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Protein

Metastasis suppressor protein 1

Gene

Mtss1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Inhibits the nucleation of actin filaments in vitro.1 Publication

GO - Molecular functioni

  • actin binding Source: MGI
  • actin filament binding Source: MGI
  • actin monomer binding Source: UniProtKB
  • identical protein binding Source: MGI
  • receptor binding Source: UniProtKB

GO - Biological processi

  • actin filament organization Source: MGI
  • actin filament polymerization Source: MGI
  • adherens junction maintenance Source: MGI
  • bone mineralization Source: MGI
  • cellular response to fluid shear stress Source: UniProtKB
  • epithelial cell proliferation involved in renal tubule morphogenesis Source: UniProtKB
  • glomerulus morphogenesis Source: UniProtKB
  • in utero embryonic development Source: MGI
  • magnesium ion homeostasis Source: MGI
  • muscle organ development Source: UniProtKB
  • negative regulation of epithelial cell proliferation Source: UniProtKB
  • nephron tubule epithelial cell differentiation Source: UniProtKB
  • nervous system development Source: UniProtKB
  • plasma membrane organization Source: InterPro
  • positive regulation of actin filament bundle assembly Source: MGI
  • positive regulation of defense response to virus by host Source: MGI
  • renal system development Source: MGI
  • renal tubule morphogenesis Source: UniProtKB
  • xenophagy Source: MGI
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Metastasis suppressor protein 1
Alternative name(s):
Missing in metastasis protein
Gene namesi
Name:Mtss1
Synonyms:Mim
OrganismiMus musculus (Mouse)Imported
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:2384818. Mtss1.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: UniProtKB
  • adherens junction Source: MGI
  • cytoplasm Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi746 – 7461K → A: Loss of actin-binding. 1 Publication
Mutagenesisi747 – 7471K → A: Loss of actin-binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 759759Metastasis suppressor protein 1PRO_0000096640Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei262 – 2621PhosphothreonineCombined sources
Modified residuei265 – 2651PhosphoserineCombined sources
Modified residuei266 – 2661PhosphoserineCombined sources
Modified residuei275 – 2751PhosphoserineCombined sources
Modified residuei326 – 3261PhosphoserineCombined sources
Modified residuei429 – 4291PhosphothreonineCombined sources
Modified residuei607 – 6071PhosphothreonineCombined sources
Modified residuei648 – 6481PhosphoserineCombined sources
Modified residuei651 – 6511PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8R1S4.
MaxQBiQ8R1S4.
PaxDbiQ8R1S4.
PRIDEiQ8R1S4.

PTM databases

iPTMnetiQ8R1S4.
PhosphoSiteiQ8R1S4.

Expressioni

Tissue specificityi

Strongly expressed in the developing neurons and skeletal and cardiac muscles in embryos. Strongly expressed also in liver, outer layers of the kidney, and in the Purkinje cells of the brain.1 Publication

Gene expression databases

CleanExiMM_MTSS1.

Interactioni

Subunit structurei

Binds to actin.

GO - Molecular functioni

  • actin binding Source: MGI
  • actin filament binding Source: MGI
  • actin monomer binding Source: UniProtKB
  • identical protein binding Source: MGI
  • receptor binding Source: UniProtKB

Protein-protein interaction databases

DIPiDIP-29271N.
STRINGi10090.ENSMUSP00000079239.

Structurei

Secondary structure

759
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1 – 2424Combined sources
Helixi27 – 6640Combined sources
Helixi71 – 10333Combined sources
Helixi105 – 15046Combined sources
Helixi154 – 1563Combined sources
Turni157 – 1593Combined sources
Helixi162 – 21453Combined sources
Helixi215 – 2195Combined sources
Helixi220 – 23314Combined sources
Helixi242 – 2443Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D1LX-ray1.85A/B1-250[»]
ProteinModelPortaliQ8R1S4.
SMRiQ8R1S4. Positions 1-246, 729-757.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8R1S4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 254254IMDPROSITE-ProRule annotationAdd
BLAST
Domaini731 – 74818WH2PROSITE-ProRule annotationCuratedAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili108 – 15750Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi242 – 363122Ser-richAdd
BLAST
Compositional biasi612 – 730119Pro-richAdd
BLAST

