ID A0A1W4WVP6_AGRPL Unreviewed; 524 AA.
AC A0A1W4WVP6;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=V-type proton ATPase subunit H isoform X1 {ECO:0000313|RefSeq:XP_018324130.1};
GN Name=LOC108736268 {ECO:0000313|RefSeq:XP_018324130.1};
OS Agrilus planipennis (Emerald ash borer) (Agrilus marcopoli).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Elateriformia;
OC Buprestoidea; Buprestidae; Agrilinae; Agrilus.
OX NCBI_TaxID=224129 {ECO:0000313|Proteomes:UP000192223, ECO:0000313|RefSeq:XP_018324130.1};
RN [1] {ECO:0000313|RefSeq:XP_018324130.1}
RP IDENTIFICATION.
RC TISSUE=Entire body {ECO:0000313|RefSeq:XP_018324130.1};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_018324130.1; XM_018468628.2.
DR AlphaFoldDB; A0A1W4WVP6; -.
DR STRING; 224129.A0A1W4WVP6; -.
DR EnsemblMetazoa; XM_018468628.2; XP_018324130.1; LOC108736268.
DR GeneID; 108736268; -.
DR KEGG; apln:108736268; -.
DR InParanoid; A0A1W4WVP6; -.
DR OrthoDB; 176803at2759; -.
DR Proteomes; UP000192223; Unplaced.
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 PIRSF; PIRSF032184; ATPase_V1_H; 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 Reference proteome {ECO:0000313|Proteomes:UP000192223};
KW Transport {ECO:0000256|ARBA:ARBA00023065}.
FT DOMAIN 384..498
FT /note="ATPase V1 complex subunit H C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11698"
SQ SEQUENCE 524 AA; 60687 MW; CBD2E7E9DAA8112A CRC64;
MAQVADDPKI KEIITSLDDD KIDMLAATSV LQQQATDIRN QKINWQSYFQ SQMISQEDYK
FIVAFDVQDH AQREKLLRTE RLQCAKTFLS LIGHVSKDQT LQYILVLIDD MLQEDRSRVE
IFHEYANINK ESVWHPFLNL LNRQDGFITN MTARIIAKIA CWSQTPMERS DLHFYLTWLK
DQLKSQYEAL RTSQAVADSL KGHGGEQPTE VYHEIGFDQD NTYHIDITNN EYIQSVGRCL
QMMLRIDEYR FAFISVDGIS TLLSVLSGRV NFQVQYQLIF CLWVLTFNPL LAEKMNKFNV
IPILADILSD SVKEKVTRII LAVFRNLIEK PEDGQVAKEH CIAMVQCKVL KHLTILEQRK
FDDEDITADV EFLIEKLQSS VHDLSSFDEY ATEVKSGRLE WSPVHKSKFW RENAERLNEK
NYELLRILIH LLETSKDPLV LSVACFDIGE YVRHYPRGKH VIEQLGGKQL VMQLLAHEDP
NVRYEALLAV QKLMVHNWEY LGRQLEKETG GEVKPSSGVI SGKA
//
