ID   VA0D2_CHICK             Reviewed;         351 AA.
AC   Q5ZHL0;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 109.
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; ORFNames=RCJMB04_37b12;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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; AJ721124; CAG32783.1; -; mRNA.
DR   RefSeq; NP_001008455.1; NM_001008455.1.
DR   AlphaFoldDB; Q5ZHL0; -.
DR   SMR; Q5ZHL0; -.
DR   STRING; 9031.ENSGALP00000025533; -.
DR   PaxDb; Q5ZHL0; -.
DR   Ensembl; ENSGALT00000055741; ENSGALP00000052021; ENSGALG00000034294.
DR   GeneID; 420210; -.
DR   KEGG; gga:420210; -.
DR   CTD; 245972; -.
DR   VEuPathDB; HostDB:geneid_420210; -.
DR   eggNOG; KOG2957; Eukaryota.
DR   GeneTree; ENSGT00390000002200; -.
DR   HOGENOM; CLU_051277_0_0_1; -.
DR   InParanoid; Q5ZHL0; -.
DR   OMA; ADFFQDC; -.
DR   OrthoDB; 910004at2759; -.
DR   PhylomeDB; Q5ZHL0; -.
DR   TreeFam; TF300857; -.
DR   Reactome; R-GGA-1222556; ROS and RNS production in phagocytes.
DR   Reactome; R-GGA-77387; Insulin receptor recycling.
DR   Reactome; R-GGA-917977; Transferrin endocytosis and recycling.
DR   Reactome; R-GGA-9639288; Amino acids regulate mTORC1.
DR   PRO; PR:Q5ZHL0; -.
DR   Proteomes; UP000000539; Chromosome 2.
DR   Bgee; ENSGALG00000034294; Expressed in colon and 7 other tissues.
DR   ExpressionAtlas; Q5ZHL0; baseline and differential.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
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_0000285661"
SQ   SEQUENCE   351 AA;  40400 MW;  D9E864046A0412DE CRC64;
     MPGYSEFYFN VDHGYLEGLV RGFKAGILTS ADYVNLAQCE TLEDLKLHLQ TTDYGNFLAN
     ESGPLTISTI DDKLKTKLLT EFHYFRNHAF EPLTTFLNFI TYSYMIDNII LLITGTLHQR
     PIAELVPKCH PLGSFEQMEA VSIASNPTEL FNAILVDTPL AAFFQDCLSE NDLDEMNVEI
     MRNKLYKSYL EAFYKFCEKQ GGTTAEIMKP ILEFEADRRA FIITINSFGT ELSKEDREKL
     YPTCGKLYPE GLHLLANADD YEQVKCVADY YAEYKAVFEG VGNDSGEKTL EDAFFEHEIK
     LNVLAFNNQF HFGVFYAYIK LKEQECRNIV WIAECISQRH RTKINNYIPI F