MTSS2_MOUSE
ID MTSS2_MOUSE Reviewed; 715 AA.
AC Q6P9S0; Q8C7B7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Protein MTSS 2 {ECO:0000305};
DE AltName: Full=MTSS1-like protein;
GN Name=Mtss2; Synonyms=Mtss1l {ECO:0000312|MGI:MGI:3039591};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 315-715.
RC STRAIN=C57BL/6J; TISSUE=Heart;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-257; SER-261; SER-575;
RP SER-597 AND SER-602, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Involved in plasma membrane dynamics. Potentiated PDGF-
CC mediated formation of membrane ruffles and lamellipodia in fibroblasts,
CC acting via RAC1 activation. May function in actin bundling.
CC {ECO:0000250|UniProtKB:Q765P7}.
CC -!- SUBUNIT: Interacts (via IMD domain) with RAC1; this interaction may be
CC important to potentiate PDGF-induced RAC1 activation.
CC {ECO:0000250|UniProtKB:Q765P7}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q765P7}. Cell
CC projection, ruffle {ECO:0000250|UniProtKB:Q765P7}. Note=Colocalizes
CC with RAC1 within membrane ruffles. {ECO:0000250|UniProtKB:Q765P7}.
CC -!- SIMILARITY: Belongs to the MTSS family. {ECO:0000305}.
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DR EMBL; BC060632; AAH60632.1; -; mRNA.
DR EMBL; AK052172; BAC34868.1; -; mRNA.
DR CCDS; CCDS22664.1; -.
DR RefSeq; NP_001297520.1; NM_001310591.1.
DR RefSeq; NP_941027.1; NM_198625.2.
DR AlphaFoldDB; Q6P9S0; -.
DR SMR; Q6P9S0; -.
DR BioGRID; 232673; 5.
DR IntAct; Q6P9S0; 1.
DR STRING; 10090.ENSMUSP00000050211; -.
DR iPTMnet; Q6P9S0; -.
DR PhosphoSitePlus; Q6P9S0; -.
DR MaxQB; Q6P9S0; -.
DR PaxDb; Q6P9S0; -.
DR PeptideAtlas; Q6P9S0; -.
DR PRIDE; Q6P9S0; -.
DR ProteomicsDB; 290115; -.
DR Antibodypedia; 58925; 32 antibodies from 12 providers.
DR Ensembl; ENSMUST00000052457; ENSMUSP00000050211; ENSMUSG00000033763.
DR GeneID; 244654; -.
DR KEGG; mmu:244654; -.
DR UCSC; uc009nkx.1; mouse.
DR CTD; 92154; -.
DR MGI; MGI:3039591; Mtss2.
DR VEuPathDB; HostDB:ENSMUSG00000033763; -.
DR eggNOG; ENOG502QRG4; Eukaryota.
DR GeneTree; ENSGT00950000183156; -.
DR HOGENOM; CLU_004805_2_1_1; -.
DR InParanoid; Q6P9S0; -.
DR OMA; CVFYTDD; -.
DR OrthoDB; 529252at2759; -.
DR PhylomeDB; Q6P9S0; -.
DR TreeFam; TF320619; -.
DR BioGRID-ORCS; 244654; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Mtss1l; mouse.
DR PRO; PR:Q6P9S0; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q6P9S0; protein.
DR Bgee; ENSMUSG00000033763; Expressed in embryonic brain and 206 other tissues.
DR ExpressionAtlas; Q6P9S0; baseline and differential.
DR Genevisible; Q6P9S0; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IDA:MGI.
DR GO; GO:0031235; C:intrinsic component of the cytoplasmic side of the plasma membrane; IBA:GO_Central.
DR GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0001726; C:ruffle; IDA:MGI.
DR GO; GO:0032587; C:ruffle membrane; ISO:MGI.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0003785; F:actin monomer binding; IDA:MGI.
DR GO; GO:0005096; F:GTPase activator activity; ISO:MGI.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:MGI.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; IDA:MGI.
DR GO; GO:0090630; P:activation of GTPase activity; ISO:MGI.
DR GO; GO:0030031; P:cell projection assembly; IBA:GO_Central.
DR GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; ISO:MGI.
DR GO; GO:0097581; P:lamellipodium organization; IMP:MGI.
DR GO; GO:0061024; P:membrane organization; IDA:MGI.
DR GO; GO:0007009; P:plasma membrane organization; IEA:InterPro.
DR GO; GO:0097178; P:ruffle assembly; IEA:InterPro.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR013606; I-BAR_dom.
DR InterPro; IPR030127; MTSS1/MTSS2.
DR InterPro; IPR030059; MTSS2.
DR PANTHER; PTHR15708; PTHR15708; 2.
DR PANTHER; PTHR15708:SF8; PTHR15708:SF8; 2.
DR Pfam; PF08397; IMD; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR PROSITE; PS51338; IMD; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Cell projection; Coiled coil; Cytoplasm; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..715
FT /note="Protein MTSS 2"
FT /id="PRO_0000319611"
FT DOMAIN 1..249
FT /note="IMD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00668"
FT DOMAIN 687..704
FT /note="WH2"
FT REGION 253..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 134..156
FT /evidence="ECO:0000255"
FT COMPBIAS 253..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..368
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 257
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 404
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q765P7"
FT MOD_RES 542
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q765P7"
FT MOD_RES 564
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q765P7"
FT MOD_RES 575
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 587
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q765P7"
FT MOD_RES 597
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 602
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 606
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q765P7"
SQ SEQUENCE 715 AA; 76844 MW; 04AE3F9004A3561C CRC64;
METAEKECGA LGGLFQAIVN DMKSSYPIWE DFNSKAAKLH SQLRTTVLAA VAFLDAFQKV
ADMATNTRGA TRDIGSALTR MCMRHRSIET KLRQFTNALL ESLINPLQER IEDWKKSANQ
LDKDHAKEYK RARHEIKKKS SDTLKLQKKA RKGKGDLQPQ LDSALQDVND MYLLLEETEK
QAVRRALIEE RGRFCTFITF LQPVVNGELT MLGEITHLQG IIDDLVVLTA DPHKLPPASE
QVIKDLKGSD YSWSYQTPPS SPSSSNSRKS SMCSLAQPAT TRLSSVSSHD SGFVSQDPTY
SKPPSPMPSD ITSQKSSSSA SSEASETCQS VSECSSPTSD WTKAGPHEQP SATTLQRRKD
RVEHLRDTEP GPTGGGTVGS SGEEVPRTRM SPATIAAKHG EEVSPAASDL AMVLTRGLSL
EHQKSSRDSL QYSSGYSTQT TTPSCSEDTI PSQGSDYDCY SVNGDADSEG PPEFDKSSTI
PRNSNIAQNY RRLIQTKRPA STAGLPTAGL PTAMGLPSGA PPGVATIRRT PSTKPTVRRA
LSSAGPIPIR PPIVPVKTPT VPDSPGYVGP TRAGSEECVF YTDEVASPLA PDLAKASPKR
LSLPNTAWGS QSPEVASYGG GAAVGLATED EEQQLAANRH SLVEKLGELV AGAHALGEGQ
FPFPTALSAT PSEETPTPPP AATSDPPAED MLVAIRRGVR LRRTVTNDRS APRIL
