ID   VATF_CAEEL              Reviewed;         121 AA.
AC   Q23680;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=Probable V-type proton ATPase subunit F;
DE            Short=V-ATPase subunit F;
DE   AltName: Full=Vacuolar proton pump subunit F;
GN   Name=vha-9 {ECO:0000312|WormBase:ZK970.4};
GN   ORFNames=ZK970.4 {ECO:0000312|WormBase:ZK970.4};
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 [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   [2]
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: Subunit of the V1 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
CC       along with other vacuolar ATPase components for the removal of protein
CC       aggregates which form in immature oocytes in the distal gonad
CC       (PubMed:29168500). This removal occurs as the oocytes mature and move
CC       to the proximal gonad, is triggered by the introduction of sperm
CC       through mating and occurs before fertilization (PubMed:29168500). The
CC       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 (PubMed:29168500). Lysosomal acidification also leads to
CC       changes in mitochondrial morphology and function (PubMed:29168500).
CC       Mitochondria in distal immature oocytes are fragmented, produce high
CC       levels of reactive oxygen species (ROS) and have high membrane
CC       potential, indicative of metabolic inactivity (PubMed:29168500). In
CC       contrast, mitochondria in proximal mature oocytes are tubular with
CC       lower ROS levels and membrane potential, indicative of an active
CC       metabolic state required for aggregate mobilization before clearance
CC       (PubMed:29168500). {ECO:0000250|UniProtKB:Q28029,
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:Q28029}.
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.
CC       {ECO:0000269|PubMed:29168500}.
CC   -!- SIMILARITY: Belongs to the V-ATPase F subunit family. {ECO:0000305}.
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DR   EMBL; BX284602; CAA88888.1; -; Genomic_DNA.
DR   PIR; T28128; T28128.
DR   RefSeq; NP_496217.1; NM_063816.5.
DR   AlphaFoldDB; Q23680; -.
DR   SMR; Q23680; -.
DR   BioGRID; 39915; 9.
DR   DIP; DIP-25749N; -.
DR   IntAct; Q23680; 1.
DR   STRING; 6239.ZK970.4.2; -.
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; Q23680; -.
DR   PaxDb; Q23680; -.
DR   PeptideAtlas; Q23680; -.
DR   EnsemblMetazoa; ZK970.4.1; ZK970.4.1; WBGene00006918.
DR   GeneID; 174596; -.
DR   UCSC; ZK970.4.1; c. elegans.
DR   CTD; 174596; -.
DR   WormBase; ZK970.4; CE02404; WBGene00006918; vha-9.
DR   eggNOG; KOG3432; Eukaryota.
DR   GeneTree; ENSGT00390000013208; -.
DR   HOGENOM; CLU_135754_0_0_1; -.
DR   InParanoid; Q23680; -.
DR   OMA; YTNAFPA; -.
DR   OrthoDB; 1483558at2759; -.
DR   PhylomeDB; Q23680; -.
DR   Reactome; R-CEL-1222556; ROS and RNS production in phagocytes.
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:Q23680; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00006918; Expressed in larva and 4 other tissues.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0033180; C:proton-transporting V-type ATPase, V1 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   Gene3D; 3.40.50.10580; -; 1.
DR   InterPro; IPR008218; ATPase_V1-cplx_f_g_su.
DR   InterPro; IPR005772; ATPase_V1-cplx_fsu_euk.
DR   InterPro; IPR036906; ATPase_V1_fsu_sf.
DR   Pfam; PF01990; ATP-synt_F; 1.
DR   PIRSF; PIRSF015945; ATPase_V1_F_euk; 1.
DR   SUPFAM; SSF159468; SSF159468; 1.
DR   TIGRFAMs; TIGR01101; V_ATP_synt_F; 1.
PE   3: Inferred from homology;
KW   Hydrogen ion transport; Ion transport; Reference proteome; Transport.
FT   CHAIN           1..121
FT                   /note="Probable V-type proton ATPase subunit F"
FT                   /id="PRO_0000144804"
SQ   SEQUENCE   121 AA;  13312 MW;  403DB2CC9996E71A CRC64;
     MASAAKGKIL AVIGDEDTVV GFLLGGVGEL NKARKPNYLI VDKQTTVQEI EEAFNGFCAR
     DDIAIILINQ HIAEMIRYAV DNHTQSIPAV LEIPSKEAPY DPSKDSILNR ARGLFNPEDF
     R