MOB1_DROME
ID MOB1_DROME Reviewed; 219 AA.
AC Q95RA8; Q9VD10;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=MOB kinase activator-like 1;
DE AltName: Full=Mob as tumor suppressor protein 1;
DE Short=Dmob1;
DE AltName: Full=Mps one binder kinase activator-like 1;
GN Name=mats {ECO:0000312|FlyBase:FBgn0038965}; ORFNames=CG13852;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000312|EMBL:AAF55993.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAF55993.2}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:AAL29068.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL29068.1};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH WTS, PHOSPHORYLATION, AND DISRUPTION PHENOTYPE.
RX PubMed=15766530; DOI=10.1016/j.cell.2004.12.036;
RA Lai Z.-C., Wei X., Shimizu T., Ramos E., Rohrbaugh M., Nikolaidis N.,
RA Ho L.-L., Li Y.;
RT "Control of cell proliferation and apoptosis by mob as tumor suppressor,
RT mats.";
RL Cell 120:675-685(2005).
RN [5] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH TRC.
RX PubMed=15975907; DOI=10.1091/mbc.e05-01-0018;
RA He Y., Emoto K., Fang X., Ren N., Tian X., Jan Y.-N., Adler P.N.;
RT "Drosophila Mob family proteins interact with the related tricornered (Trc)
RT and warts (Wts) kinases.";
RL Mol. Biol. Cell 16:4139-4152(2005).
RN [6]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=17347649; DOI=10.1038/sj.emboj.7601630;
RA Wei X., Shimizu T., Lai Z.C.;
RT "Mob as tumor suppressor is activated by Hippo kinase for growth inhibition
RT in Drosophila.";
RL EMBO J. 26:1772-1781(2007).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18245354; DOI=10.1534/genetics.107.081570;
RA Shimizu T., Ho L.L., Lai Z.C.;
RT "The mob as tumor suppressor gene is essential for early development and
RT regulates tissue growth in Drosophila.";
RL Genetics 178:957-965(2008).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19913529; DOI=10.1016/j.ydbio.2009.10.042;
RA Ho L.L., Wei X., Shimizu T., Lai Z.C.;
RT "Mob as tumor suppressor is activated at the cell membrane to control
RT tissue growth and organ size in Drosophila.";
RL Dev. Biol. 337:274-283(2010).
CC -!- FUNCTION: Coactivator of Warts (Wts) kinase in the Hippo/SWH
CC (Sav/Wts/Hpo)signaling pathway, a signaling pathway that plays a
CC pivotal role in organ size control and tumor suppression by restricting
CC proliferation and promoting apoptosis. The core of this pathway is
CC composed of a kinase cascade wherein Hippo (Hpo), in complex with its
CC regulatory protein Salvador (Sav), phosphorylates and activates Warts
CC (Wts) in complex with its regulatory protein Mats, which in turn
CC phosphorylates and inactivates the Yorkie (Yki)oncoprotein. The
CC Hippo/SWH signaling pathway inhibits the activity of the
CC transcriptional complex formed by Scalloped (sd) and Yki and the target
CC genes of this pathway include cyclin-E (cycE), diap1 and bantam. Mats
CC is essential for early development and is required for proper
CC chromosomal segregation in developing embryos.
CC {ECO:0000269|PubMed:15766530, ECO:0000269|PubMed:15975907,
CC ECO:0000269|PubMed:17347649, ECO:0000269|PubMed:18245354,
CC ECO:0000269|PubMed:19913529}.
CC -!- SUBUNIT: Interacts with and activates trc and wts.
CC {ECO:0000269|PubMed:15766530, ECO:0000269|PubMed:15975907}.
CC -!- INTERACTION:
CC Q95RA8; Q8T0S6: hpo; NbExp=2; IntAct=EBI-143689, EBI-101858;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome. Nucleus. Cytoplasm, cytosol. Cell membrane.
CC Note=Colocalizes with wts and cyclin E at the centrosome.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed at low levels in developing
CC tissues (at protein level). {ECO:0000269|PubMed:18245354}.
