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MOB kinase activator-like 1 (Mob as tumor suppressor protein 1) (Dmob1) (Mps one binder kinase activator-like 1)

 MOB1_DROME              Reviewed;         219 AA.
Q95RA8; Q9VD10;
06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
22-NOV-2017, entry version 117.
RecName: Full=MOB kinase activator-like 1;
AltName: Full=Mob as tumor suppressor protein 1;
Short=Dmob1;
AltName: Full=Mps one binder kinase activator-like 1;
Name=mats {ECO:0000312|FlyBase:FBgn0038965}; ORFNames=CG13852;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1] {ECO:0000312|EMBL:AAF55993.2}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[2] {ECO:0000305, ECO:0000312|EMBL:AAF55993.2}
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[3] {ECO:0000312|EMBL:AAL29068.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley {ECO:0000312|EMBL:AAL29068.1};
TISSUE=Embryo {ECO:0000269|PubMed:12537569};
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[4] {ECO:0000305}
FUNCTION, INTERACTION WITH WTS, PHOSPHORYLATION, AND DISRUPTION
PHENOTYPE.
PubMed=15766530; DOI=10.1016/j.cell.2004.12.036;
Lai Z.-C., Wei X., Shimizu T., Ramos E., Rohrbaugh M., Nikolaidis N.,
Ho L.-L., Li Y.;
"Control of cell proliferation and apoptosis by mob as tumor
suppressor, mats.";
Cell 120:675-685(2005).
[5] {ECO:0000305}
FUNCTION, AND INTERACTION WITH TRC.
PubMed=15975907; DOI=10.1091/mbc.E05-01-0018;
He Y., Emoto K., Fang X., Ren N., Tian X., Jan Y.-N., Adler P.N.;
"Drosophila Mob family proteins interact with the related tricornered
(Trc) and warts (Wts) kinases.";
Mol. Biol. Cell 16:4139-4152(2005).
[6]
FUNCTION, AND PHOSPHORYLATION.
PubMed=17347649; DOI=10.1038/sj.emboj.7601630;
Wei X., Shimizu T., Lai Z.C.;
"Mob as tumor suppressor is activated by Hippo kinase for growth
inhibition in Drosophila.";
EMBO J. 26:1772-1781(2007).
[7]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=18245354; DOI=10.1534/genetics.107.081570;
Shimizu T., Ho L.L., Lai Z.C.;
"The mob as tumor suppressor gene is essential for early development
and regulates tissue growth in Drosophila.";
Genetics 178:957-965(2008).
[8]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=19913529; DOI=10.1016/j.ydbio.2009.10.042;
Ho L.L., Wei X., Shimizu T., Lai Z.C.;
"Mob as tumor suppressor is activated at the cell membrane to control
tissue growth and organ size in Drosophila.";
Dev. Biol. 337:274-283(2010).
-!- FUNCTION: Coactivator of Warts (Wts) kinase in the Hippo/SWH
(Sav/Wts/Hpo)signaling pathway, a signaling pathway that plays a
pivotal role in organ size control and tumor suppression by
restricting proliferation and promoting apoptosis. The core of
this pathway is composed of a kinase cascade wherein Hippo (Hpo),
in complex with its regulatory protein Salvador (Sav),
phosphorylates and activates Warts (Wts) in complex with its
regulatory protein Mats, which in turn phosphorylates and
inactivates the Yorkie (Yki)oncoprotein. The Hippo/SWH signaling
pathway inhibits the activity of the transcriptional complex
formed by Scalloped (sd) and Yki and the target genes of this
pathway include cyclin-E (cycE), diap1 and bantam. Mats is
essential for early development and is required for proper
chromosomal segregation in developing embryos.
{ECO:0000269|PubMed:15766530, ECO:0000269|PubMed:15975907,
ECO:0000269|PubMed:17347649, ECO:0000269|PubMed:18245354,
ECO:0000269|PubMed:19913529}.
-!- SUBUNIT: Interacts with and activates trc and wts.
{ECO:0000269|PubMed:15766530, ECO:0000269|PubMed:15975907}.
-!- INTERACTION:
Q8T0S6:hpo; NbExp=2; IntAct=EBI-143689, EBI-101858;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome. Nucleus. Cytoplasm, cytosol. Cell
membrane. Note=Colocalizes with wts and cyclin E at the
centrosome.
-!- TISSUE SPECIFICITY: Ubiquitously expressed at low levels in
developing tissues (at protein level).
{ECO:0000269|PubMed:18245354}.
-!- PTM: Phosphorylated by wts/mats kinase complex. Activated by
phosphorylation by Hippo (Hpo) kinase which increases its affinity
and its ability to activate Warts (Wts) kinase.
