VATM_DICDI
ID VATM_DICDI Reviewed; 815 AA.
AC Q54E04; Q23860;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 2.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Vacuolar proton translocating ATPase 100 kDa subunit;
DE AltName: Full=Clathrin-coated vesicle/synaptic vesicle proton pump 100 kDa subunit;
DE AltName: Full=Vacuolar ATPase transmembrane subunit;
GN Name=vatM; ORFNames=DDB_G0291858;
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], AND SUBCELLULAR LOCATION.
RX PubMed=8743951; DOI=10.1242/jcs.109.5.1041;
RA Liu T., Clarke M.;
RT "The vacuolar proton pump of Dictyostelium discoideum: molecular cloning
RT and analysis of the 100 kDa subunit.";
RL J. Cell Sci. 109:1041-1051(1996).
RN [2]
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 [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11956322; DOI=10.1242/jcs.115.9.1907;
RA Liu T., Mirschberger C., Chooback L., Arana Q., Dal Sacco Z.,
RA MacWilliams H., Clarke M.;
RT "Altered expression of the 100 kDa subunit of the Dictyostelium vacuolar
RT proton pump impairs enzyme assembly, endocytic function and cytosolic pH
RT regulation.";
RL J. Cell Sci. 115:1907-1918(2002).
RN [4]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=12082150; DOI=10.1242/jcs.115.14.2893;
RA Clarke M., Koehler J., Arana Q., Liu T., Heuser J., Gerisch G.;
RT "Dynamics of the vacuolar H(+)-ATPase in the contractile vacuole complex
RT and the endosomal pathway of Dictyostelium cells.";
RL J. Cell Sci. 115:2893-2905(2002).
RN [5]
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: Essential component of the vacuolar proton pump (V-ATPase), a
CC multimeric enzyme that catalyzes the translocation of protons across
CC the membranes. Required for assembly and activity of the V-ATPase.
CC Required in both the contractile vacuole system and the
CC endosomal/lysosomal system. Also required for cytosolic pH regulation.
CC {ECO:0000269|PubMed:11956322}.
CC -!- SUBUNIT: The V-ATPase is a heteromultimeric enzyme. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Multi-pass membrane
CC protein. Endosome membrane; Multi-pass membrane protein. Vacuole
CC membrane; Multi-pass membrane protein. Lysosome membrane; Multi-pass
CC membrane protein. Note=Found in membrane of contractile vacuole
CC complex, an osmoregulatory organelle.
CC -!- DISRUPTION PHENOTYPE: Cells show defects in V-ATPase enzyme assembly,
CC endocytic function and cytosolic pH regulation.
CC {ECO:0000269|PubMed:11956322}.
CC -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAL61459.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U38803; AAB49621.1; -; mRNA.
DR EMBL; AAFI02000186; EAL61459.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_629892.1; XM_629890.1.
DR AlphaFoldDB; Q54E04; -.
DR SMR; Q54E04; -.
DR STRING; 44689.DDB0216215; -.
DR PaxDb; Q54E04; -.
DR PRIDE; Q54E04; -.
DR EnsemblProtists; EAL61459; EAL61459; DDB_G0291858.
DR GeneID; 8628392; -.
DR KEGG; ddi:DDB_G0291858; -.
DR dictyBase; DDB_G0291858; vatM.
DR eggNOG; KOG2189; Eukaryota.
DR InParanoid; Q54E04; -.
DR PhylomeDB; Q54E04; -.
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:Q54E04; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0031164; C:contractile vacuolar membrane; IDA:dictyBase.
DR GO; GO:0032009; C:early phagosome; IDA:dictyBase.
DR GO; GO:0030139; C:endocytic vesicle; IDA:dictyBase.
DR GO; GO:0010008; C:endosome membrane; IDA:dictyBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IDA:dictyBase.
DR GO; GO:0140220; C:pathogen-containing vacuole; IDA:dictyBase.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:dictyBase.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IDA:dictyBase.
DR GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IDA:dictyBase.
DR GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR GO; GO:0051117; F:ATPase binding; IBA:GO_Central.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0006911; P:phagocytosis, engulfment; IMP:dictyBase.
DR GO; GO:0051453; P:regulation of intracellular pH; IMP:dictyBase.
DR GO; GO:0007035; P:vacuolar acidification; IBA:GO_Central.
DR InterPro; IPR002490; V-ATPase_116kDa_su.
DR InterPro; IPR026028; V-type_ATPase_116kDa_su_euka.
DR PANTHER; PTHR11629; PTHR11629; 1.
DR Pfam; PF01496; V_ATPase_I; 1.
DR PIRSF; PIRSF001293; ATP6V0A1; 1.
PE 1: Evidence at protein level;
KW Cytoplasmic vesicle; Endosome; Hydrogen ion transport; Ion transport;
KW Lysosome; Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport; Vacuole.
FT CHAIN 1..815
FT /note="Vacuolar proton translocating ATPase 100 kDa
FT subunit"
FT /id="PRO_0000327961"
FT TOPO_DOM 1..402
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..421
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 422..423
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 424..440
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 441..454
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 455..484
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 485..530
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 531..550
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 551..571
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 572..592
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 593..639
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 640..659
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 660..706
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 707..731
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 732..749
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 750..788
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 789..815
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CONFLICT 170
FT /note="Q -> L (in Ref. 1; AAB49621)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 815 AA; 93288 MW; A12E11C3088B4D00 CRC64;
MSFLRPSIWR SSPMQMVQLF VQIEAAHDTV DELGKLGLIQ FLDDNEHVNL FQRNFVNEVK
RCDDMEKKLK FFEDQVKKEP KLQKLLPDNM LSVVDDDSQM DELEGRFDEL ESELKQVNAN
QETLQRNYNE LIQLRHVLTK DSVFFQENPN LIEGEGHEHS ARSPLLAEDQ HVSEVAKQGV
KLGFITGVMN TDKMPQFQRS LWRTTRGNNY VKDARIEEEI IDPQTGEETA KTVFIVFFQG
ERLQQKIKKI CESFGANIYD CPDNSFERSN LLQKVTVRIT DLYEVLQRSK DHKRQTLAGI
VPRLYSWKKK VLLEKSIYHT MNLFDYDVGR KCLIAKGWTP KDKIEEIQLA LRTATTRSGA
LVPSVLSIIK TEGSPPTHFE TNKYTSSFQE IVNAYGIAHY REVNPAVLTI VTFPFLFGVM
FGDVGHGALL LLSALGLISL EKKLAGKKLN ELIQMPFDGR YVLFLMSLFS IYVGFIYNEC
FSIPMNIFGS QYNLNSTTGL YTYQHTDRVY PVGVDPLWKG APNELVYYNS FKMKLSIIFG
VVQMSVGICF SLLNYLNQKG PIKIVNILTQ FVPQMIFLWS IFGYMSVLII LKWVVPYRSF
EVDKVDPPFI LPTIIAMFLS PGGTPDVVFF SGQGAVQTAL LFLALISIPV MLVIKPLFMK
RFHFQEVERK KLGHHEEEHD DEALYTGHHG EEFEMGEVFV HQVIHTIEFV LGAVSNTASY
LRLWALSLAH SELSSVFWER ILIGQVERGN PFLAFVGFGA WLGASVAVLL LMESLSAFLH
ALRLHWVEFQ NKFYIGDGVR FIPYSATRIL SEDDE
