MTSS1_MOUSE
ID MTSS1_MOUSE Reviewed; 759 AA.
AC Q8R1S4; Q8BMM3; Q99LB3;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 144.
DE RecName: Full=Protein MTSS 1 {ECO:0000305};
DE AltName: Full=Metastasis suppressor protein 1;
DE AltName: Full=Missing in metastasis protein;
GN Name=Mtss1 {ECO:0000312|MGI:MGI:2384818}; Synonyms=Mim;
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 {ECO:0000312|EMBL:AAH24131.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY,
RP MUTAGENESIS OF LYS-746 AND LYS-747, AND INTERACTION OF WH2 DOMAIN WITH
RP ACTIN.
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAO52743.1};
RX PubMed=12482861; DOI=10.1074/jbc.m212113200;
RA Mattila P.K., Salminen M., Yamashiro T., Lappalainen P.;
RT "Mouse MIM, a tissue-specific regulator of cytoskeletal dynamics, interacts
RT with ATP-actin monomers through its C-terminal WH2 domain.";
RL J. Biol. Chem. 278:8452-8459(2003).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000269|PubMed:15489334}, and
RC FVB/N {ECO:0000312|EMBL:AAH42632.1};
RC TISSUE=Liver {ECO:0000269|PubMed:15489334}, and
RC Mammary gland {ECO:0000269|PubMed:15489334};
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 82-759 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Pituitary;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-262; SER-265; SER-266;
RP SER-275; THR-429; THR-607; SER-648 AND SER-651, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, and
RC 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: Inhibits the nucleation of actin filaments in vitro.
CC {ECO:0000269|PubMed:12482861}.
CC -!- SUBUNIT: Binds to actin.
CC -!- INTERACTION:
CC Q8R1S4; Q8R1S4: Mtss1; NbExp=2; IntAct=EBI-15622277, EBI-15622277;
CC Q8R1S4; Q99NH2-1: Pard3; NbExp=2; IntAct=EBI-15622277, EBI-15946047;
CC Q8R1S4; Q62074: Prkci; NbExp=4; IntAct=EBI-15622277, EBI-82016;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000305}; Synonyms=Long {ECO:0000303|PubMed:12482861};
CC IsoId=Q8R1S4-1; Sequence=Displayed;
CC Name=2 {ECO:0000305}; Synonyms=Short {ECO:0000303|PubMed:12482861};
CC IsoId=Q8R1S4-2; Sequence=VSP_050527, VSP_050528, VSP_050529;
CC -!- TISSUE SPECIFICITY: Strongly expressed in the developing neurons and
CC skeletal and cardiac muscles in embryos. Strongly expressed also in
CC liver, outer layers of the kidney, and in the Purkinje cells of the
CC brain. {ECO:0000269|PubMed:12482861}.
CC -!- DOMAIN: The WH2 motif at the C-terminus binds to actin monomers.
CC {ECO:0000269|PubMed:12482861}.
CC -!- SIMILARITY: Belongs to the MTSS family. {ECO:0000305}.
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DR EMBL; AY214918; AAO52743.1; -; mRNA.
DR EMBL; BC003483; AAH03483.1; -; mRNA.
DR EMBL; BC024131; AAH24131.1; -; mRNA.
DR EMBL; BC042632; AAH42632.1; -; mRNA.
DR EMBL; AK030533; BAC27008.1; -; mRNA.
DR CCDS; CCDS27496.1; -. [Q8R1S4-1]
DR RefSeq; NP_659049.2; NM_144800.2.
DR PDB; 2D1L; X-ray; 1.85 A; A/B=1-250.
DR PDBsum; 2D1L; -.
DR AlphaFoldDB; Q8R1S4; -.
DR SMR; Q8R1S4; -.
DR BioGRID; 229230; 5.
DR DIP; DIP-29271N; -.
DR IntAct; Q8R1S4; 4.
DR STRING; 10090.ENSMUSP00000079239; -.
DR iPTMnet; Q8R1S4; -.
DR PhosphoSitePlus; Q8R1S4; -.
DR EPD; Q8R1S4; -.
DR jPOST; Q8R1S4; -.
DR MaxQB; Q8R1S4; -.
DR PaxDb; Q8R1S4; -.
DR PRIDE; Q8R1S4; -.
DR ProteomicsDB; 290218; -. [Q8R1S4-1]
DR ProteomicsDB; 290219; -. [Q8R1S4-2]
DR DNASU; 211401; -.
DR GeneID; 211401; -.
DR KEGG; mmu:211401; -.
DR CTD; 9788; -.
DR MGI; MGI:2384818; Mtss1.
DR eggNOG; ENOG502QRG4; Eukaryota.
DR InParanoid; Q8R1S4; -.
DR OrthoDB; 529252at2759; -.
DR PhylomeDB; Q8R1S4; -.
DR BioGRID-ORCS; 211401; 7 hits in 75 CRISPR screens.
DR ChiTaRS; Mtss1; mouse.
DR EvolutionaryTrace; Q8R1S4; -.
DR PRO; PR:Q8R1S4; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8R1S4; protein.
DR GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005912; C:adherens junction; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0031235; C:intrinsic component of the cytoplasmic side of the plasma membrane; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IDA:MGI.
DR GO; GO:0051015; F:actin filament binding; IDA:MGI.
DR GO; GO:0003785; F:actin monomer binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; ISS:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; IDA:MGI.
DR GO; GO:0030041; P:actin filament polymerization; IDA:MGI.
DR GO; GO:0034334; P:adherens junction maintenance; IMP:MGI.
DR GO; GO:0030282; P:bone mineralization; IMP:MGI.
