ID   VATD_PONAB              Reviewed;         247 AA.
AC   Q5RCS8;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=V-type proton ATPase subunit D;
DE            Short=V-ATPase subunit D;
DE   AltName: Full=Vacuolar proton pump subunit D;
GN   Name=ATP6V1D;
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=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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 (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 cilium biogenesis through regulation of the transport and the
CC       localization of proteins to the cilium (By similarity).
CC       {ECO:0000250|UniProtKB:P39942, ECO:0000250|UniProtKB:Q9Y5K8}.
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 SNX10 (By similarity).
CC       {ECO:0000250|UniProtKB:Q9Y5K8}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9Y5K8};
CC       Peripheral membrane protein {ECO:0000250|UniProtKB:Q9Y5K8}; Cytoplasmic
CC       side {ECO:0000250|UniProtKB:Q9Y5K8}. Cytoplasmic vesicle, clathrin-
CC       coated vesicle membrane {ECO:0000250|UniProtKB:P39942}; Peripheral
CC       membrane protein {ECO:0000305}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome {ECO:0000250|UniProtKB:Q9Y5K8}. Cell
CC       projection, cilium {ECO:0000250|UniProtKB:Q9Y5K8}. Note=Localizes to
CC       centrosome and the base of the cilium. {ECO:0000250|UniProtKB:Q9Y5K8}.
CC   -!- SIMILARITY: Belongs to the V-ATPase D subunit family. {ECO:0000305}.
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DR   EMBL; CR858190; CAH90429.1; -; mRNA.
DR   RefSeq; NP_001125215.1; NM_001131743.1.
DR   AlphaFoldDB; Q5RCS8; -.
DR   SMR; Q5RCS8; -.
DR   STRING; 9601.ENSPPYP00000006728; -.
DR   Ensembl; ENSPPYT00000006993; ENSPPYP00000006728; ENSPPYG00000005920.
DR   GeneID; 100172107; -.
DR   KEGG; pon:100172107; -.
DR   CTD; 51382; -.
DR   eggNOG; KOG1647; Eukaryota.
DR   GeneTree; ENSGT00390000010770; -.
DR   HOGENOM; CLU_069688_0_0_1; -.
DR   InParanoid; Q5RCS8; -.
DR   OMA; SKNIMGV; -.
DR   OrthoDB; 1313938at2759; -.
DR   TreeFam; TF300160; -.
DR   Proteomes; UP000001595; Chromosome 14.
DR   GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR   GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR   GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; ISS:UniProtKB.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR   GO; GO:0061512; P:protein localization to cilium; ISS:UniProtKB.
DR   InterPro; IPR002699; V_ATPase_D.
DR   PANTHER; PTHR11671; PTHR11671; 1.
DR   Pfam; PF01813; ATP-synt_D; 1.
DR   TIGRFAMs; TIGR00309; V_ATPase_subD; 1.
PE   2: Evidence at transcript level;
KW   Cell projection; Cilium biogenesis/degradation; Cytoplasm;
KW   Cytoplasmic vesicle; Cytoskeleton; Hydrogen ion transport; Ion transport;
KW   Membrane; Reference proteome; Transport.
FT   CHAIN           1..247
FT                   /note="V-type proton ATPase subunit D"
FT                   /id="PRO_0000144233"
SQ   SEQUENCE   247 AA;  28263 MW;  4185E5F6A74EFB1C CRC64;
     MSGKDRIEIF PSRMAQTIMK ARLKGAQTGR NLLKKKSDAL TLRFRQILKK IIETKMLMGE
     VMREAAFSLA EAKFTAGDFS TTVIQNVNKA QVKIRAKKDN VAGVTLPVFE HYHEGTDSYE
     LTGLARGGEQ LAKLKRNYAK AVELLVELAS LQTSFVTLDE AIKITNRRVN AIEHVIIPRI
     ERTLAYIITE LDEREREEFY RLKKIQEKKK ILKEKSEKDL EQRRAAGEVL EPANLLAEEK
     DEDLLFE