MTSS1_HUMAN
ID MTSS1_HUMAN Reviewed; 755 AA.
AC O43312; J3KNK6; Q8TCA2; Q96RX2;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Protein MTSS 1 {ECO:0000305};
DE AltName: Full=Metastasis suppressor YGL-1;
DE AltName: Full=Metastasis suppressor protein 1;
DE AltName: Full=Missing in metastasis protein;
GN Name=MTSS1 {ECO:0000312|HGNC:HGNC:20443}; Synonyms=KIAA0429, MIM;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Lee Y.-G., Macoska J.A., Schwab E.D., Korenchuk S., Pienta K.J.;
RT "Identification of potential metastasis suppressor gene (YGL-1) in bladder
RT cancer.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 65-755 (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=9455477; DOI=10.1093/dnares/4.5.307;
RA Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VIII. 78
RT new cDNA clones from brain which code for large proteins in vitro.";
RL DNA Res. 4:307-313(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 400-755 (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=12082544; DOI=10.1038/sj.neo.7900231;
RA Lee Y.-G., Macoska J.A., Korenchuk S., Pienta K.J.;
RT "MIM, a potential metastasis suppressor gene in bladder cancer.";
RL Neoplasia 4:291-294(2002).
RN [7]
RP INTERACTION OF WH2 DOMAIN WITH ACTIN, AND SUBUNIT.
RX PubMed=12570871; DOI=10.1042/bj20021962;
RA Woodings J.A., Sharp S.J., Machesky L.M.;
RT "MIM-B, a putative metastasis suppressor protein, binds to actin and to
RT protein tyrosine phosphatase delta.";
RL Biochem. J. 371:463-471(2003).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
CC -!- FUNCTION: May be related to cancer progression or tumor metastasis in a
CC variety of organ sites, most likely through an interaction with the
CC actin cytoskeleton.
CC -!- SUBUNIT: Binds to actin. Binds to the cytoplasmic domain of receptor
CC protein tyrosine phosphatase delta. {ECO:0000269|PubMed:12570871}.
CC -!- INTERACTION:
CC O43312; P42858: HTT; NbExp=3; IntAct=EBI-473954, EBI-466029;
CC O43312; O43312: MTSS1; NbExp=2; IntAct=EBI-473954, EBI-473954;
CC O43312; Q60598: Cttn; Xeno; NbExp=2; IntAct=EBI-473954, EBI-397955;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O43312-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O43312-2; Sequence=VSP_007420, VSP_007421;
CC Name=3;
CC IsoId=O43312-4; Sequence=VSP_016216;
CC Name=4;
CC IsoId=O43312-5; Sequence=VSP_054702;
CC -!- TISSUE SPECIFICITY: Expressed in many tissues, including spleen,
CC thymus, prostate, testis, uterus, colon, and peripheral blood.
CC {ECO:0000269|PubMed:12082544}.
CC -!- DOMAIN: The WH2 motif at the C-terminus binds to actin monomers.
CC -!- SIMILARITY: Belongs to the MTSS family. {ECO:0000305}.
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DR EMBL; AF086645; AAF15947.1; -; mRNA.
DR EMBL; AK027015; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC090198; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC023998; AAH23998.1; -; mRNA.
DR EMBL; AB007889; BAA24859.3; -; mRNA.
DR CCDS; CCDS6353.1; -. [O43312-1]
DR CCDS; CCDS64968.1; -. [O43312-4]
DR CCDS; CCDS64969.1; -. [O43312-5]
DR RefSeq; NP_001269900.1; NM_001282971.1. [O43312-5]
DR RefSeq; NP_001269903.1; NM_001282974.1. [O43312-4]
DR RefSeq; NP_055566.3; NM_014751.5. [O43312-1]
DR PDB; 2D1K; X-ray; 2.50 A; C=724-755.
DR PDBsum; 2D1K; -.
DR AlphaFoldDB; O43312; -.
DR SMR; O43312; -.
DR BioGRID; 115132; 15.
DR DIP; DIP-17022N; -.
DR ELM; O43312; -.
DR IntAct; O43312; 6.
DR MINT; O43312; -.
DR STRING; 9606.ENSP00000322804; -.
