VA0D1_PONAB
ID VA0D1_PONAB Reviewed; 351 AA.
AC Q5R6I1;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=V-type proton ATPase subunit d 1;
DE Short=V-ATPase subunit d 1;
DE AltName: Full=Vacuolar proton pump subunit d 1;
GN Name=ATP6V0D1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Subunit of the V0 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). May play a
CC role in coupling of proton transport and ATP hydrolysis (By
CC similarity). In aerobic conditions, involved in intracellular iron
CC homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase
CC (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent
CC proteasomal degradation (By similarity). May play a role in cilium
CC biogenesis through regulation of the transport and the localization of
CC proteins to the cilium (By similarity). {ECO:0000250|UniProtKB:P51863,
CC ECO:0000250|UniProtKB:P61421, ECO:0000250|UniProtKB:Q6PGV1}.
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 (By similarity). The V1 complex consists of three catalytic
CC AB heterodimers that form a heterohexamer, three peripheral stalks each
CC consisting of EG heterodimers, one central rotor including subunits D
CC and F, and the regulatory subunits C and H (By similarity). The proton
CC translocation complex V0 consists of the proton transport subunit a, a
CC ring of proteolipid subunits c9c'', rotary subunit d, subunits e and f,
CC and the accessory subunits ATP6AP1/Ac45 and ATP6AP2/PRR (By
CC similarity). Interacts with ATP6AP2; ATP6AP2 is a V-ATPase accessory
CC protein and the interaction promotes v-ATPase complex assembly (By
CC similarity). Interacts with TMEM9; TMEM9 is a v-ATPase assembly
CC regulator and the interaction induces the interaction with ATP6AP2 (By
CC similarity). Interacts with PIP4P1 (By similarity).
CC {ECO:0000250|UniProtKB:P61421}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P61421};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:P61421}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:P61421}. Lysosome membrane
CC {ECO:0000250|UniProtKB:P61421}; Peripheral membrane protein
CC {ECO:0000305}. Cytoplasmic vesicle, clathrin-coated vesicle membrane
CC {ECO:0000250|UniProtKB:P61420}; Peripheral membrane protein
CC {ECO:0000305}. Note=Localizes to centrosome and the base of the cilium.
CC {ECO:0000250|UniProtKB:Q6PGV1}.
CC -!- SIMILARITY: Belongs to the V-ATPase V0D/AC39 subunit family.
CC {ECO:0000305}.
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DR EMBL; CR858860; CAH91060.1; -; mRNA.
DR EMBL; CR860508; CAH92631.1; -; mRNA.
DR RefSeq; NP_001126541.1; NM_001133069.1.
DR AlphaFoldDB; Q5R6I1; -.
DR SMR; Q5R6I1; -.
DR STRING; 9601.ENSPPYP00000008426; -.
DR Ensembl; ENSPPYT00000008768; ENSPPYP00000008425; ENSPPYG00000007458.
DR GeneID; 100173531; -.
DR KEGG; pon:100173531; -.
DR CTD; 9114; -.
DR eggNOG; KOG2957; Eukaryota.
DR GeneTree; ENSGT00390000002200; -.
DR InParanoid; Q5R6I1; -.
DR OrthoDB; 910004at2759; -.
DR Proteomes; UP000001595; Chromosome 16.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IEA:UniProt.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; ISS:UniProtKB.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0006879; P:cellular iron ion homeostasis; ISS:UniProtKB.
DR GO; GO:0036295; P:cellular response to increased oxygen levels; ISS:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR Gene3D; 1.10.132.50; -; 1.
DR Gene3D; 1.20.1690.10; -; 2.
DR InterPro; IPR036079; ATPase_su_c/d_sf.
DR InterPro; IPR002843; ATPase_V0-cplx_csu/dsu.
DR InterPro; IPR016727; ATPase_V0-cplx_dsu.
DR InterPro; IPR044911; V-type_ATPase_su_c/d_dom_3.
DR InterPro; IPR035067; V-type_ATPase_suC/d.
DR PANTHER; PTHR11028; PTHR11028; 1.
DR Pfam; PF01992; vATP-synt_AC39; 1.
DR PIRSF; PIRSF018497; V-ATP_synth_D; 1.
DR SUPFAM; SSF103486; SSF103486; 1.
PE 2: Evidence at transcript level;
KW Cilium biogenesis/degradation; Cytoplasmic vesicle; Hydrogen ion transport;
KW Ion transport; Lysosome; Membrane; Phosphoprotein; Reference proteome;
KW Transport.
FT CHAIN 1..351
FT /note="V-type proton ATPase subunit d 1"
FT /id="PRO_0000229766"
FT MOD_RES 270
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P51863"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51863"
SQ SEQUENCE 351 AA; 40329 MW; A720F8A87511203C CRC64;
MSFFPELYFN VDNGYLEGLV RGLKAGVLSQ ADYLNLVQCE TLEDLKLHLQ STDYGNFLAN
EASPLTVSVI DDRLKEKMVV EFRHMRNHAY EPLASFLDFI TYSYMIDNVI LLITGTLHQR
SIAELVPKCH PLGSFEQMEA VNIAQTPAEL YNAILVDTPL AAFFQDCISE QDLDEMNIEI
IRNTLYKAYL ESFYKFCTLL GGTTADAMCP ILEFEADRRA FIITINSFGT ELSKEDRAKL
FPHCGRLYPE GLAQLARADD YEQVKNVADY YPEYKLLFEG AGSNPGDKTL EDRFFEHEVK
LNKLAFLNQF HFGVFYAFVK LKEQECRNIV WIAECIAQRH RAKIDNYIPI F
