VA0D2_XENTR
ID VA0D2_XENTR Reviewed; 350 AA.
AC Q6P335;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
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 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2003) 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. V-ATPase is responsible for acidifying and maintaining the pH
CC of intracellular compartments and in some cell types, is targeted to
CC the plasma membrane, where it is responsible for acidifying the
CC extracellular environment (By similarity). May play a role in coupling
CC of proton transport and ATP hydrolysis (By similarity). Regulator of
CC osteoclast fusion and bone formation (By similarity).
CC {ECO:0000250|UniProtKB:P61421, 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. The V1 complex consists of three catalytic AB heterodimers
CC that form a heterohexamer, three peripheral stalks each consisting of
CC EG heterodimers, one central rotor including subunits D and F, and the
CC regulatory subunits C and H. The proton translocation complex V0
CC consists of the proton transport subunit a, a ring of proteolipid
CC subunits c9c'', rotary subunit d, subunits e and f, and two accessory
CC subunits. {ECO:0000250|UniProtKB:P61421}.
CC -!- SIMILARITY: Belongs to the V-ATPase V0D/AC39 subunit family.
CC {ECO:0000305}.
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DR EMBL; BC064198; AAH64198.1; -; mRNA.
DR RefSeq; NP_989362.1; NM_204031.1.
DR AlphaFoldDB; Q6P335; -.
DR SMR; Q6P335; -.
DR STRING; 8364.ENSXETP00000030056; -.
DR PaxDb; Q6P335; -.
DR Ensembl; ENSXETT00000030056; ENSXETP00000030056; ENSXETG00000013734.
DR GeneID; 394992; -.
DR KEGG; xtr:394992; -.
DR CTD; 245972; -.
DR Xenbase; XB-GENE-957143; atp6v0d2.
DR eggNOG; KOG2957; Eukaryota.
DR HOGENOM; CLU_051277_0_0_1; -.
DR InParanoid; Q6P335; -.
DR OrthoDB; 910004at2759; -.
DR PhylomeDB; Q6P335; -.
DR Reactome; R-XTR-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-XTR-77387; Insulin receptor recycling.
DR Reactome; R-XTR-917977; Transferrin endocytosis and recycling.
DR Reactome; R-XTR-9639288; Amino acids regulate mTORC1.
DR Reactome; R-XTR-983712; Ion channel transport.
DR Proteomes; UP000008143; Chromosome 6.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000013734; Expressed in mesonephros and 9 other tissues.
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..350
FT /note="V-type proton ATPase subunit d 2"
FT /id="PRO_0000285662"
SQ SEQUENCE 350 AA; 40575 MW; 56F7627A30AAEC80 CRC64;
MANTEFYFNV DSGYLEGLVR GFKGGILRST DYLNLAQCET LEDLKLHLQS TDYGSFLANE
TRQLTVSIID QRLKDKLMAE FHYFRNHAFE PLATFLDFIT YSYMIDNIIL LITGTLHQRP
ISELVPKCHP LGSFEQMEAV NIAQTPAELF NAIIVDTPLA DFFQDCLSEN DMDEMNIEIM
RNKLYKSYLE AFYKFCKKLG GTTEEIMCPI LEFEADRRAF VITINSFGTE LNKEEREKLY
PTCGRLFPEG LRMLGNADDQ DQVKTTAEYY AEYKALFEGV GIGTGEKTLE DKFFEHEVKM
NVLAFNNQFH FGVFYAYVKL KEQECRNIVW IAECISQRHR TKINNYIPIL