ID A0A0R3NSN5_DROPS Unreviewed; 521 AA.
AC A0A0R3NSN5; A0A6I8V8C1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=V-type proton ATPase subunit H isoform X2 {ECO:0000313|RefSeq:XP_015035952.1};
GN Name=LOC4816883 {ECO:0000313|RefSeq:XP_015035952.1};
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245 {ECO:0000313|Proteomes:UP000001819, ECO:0000313|RefSeq:XP_015035952.1};
RN [1] {ECO:0000313|RefSeq:XP_015035952.1}
RP IDENTIFICATION.
RC STRAIN=MV2-25 {ECO:0000313|RefSeq:XP_015035952.1};
RC TISSUE=Whole body {ECO:0000313|RefSeq:XP_015035952.1};
RG RefSeq;
RL Submitted (NOV-2023) 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 RefSeq; XP_015035952.1; XM_015180466.2.
DR AlphaFoldDB; A0A0R3NSN5; -.
DR EnsemblMetazoa; FBtr0371124; FBpp0333388; FBgn0074492.
DR GeneID; 4816883; -.
DR Proteomes; UP000001819; Chromosome 4.
DR Bgee; FBgn0074492; Expressed in insect adult head and 2 other cell types or tissues.
DR ExpressionAtlas; A0A0R3NSN5; baseline.
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; 2.
PE 3: Inferred from homology;
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Reference proteome {ECO:0000313|Proteomes:UP000001819};
KW Transport {ECO:0000256|ARBA:ARBA00023065}.
FT DOMAIN 408..520
FT /note="ATPase V1 complex subunit H C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11698"
SQ SEQUENCE 521 AA; 59646 MW; 9325B74FC2E464BB CRC64;
MTTALYLPEE NIDMIAATSV LQQQAADIRT KTINWASYMQ SQMISEEDYR AISALDKSRA
AFLAQNSSQV VKTLLNLVSH LSKDSTIQYI LVLLDDLLQE DRSRVDLFHD TAGKLKQCIW
GPFLNLLNRQ DGFIVNMASR ILAKFACWGH ETMPKSDLNF YLQFLKDQLA SNSTSYLQEM
ALLAKRTQTI LVHTHGLHGN SKDHHGNQYS PSLAQLQHQH EQELVVSANE SYRQVPNSSE
QAHQQESKCA IPNNEYIQSV ARCLQMMLRV DEYRFAFVGV DGISTLIRIL STRVNFQVQY
QLIFCLWVLT FNPLLAAKMN KFSVIPILAD ILSDCAKEKV TRIILAVFRN LIEKPEDSSV
AKDHCIAMVQ CKVLKQLSIL EQRRFDDEDI TADVEYLSEK LQNSVQDLSS FDEYATEVRS
GRLEWSPVHK SAKFWRENAQ RLNEKNYELL RILVHLLETS KDAIILSVAC FDIGEYVRHY
PRGKHVLEQL GGKQIVMQHL GHEDPNVRYE ALLAVQKLMV L
//
