes
CC mature and move to the proximal gonad, is triggered by the introduction
CC 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). {ECO:0000250|UniProtKB:P23956,
CC ECO:0000269|PubMed:22157748, 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: Expressed in the H-shaped excretory cell, rectum,
CC and a pair of cells posterior to the anus.
CC {ECO:0000269|PubMed:9305897}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in increased
CC protein aggregation in the oocytes of sperm-deficient young adult
CC females which is not eliminated by mating (PubMed:29168500). RNAi-
CC mediated knockdown causes a reduction in the formation of neuron cell
CC corpses in a hyperactive mec-4 mutant background (PubMed:22157748).
CC {ECO:0000269|PubMed:22157748, ECO:0000269|PubMed:29168500}.
CC -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC {ECO:0000305}.
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DR EMBL; AB000918; BAA22596.1; -; mRNA.
DR EMBL; BX284603; CAA82355.1; -; Genomic_DNA.
DR PIR; C88565; C88565.
DR RefSeq; NP_499166.1; NM_066765.6.
DR RefSeq; NP_500188.1; NM_067787.6.
DR AlphaFoldDB; C0HLB3; -.
DR SMR; C0HLB3; -.
DR STRING; 6239.R10E11.2; -.
DR EnsemblMetazoa; R10E11.2.1; R10E11.2.1; WBGene00006911.
DR GeneID; 187779; -.
DR KEGG; cel:CELE_R10E11.2; -.
DR CTD; 187779; -.
DR WormBase; R10E11.2; CE06290; WBGene00006911; vha-2.
DR OMA; NFIQLGA; -.
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:C0HLB3; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00006911; Expressed in embryo and 4 other tissues.
DR ExpressionAtlas; C0HLB3; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
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:0007042; P:lysosomal lumen acidification; IMP:UniProtKB.
DR GO; GO:0070265; P:necrotic cell death; IGI:WormBase.
DR GO; GO:0012501; P:programmed cell death; IEA:UniProtKB-KW.
DR GO; GO:1902600; P:proton transmembrane transport; NAS:UniProtKB.
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; Necrosis;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..161
FT /note="V-type proton ATPase 16 kDa proteolipid subunit c 2"
FT /id="PRO_0000071758"
FT TOPO_DOM 1..15
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..58
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 80..98
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..137
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..161
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT SITE 145
FT /note="Essential for proton translocation"
FT /evidence="ECO:0000250|UniProtKB:P63081"
SQ SEQUENCE 161 AA; 16410 MW; 67EDBD2124F12F6E CRC64;
MSYDLETAER AAYAPFFGYM GAASAQIFTV LGAAYGTAKS AVGICSMGVM RPELIMKSVI
PVIMAGIIGI YGLVVAMVLK GKVTSASAGY DLNKGFAHLA AGLTCGLCGL GAGYAIGIVG
DAGVRGTAQQ PRLFVGMILI LIFSEVLGLY GMIVALILGT S