Domaini

The WH2 motif at the C-terminus binds to actin monomers.1 Publication

Sequence similaritiesi

Belongs to the MTSS1 family.Curated
Contains 1 IMD (IRSp53/MIM homology) domain.PROSITE-ProRule annotation
Contains 1 WH2 domain.PROSITE-ProRule annotationCurated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IGVU. Eukaryota.
ENOG410XRT4. LUCA.
HOGENOMiHOG000113691.
HOVERGENiHBG052530.
InParanoidiQ8R1S4.
PhylomeDBiQ8R1S4.

Family and domain databases

InterProiIPR013606. I-BAR_dom.
IPR027682. MIM.
IPR030127. MIM/ABBA.
IPR003124. WH2_dom.
[Graphical view]
PANTHERiPTHR15708. PTHR15708. 1 hit.
PTHR15708:SF10. PTHR15708:SF10. 1 hit.
PfamiPF08397. IMD. 1 hit.
PF02205. WH2. 1 hit.
[Graphical view]
PROSITEiPS51338. IMD. 1 hit.
PS51082. WH2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1Curated (identifier: Q8R1S4-1) [UniParc]FASTAAdd to basket

Also known as: Long1 Publication

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEAVIEKECS ALGGLFQTII SDMKGSYPVW EDFINKAGKL QSQLRTTVVA
60 70 80 90 100
AAAFLDAFQK VADMATNTRG GTREIGSALT RMCMRHRSIE AKLRQFSSAL
110 120 130 140 150
IDCLINPLQE QMEEWKKVAN QLDKDHAKEY KKARQEIKNK SSDTLKLQKK
160 170 180 190 200
AKKVDAQGRG DIQPQLDSAL QDVNDKYLLL EETEKQAVRK ALIEERGRFC
210 220 230 240 250
TFISMLRPVI EEEISMLGEI THLQTISEDL KSLTMDPHKL PSSSEQVILD
260 270 280 290 300
LKGSDYSWSY QTPPSSPSTT MSRKSSVCSS LNSVNSSDSR SSGSHSHSPS
310 320 330 340 350
SHYRYRSSNL AQQAPVRLSS VSSHDSGFIS QDAFQSKSPS PMPPEAANQL
360 370 380 390 400
SNGFSHCSLS SESHAGPVGA GPFPHCLPAS RLLPRVTSVH LPDYAHYYTI
410 420 430 440 450
GPGMFPSSQI PSWKDWAKPG PYDQPLVNTL QRRKEKREPD SNGGGPTTTG
460 470 480 490 500
GPPAGAEEAQ RPRSMTVSAA TRPGEEMAAC EELTLALSRG LQLDVQRSSR
510 520 530 540 550
DSLQCSSGYS TQTTTPCCSE DTIPSQVSDY DYFSVSGDQE AEQQEFDKSS
560 570 580 590 600
TIPRNSDISQ SYRRMFQAKR PASTAGLPTT LGPAMVTPGV ATIRRTPSTK
610 620 630 640 650
PSVRRGTIGA GPIPIKTPVI PVKTPTVPDL PGVLPSPPDG PEERGEHSPE
660 670 680 690 700
SPSAGEGPQG VSNIPSSLWS GQAPVNPPLP GPKPSIPEEH RQAIPESEAE
710 720 730 740 750
DQERDPPSAT VSPGPIPESD PADLSPRESP QGEDMLNAIR RGVKLKKTTT

NDRSAPRFS
Length:759
Mass (Da):82,408
Last modified:June 1, 2002 - v1
Checksum:i3E9008065FF78439
GO
Isoform 2Curated (identifier: Q8R1S4-2) [UniParc]FASTAAdd to basket

Also known as: Short1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     483-483: L → P
     487-487: L → P
     646-681: Missing.

