ID   VATD_RABIT              Reviewed;         247 AA.
AC   O97755;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=V-type proton ATPase subunit D;
DE            Short=V-ATPase subunit D;
DE   AltName: Full=V-ATPase 28 kDa accessory protein;
DE   AltName: Full=Vacuolar proton pump subunit D;
GN   Name=ATP6V1D; Synonyms=ATP6M, VATD;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=New Zealand white; TISSUE=Osteoclast;
RA   Durrin L.K., Sakai D., Minkin C.;
RT   "The rabbit vacuolar proton-ATPase Subunit D: alternative splicing and high
RT   expression in osteoclasts.";
RL   Submitted (JAN-1996) 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; U45447; AAD10366.1; -; mRNA.
DR   RefSeq; NP_001075837.1; NM_001082368.1.
DR   AlphaFoldDB; O97755; -.
DR   SMR; O97755; -.
DR   STRING; 9986.ENSOCUP00000010335; -.
DR   GeneID; 100009221; -.
DR   KEGG; ocu:100009221; -.
DR   CTD; 51382; -.
DR   eggNOG; KOG1647; Eukaryota.
DR   InParanoid; O97755; -.
DR   OrthoDB; 1313938at2759; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR   GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005815; C:microtubule organizing center; 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_0000144234"
SQ   SEQUENCE   247 AA;  28253 MW;  CBBF2D24203781D7 CRC64;
     MSGKDRIEIF PSRMAQTIMK ARLKGAQTGR NLLKKKSDAL TLRFRQILKK IIETKMLMGE
     VMREAAFSLA EAKFTAGDFS TTAIQNVNKA QVKIRAKKDN VAGVTLPVFE HYHEGTDSYE
     LTGLARGGEQ LAKLKRNYAK AVELLVELAS LQTSFVTLDE AIKITNRRVN AIEHVIIPRI
     ERTLAYIITE LDEREREEFY RLKKIQEKKK ILKEKSEKDL EQRRAAGEVM EPANLLAEEK
     DEDLLFE