VATL_DICDI
ID VATL_DICDI Reviewed; 196 AA.
AC P54642; Q554K4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 144.
DE RecName: Full=V-type proton ATPase proteolipid subunit;
DE Short=V-ATPase 16 kDa proteolipid subunit;
DE AltName: Full=Vacuolar proton pump 16 kDa proteolipid subunit;
GN Name=vatP; ORFNames=DDB_G0274381;
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=AX2;
RX PubMed=8838672; DOI=10.1242/jcs.109.2.489;
RA Xie Y., Coukell M.B., Gombos Z.;
RT "Antisense RNA inhibition of the putative vacuolar H(+)-ATPase proteolipid
RT of Dictyostelium reduces intracellular Ca2+ transport and cell viability.";
RL J. Cell Sci. 109:489-497(1996).
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).
CC -!- FUNCTION: Proton-conducting pore forming subunit of the membrane
CC integral V0 complex of vacuolar ATPase. V-ATPase is responsible for
CC acidifying a variety of intracellular compartments in eukaryotic cells.
CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral
CC catalytic V1 complex (main components: subunits A, B, C, D, E, and F)
CC attached to an integral membrane V0 proton pore complex (main
CC component: the proteolipid protein; which is present as a hexamer that
CC forms the proton-conducting pore).
CC -!- SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein.
CC -!- DEVELOPMENTAL STAGE: Expression is maintained at a relatively constant
CC level during growth and development.
CC -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC {ECO:0000305}.
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DR EMBL; X90516; CAA62102.1; -; mRNA.
DR EMBL; AAFI02000012; EAL70083.1; -; Genomic_DNA.
DR PIR; S58350; S58350.
DR RefSeq; XP_644319.1; XM_639227.1.
DR AlphaFoldDB; P54642; -.
DR SMR; P54642; -.
DR STRING; 44689.DDB0185071; -.
DR PaxDb; P54642; -.
DR EnsemblProtists; EAL70083; EAL70083; DDB_G0274381.
DR GeneID; 8619747; -.
DR KEGG; ddi:DDB_G0274381; -.
DR dictyBase; DDB_G0274381; vatP.
DR eggNOG; KOG0232; Eukaryota.
DR HOGENOM; CLU_085752_1_1_1; -.
DR InParanoid; P54642; -.
DR OMA; NFIQLGA; -.
DR PhylomeDB; P54642; -.
DR Reactome; R-DDI-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
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:P54642; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0031164; C:contractile vacuolar membrane; IDA:dictyBase.
DR GO; GO:0016021; C:integral component of membrane; 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; IDA:dictyBase.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0019954; P:asexual reproduction; IMP:dictyBase.
DR GO; GO:0006816; P:calcium ion transport; IDA:dictyBase.
DR GO; GO:0030587; P:sorocarp development; IMP:dictyBase.
DR Gene3D; 1.20.120.610; -; 1.
DR InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR InterPro; IPR000245; ATPase_proteolipid_csu.
DR InterPro; IPR011555; ATPase_proteolipid_su_C_euk.
DR InterPro; IPR035921; F/V-ATP_Csub_sf.
DR Pfam; PF00137; ATP-synt_C; 2.
DR PRINTS; PR00122; VACATPASE.
DR SUPFAM; SSF81333; SSF81333; 1.
DR TIGRFAMs; TIGR01100; V_ATP_synt_C; 1.
PE 2: Evidence at transcript level;
KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..196
FT /note="V-type proton ATPase proteolipid subunit"
FT /id="PRO_0000071748"
FT TOPO_DOM 1..25
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 47..72
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..111
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..150
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 172..196
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT SITE 158
FT /note="Essential for proton translocation"
FT /evidence="ECO:0000250"
SQ SEQUENCE 196 AA; 20149 MW; D0FE9438C2F788AB CRC64;
MFQLLSFLLS GEATAVERII TDACPVYAPF FGAMGVTAAL VFTVMGAAYG TAKASVGISN
MGVMKPDLVI KAFIPVIFAG VIAIYGLIIC VILVGGIKPN ANYTLMKSFT DLGAGLTVGL
CGLAAGMAIG IVGDSGVRAF GQQPKLYVIM MLILIFSEAL GLYGLIIGIL LSSVSDTYCP
GQALVPLNSG NVIGKN