DR GO; GO:0071498; P:cellular response to fluid shear stress; IDA:UniProtKB.
DR GO; GO:2001013; P:epithelial cell proliferation involved in renal tubule morphogenesis; IMP:UniProtKB.
DR GO; GO:0072102; P:glomerulus morphogenesis; IMP:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IGI:MGI.
DR GO; GO:0010960; P:magnesium ion homeostasis; IMP:MGI.
DR GO; GO:0072170; P:metanephric tubule development; IMP:MGI.
DR GO; GO:0007517; P:muscle organ development; NAS:UniProtKB.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:UniProtKB.
DR GO; GO:0072160; P:nephron tubule epithelial cell differentiation; IMP:UniProtKB.
DR GO; GO:0007399; P:nervous system development; NAS:UniProtKB.
DR GO; GO:0007009; P:plasma membrane organization; IEA:InterPro.
DR GO; GO:0032233; P:positive regulation of actin filament bundle assembly; IMP:MGI.
DR GO; GO:0061333; P:renal tubule morphogenesis; IMP:UniProtKB.
DR DisProt; DP02569; -.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR013606; I-BAR_dom.
DR InterPro; IPR027682; MTSS1.
DR InterPro; IPR030127; MTSS1/MTSS2.
DR InterPro; IPR003124; WH2_dom.
DR PANTHER; PTHR15708; PTHR15708; 1.
DR PANTHER; PTHR15708:SF10; PTHR15708:SF10; 1.
DR Pfam; PF08397; IMD; 1.
DR Pfam; PF02205; WH2; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR PROSITE; PS51338; IMD; 1.
DR PROSITE; PS51082; WH2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Alternative splicing; Coiled coil; Cytoplasm;
KW Cytoskeleton; Phosphoprotein; Reference proteome.
FT CHAIN 1..759
FT /note="Protein MTSS 1"
FT /id="PRO_0000096640"
FT DOMAIN 1..254
FT /note="IMD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00668"
FT DOMAIN 731..748
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406,
FT ECO:0000305"
FT REGION 259..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 108..157
FT /evidence="ECO:0000255"
FT COMPBIAS 618..638
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..673
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..705
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 262
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 429
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 607
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 648
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 651
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 483
FT /note="L -> P (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12482861"
FT /id="VSP_050527"
FT VAR_SEQ 487
FT /note="L -> P (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12482861"
FT /id="VSP_050528"
FT VAR_SEQ 646..681
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12482861"
FT /id="VSP_050529"
FT MUTAGEN 746
FT /note="K->A: Loss of actin-binding."
FT /evidence="ECO:0000269|PubMed:12482861"
FT MUTAGEN 747
FT /note="K->A: Loss of actin-binding."
FT /evidence="ECO:0000269|PubMed:12482861"
FT CONFLICT 139
FT /note="N -> K (in Ref. 3; BAC27008)"
FT /evidence="ECO:0000305"
FT CONFLICT 758
FT /note="F -> L (in Ref. 3; BAC27008)"
FT /evidence="ECO:0000305"
FT HELIX 1..24
FT /evidence="ECO:0007829|PDB:2D1L"
FT HELIX 27..66
FT /evidence="ECO:0007829|PDB:2D1L"
FT HELIX 71..103
FT /evidence="ECO:0007829|PDB:2D1L"
FT HELIX 105..150
FT /evidence="ECO:0007829|PDB:2D1L"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:2D1L"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:2D1L"
FT HELIX 162..214
FT /evidence="ECO:0007829|PDB:2D1L"
FT HELIX 215..219
FT /evidence="ECO:0007829|PDB:2D1L"
FT HELIX 220..233
FT /evidence="ECO:0007829|PDB:2D1L"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:2D1L"
SQ SEQUENCE 759 AA; 82408 MW; 3E9008065FF78439 CRC64;
MEAVIEKECS ALGGLFQTII SDMKGSYPVW EDFINKAGKL QSQLRTTVVA AAAFLDAFQK
VADMATNTRG GTREIGSALT RMCMRHRSIE AKLRQFSSAL IDCLINPLQE QMEEWKKVAN
QLDKDHAKEY KKARQEIKNK SSDTLKLQKK AKKVDAQGRG DIQPQLDSAL QDVNDKYLLL
EETEKQAVRK ALIEERGRFC TFISMLRPVI EEEISMLGEI THLQTISEDL KSLTMDPHKL
PSSSEQVILD LKGSDYSWSY QTPPSSPSTT MSRKSSVCSS LNSVNSSDSR SSGSHSHSPS
SHYRYRSSNL AQQAPVRLSS VSSHDSGFIS QDAFQSKSPS PMPPEAANQL SNGFSHCSLS
SESHAGPVGA GPFPHCLPAS RLLPRVTSVH LPDYAHYYTI GPGMFPSSQI PSWKDWAKPG
PYDQPLVNTL QRRKEKREPD SNGGGPTTTG GPPAGAEEAQ RPRSMTVSAA TRPGEEMAAC
EELTLALSRG LQLDVQRSSR DSLQCSSGYS TQTTTPCCSE DTIPSQVSDY DYFSVSGDQE
AEQQEFDKSS TIPRNSDISQ SYRRMFQAKR PASTAGLPTT LGPAMVTPGV ATIRRTPSTK
PSVRRGTIGA GPIPIKTPVI PVKTPTVPDL PGVLPSPPDG PEERGEHSPE SPSAGEGPQG
VSNIPSSLWS GQAPVNPPLP GPKPSIPEEH RQAIPESEAE DQERDPPSAT VSPGPIPESD
PADLSPRESP QGEDMLNAIR RGVKLKKTTT NDRSAPRFS