DR GlyGen; O43312; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O43312; -.
DR PhosphoSitePlus; O43312; -.
DR BioMuta; MTSS1; -.
DR EPD; O43312; -.
DR jPOST; O43312; -.
DR MassIVE; O43312; -.
DR MaxQB; O43312; -.
DR PaxDb; O43312; -.
DR PeptideAtlas; O43312; -.
DR PRIDE; O43312; -.
DR ProteomicsDB; 48887; -. [O43312-1]
DR ProteomicsDB; 48888; -. [O43312-2]
DR ProteomicsDB; 48889; -. [O43312-4]
DR Antibodypedia; 27094; 226 antibodies from 29 providers.
DR DNASU; 9788; -.
DR Ensembl; ENST00000325064.9; ENSP00000322804.5; ENSG00000170873.19. [O43312-5]
DR Ensembl; ENST00000378017.7; ENSP00000367256.3; ENSG00000170873.19. [O43312-4]
DR Ensembl; ENST00000431961.6; ENSP00000393606.2; ENSG00000170873.19. [O43312-2]
DR Ensembl; ENST00000518547.6; ENSP00000429064.1; ENSG00000170873.19. [O43312-1]
DR GeneID; 9788; -.
DR KEGG; hsa:9788; -.
DR MANE-Select; ENST00000518547.6; ENSP00000429064.1; NM_014751.6; NP_055566.3.
DR UCSC; uc003yri.4; human. [O43312-1]
DR CTD; 9788; -.
DR DisGeNET; 9788; -.
DR GeneCards; MTSS1; -.
DR HGNC; HGNC:20443; MTSS1.
DR HPA; ENSG00000170873; Low tissue specificity.
DR MIM; 608486; gene.
DR neXtProt; NX_O43312; -.
DR OpenTargets; ENSG00000170873; -.
DR PharmGKB; PA134892011; -.
DR VEuPathDB; HostDB:ENSG00000170873; -.
DR eggNOG; ENOG502QRG4; Eukaryota.
DR GeneTree; ENSGT00950000183156; -.
DR HOGENOM; CLU_004805_2_0_1; -.
DR InParanoid; O43312; -.
DR OMA; KXEEEIS; -.
DR OrthoDB; 529252at2759; -.
DR PhylomeDB; O43312; -.
DR TreeFam; TF320619; -.
DR PathwayCommons; O43312; -.
DR SignaLink; O43312; -.
DR SIGNOR; O43312; -.
DR BioGRID-ORCS; 9788; 16 hits in 1072 CRISPR screens.
DR ChiTaRS; MTSS1; human.
DR EvolutionaryTrace; O43312; -.
DR GeneWiki; MTSS1; -.
DR GenomeRNAi; 9788; -.
DR Pharos; O43312; Tbio.
DR PRO; PR:O43312; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; O43312; protein.
DR Bgee; ENSG00000170873; Expressed in pigmented layer of retina and 209 other tissues.
DR ExpressionAtlas; O43312; baseline and differential.
DR Genevisible; O43312; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR GO; GO:0030139; C:endocytic vesicle; TAS:UniProtKB.
DR GO; GO:0031235; C:intrinsic component of the cytoplasmic side of the plasma membrane; IBA:GO_Central.
DR GO; GO:0001726; C:ruffle; NAS:UniProtKB.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0003785; F:actin monomer binding; IDA: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; IPI:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; TAS:UniProtKB.
DR GO; GO:0034334; P:adherens junction maintenance; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; NAS:UniProtKB.
DR GO; GO:0071498; P:cellular response to fluid shear stress; ISS:UniProtKB.
DR GO; GO:2001013; P:epithelial cell proliferation involved in renal tubule morphogenesis; ISS:UniProtKB.
DR GO; GO:0072102; P:glomerulus morphogenesis; ISS:UniProtKB.
DR GO; GO:0030035; P:microspike assembly; NAS:UniProtKB.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISS:UniProtKB.
DR GO; GO:0072160; P:nephron tubule epithelial cell differentiation; ISS:UniProtKB.
DR GO; GO:0007009; P:plasma membrane organization; IEA:InterPro.
