ID   A0A182V1J0_ANOME        Unreviewed;       550 AA.
AC   A0A182V1J0;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   22-FEB-2023, entry version 27.
DE   RecName: Full=ATPase V1 complex subunit H C-terminal domain-containing protein {ECO:0000259|Pfam:PF11698};
OS   Anopheles merus (Mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=30066 {ECO:0000313|EnsemblMetazoa:AMEM007312-PA, ECO:0000313|Proteomes:UP000075903};
RN   [1] {ECO:0000313|Proteomes:UP000075903}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAF {ECO:0000313|Proteomes:UP000075903};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles merus MAF (V2).";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AMEM007312-PA}
RP   IDENTIFICATION.
RC   STRAIN=MAF {ECO:0000313|EnsemblMetazoa:AMEM007312-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
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. {ECO:0000256|ARBA:ARBA00029425}.
CC   -!- SIMILARITY: Belongs to the V-ATPase H subunit family.
CC       {ECO:0000256|ARBA:ARBA00008613}.
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DR   AlphaFoldDB; A0A182V1J0; -.
DR   STRING; 30066.A0A182V1J0; -.
DR   EnsemblMetazoa; AMEM007312-RA; AMEM007312-PA; AMEM007312.
DR   VEuPathDB; VectorBase:AMEM007312; -.
DR   VEuPathDB; VectorBase:AMEM21_011612; -.
DR   OrthoDB; 176803at2759; -.
DR   Proteomes; UP000075903; Unassembled WGS sequence.
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; IPR000225; Armadillo.
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   SMART; SM00185; ARM; 3.
DR   SUPFAM; SSF48371; ARM repeat; 2.
PE   3: Inferred from homology;
KW   Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Transport {ECO:0000256|ARBA:ARBA00023065}.
FT   DOMAIN          410..525
FT                   /note="ATPase V1 complex subunit H C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11698"
FT   REGION          189..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        189..203
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   550 AA;  63421 MW;  7D69672DD5E5A155 CRC64;
     MTDVQDIMSS LPDDKIDMIA ATSVLQQQAG DIRQTKPNWS SYMQSQMISQ EDYACVSSLD
     KDKKAQAAYL QENAPQCAKT LLNMLSHVSK DQTIQYILVL IDDLLQEDRT RVQIFHDYAN
     KRKESVWAPF LNLLNRQDGF IVNMASRVVG KLACWGQEQM PKSDLHFYLQ WLKDQLTVAA
     QKLLHEMEEA EKKRQAEAAA SHHDHHRHGH HGHEAHHPPN SHQHQIAERY REISSAIDDP
     QRDRAKEDLH VTLTNNEYIQ SVGRCLQMML RVDEYRFAFV TVDGISTLIS ILSSRVNFQV
     QYQLVFCLWV LTFNPLLAEK MNKFNVIPIL ADILSDCAKE KVTRIILAVF RNLIEKPEDA
     QVAKEHCIAM VQCKVMKQLT ILEQRRFDDE DITGDVEFLT EKLQNSVQDL SSFDEYATEV
     KSARLEWSPV HKSAKFWREN AQRLNEKQYE LLRILVHLLE TSKDPLVLSV ASYDIGEYVR
     HYPRGKHVIE QLGGKQLVMQ LLAHEDPNVR YEALLAVQKL MVHNWEYLGK QLEKDSEKAT
     QGNAPISGKA
//