CC -!- PTM: Phosphorylated by wts/mats kinase complex. Activated by
CC phosphorylation by Hippo (Hpo) kinase which increases its affinity and
CC its ability to activate Warts (Wts) kinase.
CC {ECO:0000269|PubMed:15766530, ECO:0000269|PubMed:17347649}.
CC -!- DISRUPTION PHENOTYPE: Increased cell proliferation, defective
CC apoptosis, and induction of tissue overgrowth.
CC {ECO:0000269|PubMed:15766530}.
CC -!- SIMILARITY: Belongs to the MOB1/phocein family. {ECO:0000255}.
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DR EMBL; AE014297; AAF55993.2; -; Genomic_DNA.
DR EMBL; AY061520; AAL29068.1; -; mRNA.
DR RefSeq; NP_001262835.1; NM_001275906.1.
DR RefSeq; NP_001287465.1; NM_001300536.1.
DR RefSeq; NP_651041.3; NM_142784.3.
DR AlphaFoldDB; Q95RA8; -.
DR SMR; Q95RA8; -.
DR BioGRID; 67590; 20.
DR DIP; DIP-21478N; -.
DR IntAct; Q95RA8; 7.
DR MINT; Q95RA8; -.
DR STRING; 7227.FBpp0083624; -.
DR PaxDb; Q95RA8; -.
DR PRIDE; Q95RA8; -.
DR DNASU; 42634; -.
DR EnsemblMetazoa; FBtr0084229; FBpp0083624; FBgn0038965.
DR EnsemblMetazoa; FBtr0337044; FBpp0307973; FBgn0038965.
DR EnsemblMetazoa; FBtr0345205; FBpp0311400; FBgn0038965.
DR GeneID; 42634; -.
DR KEGG; dme:Dmel_CG13852; -.
DR CTD; 42634; -.
DR FlyBase; FBgn0038965; mats.
DR VEuPathDB; VectorBase:FBgn0038965; -.
DR eggNOG; KOG0440; Eukaryota.
DR GeneTree; ENSGT01050000244898; -.
DR HOGENOM; CLU_038321_3_1_1; -.
DR InParanoid; Q95RA8; -.
DR OMA; HYPVIVH; -.
DR OrthoDB; 1127941at2759; -.
DR PhylomeDB; Q95RA8; -.
DR Reactome; R-DME-2028269; Signaling by Hippo.
DR Reactome; R-DME-390089; Formation of the Hippo kinase cassette.
DR Reactome; R-DME-390098; Phosphorylation-dependent inhibition of YKI.
DR Reactome; R-DME-390150; DS ligand bound to FT receptor.
DR SignaLink; Q95RA8; -.
DR BioGRID-ORCS; 42634; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 42634; -.
DR PRO; PR:Q95RA8; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0038965; Expressed in saliva-secreting gland and 26 other tissues.
DR ExpressionAtlas; Q95RA8; baseline and differential.
DR Genevisible; Q95RA8; DM.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030295; F:protein kinase activator activity; IDA:FlyBase.
DR GO; GO:0019901; F:protein kinase binding; IPI:FlyBase.
DR GO; GO:0006915; P:apoptotic process; IMP:UniProtKB.
DR GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB.
DR GO; GO:0035329; P:hippo signaling; IMP:FlyBase.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0030707; P:ovarian follicle cell development; IMP:FlyBase.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IMP:UniProtKB.
DR Gene3D; 1.20.140.30; -; 1.
DR InterPro; IPR005301; MOB_kinase_act_fam.
DR InterPro; IPR036703; MOB_kinase_act_sf.
DR PANTHER; PTHR22599; PTHR22599; 1.
DR Pfam; PF03637; Mob1_phocein; 1.
DR SMART; SM01388; Mob1_phocein; 1.
DR SUPFAM; SSF101152; SSF101152; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Cell membrane; Chromosome partition; Cytoplasm; Cytoskeleton;
KW Developmental protein; Membrane; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Zinc.
FT CHAIN 1..219
FT /note="MOB kinase activator-like 1"
FT /id="PRO_0000279700"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9H8S9"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9H8S9"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9H8S9"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9H8S9"
SQ 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
