ID   VA0D2_PONAB             Reviewed;         350 AA.
AC   Q5R7B7;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   03-AUG-2022, entry version 61.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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 the accessory
CC       subunits ATP6AP1/Ac45 and ATP6AP2/PRR. {ECO:0000250|UniProtKB:P61421}.
CC   -!- SIMILARITY: Belongs to the V-ATPase V0D/AC39 subunit family.
CC       {ECO:0000305}.
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DR   EMBL; CR860201; CAH92343.1; ALT_TERM; mRNA.
DR   RefSeq; NP_001126378.1; NM_001132906.2.
DR   AlphaFoldDB; Q5R7B7; -.
DR   SMR; Q5R7B7; -.
DR   STRING; 9601.ENSPPYP00000020999; -.
DR   GeneID; 100173359; -.
DR   KEGG; pon:100173359; -.
DR   CTD; 245972; -.
DR   eggNOG; KOG2957; Eukaryota.
DR   InParanoid; Q5R7B7; -.
DR   OrthoDB; 910004at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005768; C:endosome; IEA:UniProt.
DR   GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
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_0000285659"
SQ   SEQUENCE   350 AA;  40372 MW;  407E6CB30DFA5B02 CRC64;
     MLEGAELYFN VDHGYLEGLV RGCKASLLTQ QDYINLVQCE TLEDLKIHLQ TTDYGNFLAN
     QTNPLTVSKI DTEMRKRLCG EFEYFRNHSL EPLSTFLTYM TCSYMIDNVI PLMNGALQKK
     SVKEILGKCH PLGRFTEMEA VNIAETPSDL FNAILIETPL APFFQDCMSE NALNELNIEL
     LRNKLYKSYL EAFYKFCKNH GDVTAEVMCP ILEFEADRRA FIITLNSFGT ELSKEDRETL
     YPTFGKLYPE GLRLLAQAED FDQMKNVADH YGVYKPLFEA VGGSGGKTLE DVFYEREVQM
     NVLAFNRQFH YGVFYAYVKL KEQEIRNIAW IAECISQRHR TKINSYIPIL