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Database: UniProt
Entry: VATH2_CAEBR
LinkDB: VATH2_CAEBR
Original site: VATH2_CAEBR 
ID   VATH2_CAEBR             Reviewed;         470 AA.
AC   Q619W9; A8XJ95;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   24-JAN-2024, entry version 101.
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:0000250|UniProtKB:Q22494};
GN   ORFNames=CBG14055 {ECO:0000312|WormBase:CBG14055};
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: 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; HE600983; CAP32720.3; -; Genomic_DNA.
DR   RefSeq; XP_002644282.1; XM_002644236.1.
DR   AlphaFoldDB; Q619W9; -.
DR   SMR; Q619W9; -.
DR   STRING; 6238.Q619W9; -.
DR   EnsemblMetazoa; CBG14055.1; CBG14055.1; WBGene00034689.
DR   GeneID; 8586277; -.
DR   KEGG; cbr:CBG_14055; -.
DR   CTD; 8586277; -.
DR   WormBase; CBG14055; CBP03456; WBGene00034689; Cbr-vha-15.
DR   eggNOG; KOG2759; Eukaryota.
DR   HOGENOM; CLU_025709_2_0_1; -.
DR   InParanoid; Q619W9; -.
DR   OMA; DMLQEDK; -.
DR   OrthoDB; 176803at2759; -.
DR   Proteomes; UP000008549; Chromosome X.
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   CDD; cd00256; VATPase_H; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   Gene3D; 1.25.40.150; V-type ATPase, subunit H, C-terminal domain; 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; V-TYPE PROTON ATPASE SUBUNIT H; 1.
DR   PANTHER; PTHR10698:SF0; V-TYPE PROTON ATPASE SUBUNIT H; 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; ARM repeat; 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_0000279720"
SQ   SEQUENCE   470 AA;  53898 MW;  ED0247A7BC1DC312 CRC64;
     MAEVAHHNIP AVDMINATSR LQLEAAEVRS NKPNWGSYFR SKMIQEDDYT LVTSYENAKS
     KDERDQVIAA NDANGQLAKT MANLITQVAK DQNVRYVLTL FDDMLQEDKS RVEIFHKAAH
     RQKRTAFSQY LGILQRQDNF IVNQMSSIIA KLACFGVTRM EGQDLQYYFS FLKEQLKNST
     TNEYMNTTAR CLQMMLRHDE YRHEFVVTDG VQTLVTALNG KTNFQLQYQL IFSVWCLTFN
     ADIAKKTPSL GVITALGDIL SESTKEKVIR IILASFVNIL NKVEEREIKR EAALQMVQCK
     TLKTLELMDA KKYDDPDLED DVKFLTEELT LSVHDLSSYD EYYSEVRSGR LTWSPVHKSE
     KFWRENAAKF NDKQYEVVKI LIKLLESSSD PLILCVASHD IGEYVRHYPR GKTVVEQQQG
     KAAVMRLLTA EDPNVRYHAL LAVQKLMVHN WEYLGKQLDS DAQGDGVAAK
//
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