VA0D2_RAT
ID VA0D2_RAT Reviewed; 350 AA.
AC Q5FVL0;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=16192400; DOI=10.1095/biolreprod.105.043752;
RA Pietrement C., Sun-Wada G.H., Silva N.D., McKee M., Marshansky V.,
RA Brown D., Futai M., Breton S.;
RT "Distinct expression patterns of different subunit isoforms of the V-ATPase
RT in the rat epididymis.";
RL Biol. Reprod. 74:185-194(2006).
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 -!- TISSUE SPECIFICITY: Epididymis and vas deferens.
CC {ECO:0000269|PubMed:16192400}.
CC -!- SIMILARITY: Belongs to the V-ATPase V0D/AC39 subunit family.
CC {ECO:0000305}.
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DR EMBL; BC089917; AAH89917.1; -; mRNA.
DR RefSeq; NP_001011972.1; NM_001011972.1.
DR AlphaFoldDB; Q5FVL0; -.
DR SMR; Q5FVL0; -.
DR STRING; 10116.ENSRNOP00000009334; -.
DR PaxDb; Q5FVL0; -.
DR PRIDE; Q5FVL0; -.
DR Ensembl; ENSRNOT00000009334; ENSRNOP00000009334; ENSRNOG00000006926.
DR GeneID; 297932; -.
DR KEGG; rno:297932; -.
DR UCSC; RGD:1306900; rat.
DR CTD; 245972; -.
DR RGD; 1306900; Atp6v0d2.
DR eggNOG; KOG2957; Eukaryota.
DR GeneTree; ENSGT00390000002200; -.
DR HOGENOM; CLU_051277_0_0_1; -.
DR InParanoid; Q5FVL0; -.
DR OMA; FCKDHGD; -.
DR OrthoDB; 910004at2759; -.
DR PhylomeDB; Q5FVL0; -.
DR TreeFam; TF300857; -.
DR Reactome; R-RNO-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-RNO-77387; Insulin receptor recycling.
DR Reactome; R-RNO-917977; Transferrin endocytosis and recycling.
DR Reactome; R-RNO-9639288; Amino acids regulate mTORC1.
DR Reactome; R-RNO-983712; Ion channel transport.
DR PRO; PR:Q5FVL0; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000006926; Expressed in kidney and 7 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0005769; C:early endosome; ISO:RGD.
DR GO; GO:0005768; C:endosome; IDA:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
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; ISO:RGD.
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..350
FT /note="V-type proton ATPase subunit d 2"
FT /id="PRO_0000285660"
SQ SEQUENCE 350 AA; 40520 MW; 3B1E7969788BC6FA CRC64;
MLETAELYFN VDHGYLEGLV RGCKASLLTQ QDYVNLVQCE TLEDLKIHLQ TTDYGNFLAH
ETNPLTVSKI DTEMRKKLCR EFDYFRNHSL EPLSTFFTYM TCSYMIDNII LLMNGALQKK
SVKEVLAKCH PLGRFTEMEA VNIAESASEL FKAVLVETPL APFFQDCMSE NTLDELNIEL
LRNKLYKSYL EAFYKFCKDH GDVTAEVMCP ILEFEADRRA LIITLNSFGT ELSKEDRETL
FPTCGKLYPE GLRLLAQAED FEHMKRVADN YGVYKPLFDA VGGSGGKTLE DVFYEREVQM
NVLAFNRQFH YGVFYAYVKL KEQEMRNIVW IAECISQRHR TKINSYIPIL
