ID   A0A182LU55_9DIPT        Unreviewed;       571 AA.
AC   A0A182LU55;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   22-FEB-2023, entry version 29.
DE   RecName: Full=ATPase V1 complex subunit H C-terminal domain-containing protein {ECO:0000259|Pfam:PF11698};
OS   Anopheles culicifacies.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles; culicifacies species complex.
OX   NCBI_TaxID=139723 {ECO:0000313|EnsemblMetazoa:ACUA002036-PA, ECO:0000313|Proteomes:UP000075883};
RN   [1] {ECO:0000313|Proteomes:UP000075883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A-37 {ECO:0000313|Proteomes:UP000075883};
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 culicifacies species A.";
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:ACUA002036-PA}
RP   IDENTIFICATION.
RC   STRAIN=A-37 {ECO:0000313|EnsemblMetazoa:ACUA002036-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   EMBL; AXCM01000440; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A182LU55; -.
DR   STRING; 139723.A0A182LU55; -.
DR   EnsemblMetazoa; ACUA002036-RA; ACUA002036-PA; ACUA002036.
DR   VEuPathDB; VectorBase:ACUA002036; -.
DR   OrthoDB; 176803at2759; -.
DR   Proteomes; UP000075883; 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          431..546
FT                   /note="ATPase V1 complex subunit H C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11698"
FT   REGION          194..226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        205..220
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   571 AA;  65774 MW;  806A5BB8BB0E13BC CRC64;
     MTDVQDIMSS LPDDKIDMIA ATSVLQQQAG DIRQNKPNWY SYMQSQMISQ EDYACVSSLD
     KDKKAQAQYL QENASQCAKT LLNMLSHVSK DQTIQYILVL IDDLLQEDRG RVQIFHDYAT
     KKKESVWAPF LNLLNRQDGF IVNMASRVVG KLACWGQEQM PKSDLHFYLQ WLKDQLTVAA
     QKLLHEMEEA EKKRLAEAAA SHHGHHGHGH QSHHGEAHHP NSHHHQIAER YREISSAIDD
     PQRGSSKEDL HSIFVTIDYF YILTILIDLI PVCFKNNEYI QSVARCLQMM LRVDEYRFAF
     VTVDGISTLI SILSSRVNFQ VQYQLVFCLW VLTFNPLLAE KMNKFNVIPI LADILSDCAK
     EKVTRIILAV FRNLIEKPED SQVAKEHCIA MVQCKVMKQL TILEQRRFDD EDITGDVEFL
     TEKLQNSVQD LSSFDEYATE VKSARLEWSP VHKSAKFWRE NAQRLNEKQY ELLRILVHLL
     ETSKDPLVLS VASYDIGEYV RHYPRGKHVI EQLGGKQLVM QLLAHEDPNV RYEALLAVQK
     LMVHNWEYLG KQLEKENEKA PQGSAPISGK A
//