Entry sw: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   02-NOV-2016, entry version 76.
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; Mycetozoa; Dictyosteliida; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RX   PubMed=8743951;
RA   Liu T., Clarke M.;
RT   "The vacuolar proton pump of Dictyostelium discoideum: molecular
RT   cloning 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.,
RA   Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
RA   Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
RA   Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
RA   Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
RA   Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
RA   Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
RA   Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
RA   Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
RA   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.,
RA   Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
RA   Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
RA   Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
RA   Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
RA   Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
RA   Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
RA   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;
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
RT   vacuolar proton pump impairs enzyme assembly, endocytic function and
RT   cytosolic pH regulation.";
RL   J. Cell Sci. 115:1907-1918(2002).
RN   [4]
RP   SUBCELLULAR LOCATION, AND TOPOLOGY.
RX   PubMed=12082150;
RA   Clarke M., Koehler J., Arana Q., Liu T., Heuser J., Gerisch G.;
RT   "Dynamics of the vacuolar H(+)-ATPase in the contractile vacuole
RT   complex 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
RT   the role of a Galpha during uptake.";
RL   Mol. Cell. Proteomics 5:2228-2243(2006).
CC   -!- FUNCTION: Essential component of the vacuolar proton pump (V-
CC       ATPase), a multimeric enzyme that catalyzes the translocation of
CC       protons across the membranes. Required for assembly and activity
CC       of the V-ATPase. Required in both the contractile vacuole system
CC       and the endosomal/lysosomal system. Also required for cytosolic pH
CC       regulation. {ECO:0000269|PubMed:11956322}.
CC   -!- SUBUNIT: The V-ATPase is a heteromultimeric enzyme. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Multi-pass
CC       membrane protein. Endosome membrane; Multi-pass membrane protein.
CC       Vacuole membrane; Multi-pass membrane protein. Lysosome membrane;
CC       Multi-pass membrane protein. Note=Found in membrane of contractile
CC       vacuole complex, an osmoregulatory organelle.
CC   -!- DISRUPTION PHENOTYPE: Cells show defects in V-ATPase enzyme
CC       assembly, 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};
DR   EMBL; U38803; AAB49621.1; -; mRNA.
DR   EMBL; AAFI02000186; EAL61459.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_629892.1; XM_629890.1.
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   eggNOG; COG1269; LUCA.
DR   InParanoid; Q54E04; -.
DR   KO; K02154; -.
DR   PhylomeDB; Q54E04; -.
DR   PRO; PR:Q54E04; -.
DR   Proteomes; UP000002195; Chromosome 6.
DR   Proteomes; UP000002195; Unassembled WGS sequence.
DR   GO; GO:0031164; C:contractile vacuolar membrane; IDA:dictyBase.
DR   GO; GO:0000331; C:contractile vacuole; IDA:dictyBase.
DR   GO; GO:0030666; C:endocytic vesicle membrane; 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: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; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
DR   GO; GO:0015986; P:ATP synthesis coupled proton transport; IBA:GO_Central.
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   GO; GO:0070072; P:vacuolar proton-transporting V-type ATPase complex assembly; 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   Complete proteome; Cytoplasmic vesicle; Endosome;
KW   Hydrogen ion transport; Ion transport; Lysosome; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW   Vacuole.
FT   CHAIN         1    815       Vacuolar proton translocating ATPase 100
FT                                kDa subunit.
FT                                /FTId=PRO_0000327961.
FT   TOPO_DOM      1    402       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    403    421       Helical. {ECO:0000255}.
FT   TOPO_DOM    422    423       Vacuolar. {ECO:0000255}.
FT   TRANSMEM    424    440       Helical. {ECO:0000255}.
FT   TOPO_DOM    441    454       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    455    484       Helical. {ECO:0000255}.
FT   TOPO_DOM    485    530       Vacuolar. {ECO:0000255}.
FT   TRANSMEM    531    550       Helical. {ECO:0000255}.
FT   TOPO_DOM    551    571       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    572    592       Helical. {ECO:0000255}.
FT   TOPO_DOM    593    639       Vacuolar. {ECO:0000255}.
FT   TRANSMEM    640    659       Helical. {ECO:0000255}.
FT   TOPO_DOM    660    706       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    707    731       Helical. {ECO:0000255}.
FT   TOPO_DOM    732    749       Vacuolar. {ECO:0000255}.
FT   TRANSMEM    750    788       Helical. {ECO:0000255}.
FT   TOPO_DOM    789    815       Cytoplasmic. {ECO:0000255}.
FT   CONFLICT    170    170       Q -> L (in Ref. 1; AAB49621).
FT                                {ECO:0000305}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT        32    805       ipfam:V_ATPase_I [T]
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
//