VA0D_DICDI
ID VA0D_DICDI Reviewed; 356 AA.
AC P54641; Q557C4; Q86AH9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 25-MAY-2022, entry version 133.
DE RecName: Full=V-type proton ATPase subunit d;
DE Short=V-ATPase subunit d;
DE AltName: Full=DVA41;
DE AltName: Full=V-ATPase 41 kDa accessory protein;
DE AltName: Full=Vacuolar proton pump subunit d;
GN Name=vatD-1; ORFNames=DDB_G0273071;
GN and
GN Name=vatD-2; ORFNames=DDB_G0273657;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=AX3;
RX PubMed=7929276; DOI=10.1016/s0021-9258(18)47307-3;
RA Temesvari L., Rodriguez-Paris J., Bush J., Steck T.L., Cardelli J.;
RT "Characterization of lysosomal membrane proteins of Dictyostelium
RT discoideum. A complex population of acidic integral membrane glycoproteins,
RT Rab GTP-binding proteins and vacuolar ATPase subunits.";
RL J. Biol. Chem. 269:25719-25727(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=AX2;
RX PubMed=16926386; DOI=10.1074/mcp.m600113-mcp200;
RA Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M.,
RA Soldati T.;
RT "Proteomics fingerprinting of phagosome maturation and evidence for the
RT role of a Galpha during uptake.";
RL Mol. Cell. Proteomics 5:2228-2243(2006).
CC -!- FUNCTION: Subunit of the integral membrane V0 complex of vacuolar
CC ATPase. Vacuolar ATPase is responsible for acidifying a variety of
CC intracellular compartments in eukaryotic cells, thus providing most of
CC the energy required for transport processes in the vacuolar system.
CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral
CC catalytic V1 complex (components A to H) attached to an integral
CC membrane V0 proton pore complex (components: a, c, c', c'' and d).
CC -!- SIMILARITY: Belongs to the V-ATPase V0D/AC39 subunit family.
CC {ECO:0000305}.
CC -!- CAUTION: The gene for this protein is duplicated in strains AX3 and
CC AX4. These strains contain a duplication of a segment of 750 kb of
CC chromosome 2 compared to the corresponding sequence in strain AX2.
CC {ECO:0000305}.
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DR EMBL; U13150; AAA64993.1; -; mRNA.
DR EMBL; AAFI02000011; EAL70519.1; -; Genomic_DNA.
DR EMBL; AAFI02000009; EAL70753.1; -; Genomic_DNA.
DR PIR; A55016; A55016.
DR RefSeq; XP_644445.1; XM_639353.1.
DR RefSeq; XP_644805.1; XM_639713.1.
DR AlphaFoldDB; P54641; -.
DR SMR; P54641; -.
DR STRING; 44689.DDB0185227; -.
DR PaxDb; P54641; -.
DR EnsemblProtists; EAL70519; EAL70519; DDB_G0273657.
DR EnsemblProtists; EAL70753; EAL70753; DDB_G0273071.
DR GeneID; 8618907; -.
DR GeneID; 8619070; -.
DR KEGG; ddi:DDB_G0273071; -.
DR KEGG; ddi:DDB_G0273657; -.
DR dictyBase; DDB_G0273071; vatD-1.
DR dictyBase; DDB_G0273657; vatD-2.
DR eggNOG; KOG2957; Eukaryota.
DR HOGENOM; CLU_051277_0_0_1; -.
DR InParanoid; P54641; -.
DR OMA; MLSRAED; -.
DR PhylomeDB; P54641; -.
DR Reactome; R-DDI-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-DDI-77387; Insulin receptor recycling.
DR Reactome; R-DDI-917977; Transferrin endocytosis and recycling.
DR Reactome; R-DDI-9639288; Amino acids regulate mTORC1.
DR PRO; PR:P54641; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0031164; C:contractile vacuolar membrane; TAS:dictyBase.
DR GO; GO:0032009; C:early phagosome; IDA:dictyBase.
DR GO; GO:0030139; C:endocytic vesicle; IDA:dictyBase.
DR GO; GO:0005765; C:lysosomal membrane; IDA:dictyBase.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
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 1: Evidence at protein level;
KW Hydrogen ion transport; Ion transport; Reference proteome; Transport.
FT CHAIN 1..356
FT /note="V-type proton ATPase subunit d"
FT /id="PRO_0000119352"
FT CONFLICT 184
FT /note="I -> N (in Ref. 1; AAA64993)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 356 AA; 40831 MW; 93BBF84DD624EEF6 CRC64;
MGLFGGRKHG GLFTFNKDDG YLEAILRGFK KGILSRADYN NLCQCDNLED MKMHFISTDY
GDFLAGEPSP IHTTTIAEKA TGKLVSEFNH IRNQAVEPLS TFMDFISYGY MIDNVVLLIT
GTLHERDISE LVDKCHPLGL FKSMATLSVV HNVADLYNNV LIDTPLAPYI QGCLSEEDLD
EMNIEIIRNT LYKAYLEDFY NYCKYLGGQT ELIMSDILKF EADRRSINIT INSFGATELS
KDDREKLYPS LGLLYPEGTS KLGKAEDVDQ VRGILEVYST YRNFFSDGVN NEKSLEDSFF
EHEVHLNRMA FEDQYGYGVF YAYIKLREQE IRNIVWIAEC ISQNMKQKMN QYIPIF