ID A0A2K5BZA6_AOTNA Unreviewed; 475 AA.
AC A0A2K5BZA6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=V-type proton ATPase subunit H {ECO:0000256|PIRNR:PIRNR032184};
GN Name=ATP6V1H {ECO:0000313|Ensembl:ENSANAP00000001786.1};
OS Aotus nancymaae (Ma's night monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000001786.1, ECO:0000313|Proteomes:UP000233020};
RN [1] {ECO:0000313|Ensembl:ENSANAP00000001786.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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. V-ATPase is responsible for acidifying and maintaining the pH
CC of intracellular compartments. {ECO:0000256|PIRNR:PIRNR032184}.
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. {ECO:0000256|PIRNR:PIRNR032184}.
CC -!- SIMILARITY: Belongs to the V-ATPase H subunit family.
CC {ECO:0000256|ARBA:ARBA00008613, ECO:0000256|PIRNR:PIRNR032184}.
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DR AlphaFoldDB; A0A2K5BZA6; -.
DR STRING; 37293.ENSANAP00000001786; -.
DR Ensembl; ENSANAT00000016038.1; ENSANAP00000001786.1; ENSANAG00000012840.1.
DR GeneTree; ENSGT00390000003289; -.
DR Proteomes; UP000233020; Unplaced.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:1902495; C:transmembrane transporter complex; IEA:Ensembl.
DR GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; IEA:UniProtKB-UniRule.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR GO; GO:0006897; P:endocytosis; IEA:Ensembl.
DR GO; GO:0097401; P:synaptic vesicle lumen acidification; IEA:Ensembl.
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 {ECO:0000256|ARBA:ARBA00022781,
KW ECO:0000256|PIRNR:PIRNR032184};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|PIRNR:PIRNR032184};
KW Reference proteome {ECO:0000313|Proteomes:UP000233020};
KW Transport {ECO:0000256|PIRNR:PIRNR032184}.
FT DOMAIN 348..463
FT /note="ATPase V1 complex subunit H C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11698"
SQ SEQUENCE 475 AA; 55152 MW; F3861528259C4CA3 CRC64;
MTKMDIRGAV DAAVPTNIIA AKAAEVRANK VNWQSYLQGQ MISAEDCEFI QRFEMKRSPE
EKQEMLQTEG SQCAKTFINL MTHISKEQTV QYILTMVDDM LQENHQRVSI FFDYARRSKN
TAWPYFLPML NRQDPFTVHM QELLPKLAAW GKELMEGSDL NYYFNWIKTQ LSSQKLRGSG
VAVETGTVSS NDSSQYVQCV AGCLQLMLRV NEYRFAWVEA DGVNCIMGVL SNKCGFQLQY
QMIFSIWLLA FSPQMCEHLR RYNIIPVLSD ILQESVKEKV TRIILAAFRN FLEKSTERET
RQEYALAMIQ CKVLKQLENL EQQKYDDEDI SEDIKFLLEK LGESVQDLSS FDEYSSELKS
GRLEWSPVHK SEKFWRENAV RLNEKNYELL KILTKLLEVS DDPQVLAVAA HDVGEYVRHY
PRGKRVIEQL GGKQLVMNHM HHEDQQVRYN ALLAVQKLMV HNWYALAFSH TCTLV
//