VATL3_CAEBR
ID VATL3_CAEBR Reviewed; 161 AA.
AC C0HLB6; A8XA51; Q612A5;
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:0000250|UniProtKB:C0HLB4};
GN ORFNames=CBG16825 {ECO:0000312|WormBase:CBG16825};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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 -!- 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. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HE600944; CAP34689.1; -; Genomic_DNA.
DR RefSeq; XP_002641670.1; XM_002641624.1.
DR RefSeq; XP_002645131.1; XM_002645085.1.
DR AlphaFoldDB; C0HLB6; -.
DR SMR; C0HLB6; -.
DR EnsemblMetazoa; CBG10000.1; CBG10000.1; WBGene00031488.
DR EnsemblMetazoa; CBG16825.1; CBG16825.1; WBGene00036658.
DR GeneID; 8583664; -.
DR GeneID; 8587129; -.
DR KEGG; cbr:CBG_10000; -.
DR KEGG; cbr:CBG_16825; -.
DR CTD; 8583664; -.
DR CTD; 8587129; -.
DR WormBase; CBG16825; CBP10352; WBGene00036658; Cbr-vha-3.
DR OMA; NFIQLGA; -.
DR Proteomes; UP000008549; Chromosome IV.
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; IEA:EnsemblMetazoa.
DR GO; GO:0070265; P:necrotic cell death; IEA:EnsemblMetazoa.
DR GO; GO:0012501; P:programmed cell death; IEA:UniProtKB-KW.
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 3: Inferred from homology;
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_0000445075"
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; 16402 MW; 90561A2B32220198 CRC64;
MSYDLETAEH AAYAPFFGYM GAASAQIFTV LGAAYGTAKS AVGICSMGVM RPELIMKSVI
PVIMAGIIGI YGLVVAMVLK GKVQAASAGY DLNKGFAHLA AGLTCGLCGL GAGYAIGIVG
DAGVRGTAQQ PRLFVGMILI LIFSEVLGLY GMIVALILGT S
