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 03-AUG-2022, entry version 97.
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}.
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; HE600983; CAP32720.3; -; Genomic_DNA.
DR RefSeq; XP_002644282.1; XM_002644236.1.
DR AlphaFoldDB; Q619W9; -.
DR SMR; Q619W9; -.
DR STRING; 6238.CBG14055; -.
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; KDQNVRY; -.
DR OrthoDB; 751335at2759; -.
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 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_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