ID   VATH1_CAEBR             Reviewed;         451 AA.
AC   A8XDF8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Probable V-type proton ATPase subunit H 1 {ECO:0000250|UniProtKB:Q20666};
DE            Short=V-ATPase subunit H 1 {ECO:0000250|UniProtKB:Q20666};
DE   AltName: Full=Vacuolar proton pump subunit H 1 {ECO:0000250|UniProtKB:Q20666};
GN   Name=vha-18 {ECO:0000312|EMBL:CAP30677.1};
GN   ORFNames=CBG11248 {ECO:0000312|WormBase:CBG11248};
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1] {ECO:0000312|EMBL:CAP30677.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16 {ECO:0000312|EMBL:CAP30677.1};
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: 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:0000255}.
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DR   EMBL; HE600908; CAP30677.1; -; Genomic_DNA.
DR   RefSeq; XP_002635048.1; XM_002635002.1.
DR   AlphaFoldDB; A8XDF8; -.
DR   SMR; A8XDF8; -.
DR   STRING; 6238.CBG11248; -.
DR   EnsemblMetazoa; CBG11248.1; CBG11248.1; WBGene00032402.
DR   GeneID; 8577043; -.
DR   KEGG; cbr:CBG_11248; -.
DR   CTD; 8577043; -.
DR   WormBase; CBG11248; CBP17155; WBGene00032402; Cbr-vha-18.
DR   eggNOG; KOG2759; Eukaryota.
DR   HOGENOM; CLU_025709_4_0_1; -.
DR   InParanoid; A8XDF8; -.
DR   OMA; RTHFQKE; -.
DR   OrthoDB; 751335at2759; -.
DR   Proteomes; UP000008549; Chromosome V.
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..451
FT                   /note="Probable V-type proton ATPase subunit H 1"
FT                   /id="PRO_0000370220"
SQ   SEQUENCE   451 AA;  52374 MW;  28D57B9533ACEBE2 CRC64;
     MVFGENQDLI RTHFQKEADK VRQMKTNWGL FTRSRMIAQS DYDFVVTYEQ AETEQDRSTV
     LSVFKEKAVY AFVHLMSQIS KDDYVRYTLT IIDDMLREDV SRTKIFEEVA VLLKRSPFSF
     FLGLLHRQDQ YIVHTTFSVL TKMAVFGNIK VTGDELDYFM GSLKEAITRG IANDYIATAV
     RCMQTLFRID PYRVSFVNIS GYESLSHALY STRKCGFQIQ YQIIFCMWLL TFNGHAAEVA
     LCGNLIQTIS TILGTSHKEK VIRIVLATLR NLIASNEDEY MKKQAARQMV QNQILVKLDH
     LENRKFQDVD LIDDMAFLQK ELKKVVEVLT SFEEYESELR HGALFWSPPH KCEIFWTENA
     HKLNDNRQEL LKMLITMLEK SNDPLVLCVA ANDIGEFVRY YPRGKMHVEQ LGGKEALMRL
     LTVPDPNVRY FALLAAQKLM VNHWKDLGLE I