ID A0A369JJI3_HYPMA Unreviewed; 470 AA.
AC A0A369JJI3;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 28-JUN-2023, entry version 11.
DE RecName: Full=V-type proton ATPase subunit H {ECO:0000256|PIRNR:PIRNR032184};
GN Name=Atp6v1h {ECO:0000313|EMBL:RDB21360.1};
GN ORFNames=Hypma_011388 {ECO:0000313|EMBL:RDB21360.1};
OS Hypsizygus marmoreus (White beech mushroom) (Agaricus marmoreus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Tricholomatineae; Lyophyllaceae; Hypsizygus.
OX NCBI_TaxID=39966 {ECO:0000313|EMBL:RDB21360.1, ECO:0000313|Proteomes:UP000076154};
RN [1] {ECO:0000313|EMBL:RDB21360.1, ECO:0000313|Proteomes:UP000076154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=51987-8 {ECO:0000313|EMBL:RDB21360.1,
RC ECO:0000313|Proteomes:UP000076154};
RA Choi I.-G., Min B., Kim J.-G., Kim S., Oh Y.-L., Kong W.-S., Park H.,
RA Jeong J., Song E.-S.;
RT "Whole genome sequencing of Hypsizygus marmoreus.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RDB21360.1}.
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DR EMBL; LUEZ02000055; RDB21360.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369JJI3; -.
DR STRING; 39966.A0A369JJI3; -.
DR InParanoid; A0A369JJI3; -.
DR Proteomes; UP000076154; Unassembled WGS sequence.
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 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:UP000076154};
KW Transport {ECO:0000256|PIRNR:PIRNR032184}.
FT DOMAIN 319..417
FT /note="ATPase V1 complex subunit H C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11698"
SQ SEQUENCE 470 AA; 53164 MW; 045853E13F036879 CRC64;
MSVSLVSNAY LDEHSSKIRA KPVPWEGYQR ADLITAEELT LIKKVDKQPR ARVESILLSD
GPTYALLYLR LLKKLQRVDT MQCILVLIAD ALADHDERIP VFLRTVESDP DLPFYPLLRT
LDTQDEFVQL KAAQILTVIL SSQSTPLPSQ HLKPFLDTLA ALVQGPSQNK RDVAVQCLES
LLARRECRQA IWAVPGIIAG FLEILKHKPG PQMSYQVAFC FWLLSFEQNV AEELNKKYDV
IPLLIDIAQG AVKEKVIRVI VATFRNLVTK APTANLPAML VAQLLPFAKN LCTRKWQDED
ILEDVQFLRD ELNTNFQSLT NYDEYTSELA SGHLSWTPVH ESDDFWKANA AKLNDNDGEQ
LKILLRLLKE SADPLVLAVA AHDVGQYVKH CDKGKKLVTE HGGKARVMQL MTHEDADFNG
FYLIRCRTAP PMNTYSPDIT LLATTSTSTA TSNPYDSLRR WATKYYMHHH
//