{ECO:0000269|PubMed:15766530, ECO:0000269|PubMed:17347649}.
-!- DISRUPTION PHENOTYPE: Increased cell proliferation, defective
apoptosis, and induction of tissue overgrowth.
{ECO:0000269|PubMed:15766530}.
-!- SIMILARITY: Belongs to the MOB1/phocein family. {ECO:0000255}.
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EMBL; AE014297; AAF55993.2; -; Genomic_DNA.
EMBL; AY061520; AAL29068.1; -; mRNA.
RefSeq; NP_001262835.1; NM_001275906.1.
RefSeq; NP_001287465.1; NM_001300536.1.
RefSeq; NP_651041.3; NM_142784.3.
UniGene; Dm.3572; -.
ProteinModelPortal; Q95RA8; -.
SMR; Q95RA8; -.
BioGrid; 67590; 19.
DIP; DIP-21478N; -.
IntAct; Q95RA8; 6.
MINT; MINT-1026430; -.
STRING; 7227.FBpp0083624; -.
PaxDb; Q95RA8; -.
PRIDE; Q95RA8; -.
EnsemblMetazoa; FBtr0084229; FBpp0083624; FBgn0038965.
EnsemblMetazoa; FBtr0337044; FBpp0307973; FBgn0038965.
EnsemblMetazoa; FBtr0345205; FBpp0311400; FBgn0038965.
GeneID; 42634; -.
KEGG; dme:Dmel_CG13852; -.
CTD; 42634; -.
FlyBase; FBgn0038965; mats.
eggNOG; KOG0440; Eukaryota.
eggNOG; ENOG410XSUJ; LUCA.
GeneTree; ENSGT00550000074456; -.
InParanoid; Q95RA8; -.
KO; K06685; -.
OMA; DFFNHLN; -.
OrthoDB; EOG091G0LDA; -.
PhylomeDB; Q95RA8; -.
Reactome; R-DME-2028269; Signaling by Hippo.
Reactome; R-DME-390089; Formation of the Hippo kinase cassette.
Reactome; R-DME-390098; Phosphorylation-dependent inhibition of YKI.
Reactome; R-DME-390197; Negative regulation of TH.
GenomeRNAi; 42634; -.
PRO; PR:Q95RA8; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0038965; -.
ExpressionAtlas; Q95RA8; differential.
Genevisible; Q95RA8; DM.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0019901; F:protein kinase binding; IPI:FlyBase.
GO; GO:0006915; P:apoptotic process; IMP:UniProtKB.
GO; GO:0008283; P:cell proliferation; IMP:UniProtKB.
GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB.
GO; GO:0007275; P:multicellular organism development; IMP:UniProtKB.
GO; GO:0030707; P:ovarian follicle cell development; IMP:FlyBase.
GO; GO:0007165; P:signal transduction; IMP:UniProtKB.
Gene3D; 1.20.140.30; -; 1.
InterPro; IPR005301; MOB_kinase_act_fam.
InterPro; IPR036703; MOB_kinase_act_sf.
PANTHER; PTHR22599; PTHR22599; 1.
Pfam; PF03637; Mob1_phocein; 1.
SMART; SM01388; Mob1_phocein; 1.
SUPFAM; SSF101152; SSF101152; 1.
1: Evidence at protein level;
Apoptosis; Cell membrane; Chromosome partition; Complete proteome;
Cytoplasm; Cytoskeleton; Developmental protein; Membrane;
Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Zinc.
CHAIN 1 219 MOB kinase activator-like 1.
/FTId=PRO_0000279700.
METAL 79 79 Zinc. {ECO:0000250|UniProtKB:Q9H8S9}.
METAL 84 84 Zinc. {ECO:0000250|UniProtKB:Q9H8S9}.
METAL 161 161 Zinc. {ECO:0000250|UniProtKB:Q9H8S9}.
METAL 166 166 Zinc. {ECO:0000250|UniProtKB:Q9H8S9}.
SEQUENCE 219 AA; 25229 MW; 6B16E04A08B59208 CRC64;
MDFLFGSRSS KTFKPKKNIP EGTHQYDLMK HAAATLGSGN LRNAVALPDG EDLNEWVAVN
TVDFFNQINM LYGTITEFCT EETCGIMSAG PKYEYHWADG LTVKKPIKCS APKYIDYLMT
WVQDQLDDET LFPSKIGVPF PKNFHSSAKT ILKRLFRVYA HIYHQHFTEV VTLGEEAHLN
TSFKHFIFFV QEFNLIERRE LAPLQELIDK LTAKDERQI


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