VA0D2_BOVIN
ID VA0D2_BOVIN Reviewed; 351 AA.
AC Q2KJB6;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=V-type proton ATPase subunit d 2;
DE Short=V-ATPase subunit d 2;
DE AltName: Full=Vacuolar proton pump subunit d 2;
GN Name=ATP6V0D2;
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 [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) 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). Regulator of osteoclast fusion and bone formation (By
CC similarity). {ECO:0000250|UniProtKB:P61420,
CC ECO:0000250|UniProtKB:Q80SY3}.
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). {ECO:0000250|UniProtKB:P61420}.
CC -!- SIMILARITY: Belongs to the V-ATPase V0D/AC39 subunit family.
CC {ECO:0000305}.
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DR EMBL; BC105425; AAI05426.1; -; mRNA.
DR RefSeq; NP_001039566.1; NM_001046101.1.
DR AlphaFoldDB; Q2KJB6; -.
DR SMR; Q2KJB6; -.
DR STRING; 9913.ENSBTAP00000028091; -.
DR PaxDb; Q2KJB6; -.
DR Ensembl; ENSBTAT00000028091; ENSBTAP00000028091; ENSBTAG00000021092.
DR GeneID; 511839; -.
DR KEGG; bta:511839; -.
DR CTD; 245972; -.
DR VEuPathDB; HostDB:ENSBTAG00000021092; -.
DR VGNC; VGNC:26313; ATP6V0D2.
DR eggNOG; KOG2957; Eukaryota.
DR GeneTree; ENSGT00390000002200; -.
DR HOGENOM; CLU_051277_0_0_1; -.
DR InParanoid; Q2KJB6; -.
DR OMA; FCKDHGD; -.
DR OrthoDB; 910004at2759; -.
DR TreeFam; TF300857; -.
DR Proteomes; UP000009136; Chromosome 14.
DR Bgee; ENSBTAG00000021092; Expressed in pigment epithelium of eye and 72 other tissues.
DR ExpressionAtlas; Q2KJB6; baseline and differential.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0033181; C:plasma membrane proton-transporting V-type ATPase complex; IBA:GO_Central.
DR GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IBA:GO_Central.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0007035; P:vacuolar acidification; IBA:GO_Central.
DR GO; GO:0007034; P:vacuolar transport; IBA:GO_Central.
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 Hydrogen ion transport; Ion transport; Reference proteome; Transport.
FT CHAIN 1..351
FT /note="V-type proton ATPase subunit d 2"
FT /id="PRO_0000285656"
SQ SEQUENCE 351 AA; 40497 MW; 8C5456CED8DBECCB CRC64;
MLESAELNFN ADHGYLEGLV RGCKAGLLTR RDYVNLVQCE NLEDLKIHLQ TTDYGNFLAN
QATPLTVSVI DTEMRKKLCR EFEYFRNHSL EPLSTFFTYM TCSYMIDNVI LLMNGALQNK
PVKDVLVKCH PLGHFTEMEA VNIAETPSDL FNAILVETPL APFFQDCTSE NALDELNIEI
LRNKLYKSYI EAFYKFCKNH GDVTAEVMCP ILEFEADRRA FIITLNSFGT ELSKEDRETL
YPTCGKLHPE GLRLLAQAED FEQMKRVADS YGVYKPLFEA VSDSSGGKTL EDVFYEREVQ
MNVLAFNRQF HYGVFYAYTK LKEQEMRNIV WIAECISQRQ RTKINSYIPI L