ID   VATH2_CAEEL             Reviewed;         470 AA.
AC   Q22494;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 168.
DE   RecName: Full=Probable V-type proton ATPase subunit H 2;
DE            Short=V-ATPase subunit H 2;
DE   AltName: Full=Vacuolar proton pump subunit H 2;
GN   Name=vha-15 {ECO:0000312|WormBase:T14F9.1};
GN   ORFNames=T14F9.1 {ECO:0000312|WormBase:T14F9.1};
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).
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). Subunit H is
CC       essential for V-ATPase activity, but not for the assembly of the
CC       complex (By similarity). {ECO:0000250|UniProtKB:O46563,
CC       ECO:0000250|UniProtKB:P41807}.
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:O46563}.
CC   -!- SIMILARITY: Belongs to the V-ATPase H subunit family. {ECO:0000305}.
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DR   EMBL; BX284606; CCD68940.1; -; Genomic_DNA.
DR   PIR; T29380; T29380.
DR   RefSeq; NP_508412.1; NM_076011.3.
DR   AlphaFoldDB; Q22494; -.
DR   SMR; Q22494; -.
DR   BioGRID; 45479; 21.
DR   DIP; DIP-24603N; -.
DR   STRING; 6239.T14F9.1.1; -.
DR   TCDB; 3.A.2.2.7; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR   iPTMnet; Q22494; -.
DR   EPD; Q22494; -.
DR   PaxDb; Q22494; -.
DR   PeptideAtlas; Q22494; -.
DR   EnsemblMetazoa; T14F9.1.1; T14F9.1.1; WBGene00020507.
DR   EnsemblMetazoa; T14F9.1.2; T14F9.1.2; WBGene00020507.
DR   GeneID; 180534; -.
DR   KEGG; cel:CELE_T14F9.1; -.
DR   UCSC; T14F9.1.1; c. elegans.
DR   CTD; 180534; -.
DR   WormBase; T14F9.1; CE07497; WBGene00020507; vha-15.
DR   eggNOG; KOG2759; Eukaryota.
DR   GeneTree; ENSGT00390000003289; -.
DR   HOGENOM; CLU_025709_2_0_1; -.
DR   InParanoid; Q22494; -.
DR   OMA; KDQNVRY; -.
DR   OrthoDB; 751335at2759; -.
DR   PhylomeDB; Q22494; -.
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:Q22494; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00020507; Expressed in larva and 4 other tissues.
DR   GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; IEA:InterPro.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   Gene3D; 1.25.10.10; -; 1.
DR   Gene3D; 1.25.40.150; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR004908; ATPase_V1-cplx_hsu.
DR   InterPro; IPR011987; ATPase_V1-cplx_hsu_C.
DR   InterPro; IPR038497; ATPase_V1-cplx_hsu_C_sf.
DR   PANTHER; PTHR10698; PTHR10698; 1.
DR   Pfam; PF11698; V-ATPase_H_C; 1.
DR   Pfam; PF03224; V-ATPase_H_N; 1.
DR   PIRSF; PIRSF032184; ATPase_V1_H; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   3: Inferred from homology;
KW   Hydrogen ion transport; Ion transport; Reference proteome; Transport.
FT   CHAIN           1..470
FT                   /note="Probable V-type proton ATPase subunit H 2"
FT                   /id="PRO_0000124199"
SQ   SEQUENCE   470 AA;  54213 MW;  1B5989D2F405B562 CRC64;
     MAEVPHHNIP AVDMLNATSR LQLEAQELRN NKPNWGSYFR SQMIQEDDYN FITSFENAKS
     KEERDQVLAA NNANGQAAKT MANLITQVAK DQNVRYVLTL FDDMLQEDKS RVELFHSAAA
     RQKRTVWSQY LGILQRQDNF IVNQMSSIIA KLACFGTTRM EGQDLQYYFS FLKEQLKNST
     TNDYMNTTAR CLQMMLRHDE YRHEFVDSDG VQTLVTALNG KTNFQLQYQL IFAVWCLTFN
     ADIARKAPSL GLIQALGDIL SESTKEKVIR IILASFVNIL SKVDEREVKR EAALQMVQCK
     TLKTLELMDA KKYDDPDLED DVKFLTEELT LSVHDLSSYD EYYSEVRSGR LQWSPVHKSE
     KFWRENASKF NDKQFEVVKI LIKLLESSHD PLILCVASHD IGEYVRHYPR GKTVVEQYQG
     KAAVMRLLTA EDPNVRYHAL LAVQKLMVHN WEYLGKQLDS DVQTDTVAVK