VATD_BOVIN
ID VATD_BOVIN Reviewed; 247 AA.
AC P39942;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 106.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 111-137, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Adrenal medulla;
RX PubMed=7831318; DOI=10.1073/pnas.92.2.497;
RA Nelson H., Mandiyan S., Nelson N.;
RT "A bovine cDNA and a yeast gene (VMA8) encoding the subunit D of the
RT vacuolar H(+)-ATPase.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:497-501(1995).
RN [2] {ECO:0007744|PDB:6XBW, ECO:0007744|PDB:6XBY}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.37 ANGSTROMS), FUNCTION, IDENTIFICATION
RP IN THE V-ATPASE COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND TISSUE SPECIFICITY.
RX PubMed=32764564; DOI=10.1038/s41467-020-17762-9;
RA Wang R., Long T., Hassan A., Wang J., Sun Y., Xie X.S., Li X.;
RT "Cryo-EM structures of intact V-ATPase from bovine brain.";
RL Nat. Commun. 11:3921-3921(2020).
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 (PubMed:32764564). 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 (PubMed:32764564). 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:Q9Y5K8, ECO:0000269|PubMed:32764564}.
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 (PubMed:32764564). The V1 complex consists of three
CC catalytic AB heterodimers that form a heterohexamer, three peripheral
CC stalks each consisting of EG heterodimers, one central rotor including
CC subunits D and F, and the regulatory subunits C and H
CC (PubMed:32764564). The proton translocation complex V0 consists of the
CC proton transport subunit a, a ring of proteolipid subunits c9c'',
CC rotary subunit d, subunits e and f, and the accessory subunits
CC ATP6AP1/Ac45 and ATP6AP2/PRR (PubMed:32764564). Interacts with SNX10
CC (By similarity). {ECO:0000250|UniProtKB:Q9Y5K8,
CC ECO:0000269|PubMed:32764564}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9Y5K8};
CC Peripheral membrane protein {ECO:0000305}; Cytoplasmic side
CC {ECO:0000305}. Cytoplasmic vesicle, clathrin-coated vesicle membrane
CC {ECO:0000269|PubMed:32764564}; Peripheral membrane protein
CC {ECO:0000305}. Cytoplasm, cytoskeleton, microtubule organizing center,
CC centrosome {ECO:0000250|UniProtKB:Q9Y5K8}. Cell projection, cilium
CC {ECO:0000250|UniProtKB:Q9Y5K8}. Note=Localizes to centrosome and the
CC base of the cilium. {ECO:0000250|UniProtKB:Q9Y5K8}.
CC -!- TISSUE SPECIFICITY: Expressed in brain (at protein level)
CC (PubMed:7831318, PubMed:32764564). Present in tissues active in
CC secretion (PubMed:7831318, PubMed:32764564). Amounts elevated in brain,
CC kidney and testis (PubMed:7831318, PubMed:32764564).
CC {ECO:0000269|PubMed:32764564, ECO:0000269|PubMed:7831318}.
CC -!- SIMILARITY: Belongs to the V-ATPase D subunit family. {ECO:0000305}.
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DR EMBL; U11927; AAC48458.1; -; mRNA.
DR PIR; A55910; A55910.
DR PDB; 6XBW; EM; 3.37 A; H=1-247.
DR PDB; 6XBY; EM; 3.79 A; H=1-247.
DR PDB; 7KHR; EM; 3.62 A; H=1-247.
DR PDBsum; 6XBW; -.
DR PDBsum; 6XBY; -.
DR PDBsum; 7KHR; -.
DR AlphaFoldDB; P39942; -.
DR SMR; P39942; -.
DR CORUM; P39942; -.
DR STRING; 9913.ENSBTAP00000021699; -.
DR PaxDb; P39942; -.
DR PRIDE; P39942; -.
DR eggNOG; KOG1647; Eukaryota.
DR InParanoid; P39942; -.
DR Proteomes; UP000009136; 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; IDA: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:0045851; P:pH reduction; IC:UniProtKB.
DR GO; GO:0061512; P:protein localization to cilium; ISS:UniProtKB.
DR GO; GO:1902600; P:proton transmembrane transport; IC: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 1: Evidence at protein level;
KW 3D-structure; Cell projection; Cilium biogenesis/degradation; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW Transport.
FT CHAIN 1..247
FT /note="V-type proton ATPase subunit D"
FT /id="PRO_0000144230"
FT HELIX 15..75
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 91..101
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 104..113
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:6XBW"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 134..174
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 177..215
FT /evidence="ECO:0007829|PDB:6XBW"
SQ SEQUENCE 247 AA; 28334 MW; 8E79C346B0C6651B CRC64;
MSGKDRIEIF PSRMAQTIMK ARLKGAQTGR NLLKKKSDAL TLRFRQILKK IIETKMLMGE
VMREAAFSLA EAKFTAGDFS TTVIQNVNKA QVKIRAKKDN VAGVTLPVFE HYHEGTDSYE
LTGLARGGEQ LAKLKRNYAK AVELLVELAS LQTSFVTLDE AIKITNRRVN RIEHVIIPRI
ERTLAYIITE LDEREREEFY RLKKIQEKKK ILKEKSDKDL EQRRAAGEVI EPANLLAEEK
DEDLLFE