Show »
Length:723
Mass (Da):78,829
Checksum:i52B227AA050AB392
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti139 – 1391N → K in BAC27008 (PubMed:16141072).Curated
Sequence conflicti758 – 7581F → L in BAC27008 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei483 – 4831L → P in isoform 2. 1 PublicationVSP_050527
Alternative sequencei487 – 4871L → P in isoform 2. 1 PublicationVSP_050528
Alternative sequencei646 – 68136Missing in isoform 2. 1 PublicationVSP_050529Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY214918 mRNA. Translation: AAO52743.1.
BC003483 mRNA. Translation: AAH03483.1.
BC024131 mRNA. Translation: AAH24131.1.
BC042632 mRNA. Translation: AAH42632.1.
AK030533 mRNA. Translation: BAC27008.1.
CCDSiCCDS27496.1. [Q8R1S4-1]
RefSeqiNP_659049.2. NM_144800.2.
UniGeneiMm.215481.
Mm.394414.

Genome annotation databases

GeneIDi211401.
KEGGimmu:211401.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY214918 mRNA. Translation: AAO52743.1.
BC003483 mRNA. Translation: AAH03483.1.
BC024131 mRNA. Translation: AAH24131.1.
BC042632 mRNA. Translation: AAH42632.1.
AK030533 mRNA. Translation: BAC27008.1.
CCDSiCCDS27496.1. [Q8R1S4-1]
RefSeqiNP_659049.2. NM_144800.2.
UniGeneiMm.215481.
Mm.394414.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D1LX-ray1.85A/B1-250[»]
ProteinModelPortaliQ8R1S4.
SMRiQ8R1S4. Positions 1-246, 729-757.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29271N.
STRINGi10090.ENSMUSP00000079239.

PTM databases

iPTMnetiQ8R1S4.
PhosphoSiteiQ8R1S4.

Proteomic databases

EPDiQ8R1S4.
MaxQBiQ8R1S4.
PaxDbiQ8R1S4.
PRIDEiQ8R1S4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi211401.
KEGGimmu:211401.

Organism-specific databases

CTDi9788.
MGIiMGI:2384818. Mtss1.

Phylogenomic databases

eggNOGiENOG410IGVU. Eukaryota.
ENOG410XRT4. LUCA.
HOGENOMiHOG000113691.
HOVERGENiHBG052530.
InParanoidiQ8R1S4.
PhylomeDBiQ8R1S4.

Miscellaneous databases

ChiTaRSiMtss1. mouse.
EvolutionaryTraceiQ8R1S4.
NextBioi373226.
PROiQ8R1S4.
SOURCEiSearch...

Gene expression databases

CleanExiMM_MTSS1.

Family and domain databases

InterProiIPR013606. I-BAR_dom.
IPR027682. MIM.
IPR030127. MIM/ABBA.
IPR003124. WH2_dom.
[Graphical view]
PANTHERiPTHR15708. PTHR15708. 1 hit.
PTHR15708:SF10. PTHR15708:SF10. 1 hit.
PfamiPF08397. IMD. 1 hit.
PF02205. WH2. 1 hit.
[Graphical view]
PROSITEiPS51338. IMD. 1 hit.
PS51082. WH2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mouse MIM, a tissue-specific regulator of cytoskeletal dynamics, interacts with ATP-actin monomers through its C-terminal WH2 domain."
    Mattila P.K., Salminen M., Yamashiro T., Lappalainen P.
    J. Biol. Chem. 278:8452-8459(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, MUTAGENESIS OF LYS-746 AND LYS-747, INTERACTION OF WH2 DOMAIN WITH ACTIN.
    Strain: FVB/NImported.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J1 Publication and FVB/NImported.
    Tissue: Liver1 Publication and Mammary gland1 Publication.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 82-759 (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Pituitary.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-262; SER-265; SER-266; SER-275; THR-429; THR-607; SER-648 AND SER-651, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas and Spleen.

Entry informationi

Entry nameiMTSS1_MOUSE
AccessioniPrimary (citable) accession number: Q8R1S4
Secondary accession number(s): Q8BMM3, Q99LB3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2003
Last sequence update: June 1, 2002
Last modified: May 11, 2016
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.