DR GO; GO:0032233; P:positive regulation of actin filament bundle assembly; IBA:GO_Central.
DR GO; GO:0061333; P:renal tubule morphogenesis; ISS:UniProtKB.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; TAS:UniProtKB.
DR DisProt; DP01224; -.
DR Gene3D; 1.20.1270.60; -; 1.
DR IDEAL; IID00257; -.
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; 2.
DR PANTHER; PTHR15708:SF10; PTHR15708:SF10; 2.
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; Tumor suppressor.
FT CHAIN 1..755
FT /note="Protein MTSS 1"
FT /id="PRO_0000096639"
FT DOMAIN 1..250
FT /note="IMD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00668"
FT DOMAIN 727..744
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 139..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 108..155
FT /evidence="ECO:0000255"
FT COMPBIAS 139..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..634
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..701
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 258
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8R1S4"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R1S4"
FT MOD_RES 262
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R1S4"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R1S4"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R1S4"
FT MOD_RES 425
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8R1S4"
FT MOD_RES 603
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8R1S4"
FT MOD_RES 644
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R1S4"
FT MOD_RES 647
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R1S4"
FT VAR_SEQ 1..200
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007420"
FT VAR_SEQ 153
FT /note="K -> KVDTL (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054702"
FT VAR_SEQ 345..426
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007421"
FT VAR_SEQ 346..409
FT /note="LSNGFSHYSLSSESHVGPTGAGLFPHCLPASRLLPRVTSVHLPDYAHYYTIG
FT PGMFPSSQIPSW -> NSSSSASSEASETCQSVSECSSPTSVSSGSTMGAWVSTE (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:9455477"
FT /id="VSP_016216"
FT VARIANT 305
FT /note="N -> I (in dbSNP:rs2303956)"
FT /id="VAR_054010"
FT VARIANT 725
FT /note="T -> A (in dbSNP:rs3829037)"
FT /id="VAR_054011"
FT CONFLICT 586
FT /note="V -> A (in Ref. 2; AK027015)"
FT /evidence="ECO:0000305"
FT CONFLICT 630
FT /note="L -> M (in Ref. 1; AAF15947)"
FT /evidence="ECO:0000305"
FT HELIX 729..737
FT /evidence="ECO:0007829|PDB:2D1K"
SQ SEQUENCE 755 AA; 82251 MW; 76FEE3224CBA9287 CRC64;
MEAVIEKECS ALGGLFQTII SDMKGSYPVW EDFINKAGKL QSQLRTTVVA AAAFLDAFQK
VADMATNTRG GTREIGSALT RMCMRHRSIE AKLRQFSSAL IDCLINPLQE QMEEWKKVAN
QLDKDHAKEY KKARQEIKKK SSDTLKLQKK AKKGRGDIQP QLDSALQDVN DKYLLLEETE
KQAVRKALIE ERGRFCTFIS MLRPVIEEEI SMLGEITHLQ TISEDLKSLT MDPHKLPSSS
EQVILDLKGS DYSWSYQTPP SSPSTTMSRK SSVCSSLNSV NSSDSRSSGS HSHSPSSHYR
YRSSNLAQQA PVRLSSVSSH DSGFISQDAF QSKSPSPMPP EAPNQLSNGF SHYSLSSESH
VGPTGAGLFP HCLPASRLLP RVTSVHLPDY AHYYTIGPGM FPSSQIPSWK DWAKPGPYDQ
PLVNTLQRRK EKREPDPNGG GPTTASGPPA AAEEAQRPRS MTVSAATRPG EEMEACEELA
LALSRGLQLD TQRSSRDSLQ CSSGYSTQTT TPCCSEDTIP SQVSDYDYFS VSGDQEADQQ
EFDKSSTIPR NSDISQSYRR MFQAKRPAST AGLPTTLGPA MVTPGVATIR RTPSTKPSVR
RGTIGAGPIP IKTPVIPVKT PTVPDLPGVL PAPPDGPEER GEHSPESPSV GEGPQGVTSM
PSSMWSGQAS VNPPLPGPKP SIPEEHRQAI PESEAEDQER EPPSATVSPG QIPESDPADL
SPRDTPQGED MLNAIRRGVK LKKTTTNDRS APRFS
