VATL3_CAEEL
ID VATL3_CAEEL Reviewed; 161 AA.
AC C0HLB4; P34546; P83577;
DT 12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT 12-SEP-2018, sequence version 1.
DT 03-AUG-2022, entry version 19.
DE RecName: Full=V-type proton ATPase 16 kDa proteolipid subunit c 3 {ECO:0000305};
DE Short=V-ATPase 16 kDa proteolipid subunit c 3 {ECO:0000305};
DE AltName: Full=Vacuolar proton pump 16 kDa proteolipid subunit c 3 {ECO:0000305};
GN Name=vha-3 {ECO:0000312|WormBase:Y38F2AL.4};
GN ORFNames=Y38F2AL.4 {ECO:0000312|WormBase:Y38F2AL.4};
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], 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 [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).
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. V-ATPase is responsible for
CC acidifying and maintaining the pH of intracellular compartments and in
CC some cell types, is targeted to the plasma membrane, where it is
CC responsible for acidifying the extracellular environment (By
CC similarity). Involved in necrotic cell death. Required along with other
CC vacuolar ATPase components for the removal of protein aggregates which
CC form in immature oocytes in the distal gonad. 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 The introduction of sperm triggers V-ATPase accumulation in proximal
CC oocytes and induces lysosomal acidification which leads to engulfing of
CC protein aggregates by lysosomes and subsequent clearance of the
CC aggregates. Lysosomal acidification also leads to changes in
CC mitochondrial morphology and function. Mitochondria in distal immature
CC oocytes are fragmented, produce high levels of reactive oxygen species
CC (ROS) and have high membrane potential, indicative of metabolic
CC inactivity. In contrast, mitochondria in proximal mature oocytes are
CC tubular with lower ROS levels and membrane potential, indicative of an
CC active metabolic state required for aggregate mobilization before
CC clearance (By similarity). {ECO:0000250|UniProtKB:C0HLB3,
CC ECO:0000250|UniProtKB:P23956}.
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 ubiquitously. Higher levels of vha-2 are
CC found in adult H-shaped excretory cell and rectum. Higher levels of
CC vha-3 are found in gastrointestinal and hypodermal cells, as well as H-
CC shaped excretory cell. {ECO:0000269|PubMed:9712884}.
CC -!- DEVELOPMENTAL STAGE: High levels during embryogenesis, moderate levels
CC during L1, L4 and adult stages and very low levels during L2 and L3
CC stages. {ECO:0000269|PubMed:9712884}.
CC -!- MISCELLANEOUS: Vha-11 and vha-3 are transcribed on a dicistronic
CC transcript where vha-3 is the upstream transcript and vha-11 the
CC downstream.
CC -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC {ECO:0000305}.
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DR EMBL; AB009566; BAA75066.1; -; mRNA.
DR EMBL; BX284603; CAA82355.1; -; Genomic_DNA.
DR PIR; S40714; S40714.
DR RefSeq; NP_499166.1; NM_066765.6.
DR RefSeq; NP_500188.1; NM_067787.6.
DR AlphaFoldDB; C0HLB4; -.
DR SMR; C0HLB4; -.
DR EnsemblMetazoa; R10E11.2.1; R10E11.2.1; WBGene00006911.
DR GeneID; 187779; -.
DR KEGG; cel:CELE_R10E11.2; -.
DR CTD; 187779; -.
DR WormBase; Y38F2AL.4; CE06290; WBGene00006912; vha-3.
DR GeneTree; ENSGT00550000074873; -.
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:C0HLB4; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00006911; Expressed in embryo and 4 other tissues.
DR ExpressionAtlas; C0HLB4; 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: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 3"
FT /id="PRO_0000445076"
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
