ID   TMOD3_MOUSE             Reviewed;         352 AA.
AC   Q9JHJ0; Q3TIT1;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Tropomodulin-3;
DE   AltName: Full=Ubiquitous tropomodulin;
DE            Short=U-Tmod;
GN   Name=Tmod3;
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 [MRNA].
RA   Conley C.A., Fowler V.M.;
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10662549; DOI=10.1006/geno.1999.6061;
RA   Cox P.R., Zoghbi H.Y.;
RT   "Sequencing, expression analysis, and mapping of three unique human
RT   tropomodulin genes and their mouse orthologs.";
RL   Genomics 63:97-107(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Liver, and Placenta;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, Lung, Pancreas, Spleen, and Testis;
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: Blocks the elongation and depolymerization of the actin
CC       filaments at the pointed end. The Tmod/TM complex contributes to the
CC       formation of the short actin protofilament, which in turn defines the
CC       geometry of the membrane skeleton (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Binds to the N-terminus of tropomyosin and to actin.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- SIMILARITY: Belongs to the tropomodulin family. {ECO:0000305}.
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DR   EMBL; AF237630; AAF45298.1; -; mRNA.
DR   EMBL; AF177172; AAF31671.1; -; mRNA.
DR   EMBL; AK050372; BAC34216.1; -; mRNA.
DR   EMBL; AK167723; BAE39765.1; -; mRNA.
DR   EMBL; BC082595; AAH82595.1; -; mRNA.
DR   CCDS; CCDS23344.1; -.
DR   RefSeq; NP_058659.1; NM_016963.2.
DR   AlphaFoldDB; Q9JHJ0; -.
DR   SMR; Q9JHJ0; -.
DR   BioGRID; 206138; 95.
DR   IntAct; Q9JHJ0; 92.
DR   MINT; Q9JHJ0; -.
DR   STRING; 10090.ENSMUSP00000072087; -.
DR   iPTMnet; Q9JHJ0; -.
DR   PhosphoSitePlus; Q9JHJ0; -.
DR   EPD; Q9JHJ0; -.
DR   jPOST; Q9JHJ0; -.
DR   MaxQB; Q9JHJ0; -.
DR   PaxDb; Q9JHJ0; -.
DR   PRIDE; Q9JHJ0; -.
DR   ProteomicsDB; 259041; -.
DR   Antibodypedia; 978; 156 antibodies from 28 providers.
DR   DNASU; 50875; -.
DR   Ensembl; ENSMUST00000072232; ENSMUSP00000072087; ENSMUSG00000058587.
DR   GeneID; 50875; -.
DR   KEGG; mmu:50875; -.
DR   UCSC; uc009qsi.1; mouse.
DR   CTD; 29766; -.
DR   MGI; MGI:1355315; Tmod3.
DR   VEuPathDB; HostDB:ENSMUSG00000058587; -.
DR   eggNOG; KOG3735; Eukaryota.
DR   GeneTree; ENSGT00940000158280; -.
DR   HOGENOM; CLU_031052_0_1_1; -.
DR   InParanoid; Q9JHJ0; -.
DR   OMA; NTHVKHF; -.
DR   OrthoDB; 1025132at2759; -.
DR   PhylomeDB; Q9JHJ0; -.
DR   TreeFam; TF315841; -.
DR   Reactome; R-MMU-390522; Striated Muscle Contraction.
DR   Reactome; R-MMU-9013418; RHOBTB2 GTPase cycle.
DR   Reactome; R-MMU-9696264; RND3 GTPase cycle.
DR   BioGRID-ORCS; 50875; 3 hits in 71 CRISPR screens.
DR   ChiTaRS; Tmod3; mouse.
DR   PRO; PR:Q9JHJ0; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q9JHJ0; protein.
DR   Bgee; ENSMUSG00000058587; Expressed in thoracic mammary gland and 286 other tissues.
DR   ExpressionAtlas; Q9JHJ0; baseline and differential.
DR   Genevisible; Q9JHJ0; MM.
DR   GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR   GO; GO:0031941; C:filamentous actin; ISO:MGI.
DR   GO; GO:0030027; C:lamellipodium; ISO:MGI.
DR   GO; GO:0030016; C:myofibril; IBA:GO_Central.
DR   GO; GO:0001726; C:ruffle; ISO:MGI.
DR   GO; GO:0005865; C:striated muscle thin filament; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0051011; F:microtubule minus-end binding; ISO:MGI.
DR   GO; GO:0005523; F:tropomyosin binding; IDA:MGI.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IMP:MGI.
DR   GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR   GO; GO:0048821; P:erythrocyte development; IMP:MGI.
DR   GO; GO:0044772; P:mitotic cell cycle phase transition; IMP:MGI.
DR   GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR   GO; GO:0030239; P:myofibril assembly; IBA:GO_Central.
DR   GO; GO:0051694; P:pointed-end actin filament capping; ISO:MGI.
DR   GO; GO:1901992; P:positive regulation of mitotic cell cycle phase transition; IMP:MGI.
DR   Gene3D; 3.80.10.10; -; 1.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR004934; TMOD.
DR   InterPro; IPR030133; TMOD3.
DR   PANTHER; PTHR10901; PTHR10901; 1.
DR   PANTHER; PTHR10901:SF18; PTHR10901:SF18; 1.
DR   Pfam; PF03250; Tropomodulin; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome.
FT   CHAIN           1..352
FT                   /note="Tropomodulin-3"
FT                   /id="PRO_0000186135"
FT   MOD_RES         25
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
SQ   SEQUENCE   352 AA;  39503 MW;  6F8602C74C2AEF9C CRC64;
     MALPFRKDLG DYKDLDEDEL LGKLSESELK QLETVLDDLD PENALLPAGF RQKNQTSKSA
     TGPFDRERLL SYLEKQALEH KDRDDYVPYT GEKKGKIFIP KQKPAQTLTE ETISLDPELE
     EALTSASDTE LCDLAAILGM HNLIADTPFC DVLGSSNGVN QERFPNVVKG EKILPVFDEP
     PNPTNVEESL KRIRENDARL VEVNLNNIKN IPIPTLKDFA KTLEANTHVK HFSLAATRSN
     DPVAVAFADM LKVNKTLKSL NMESNFITGA GVLALIDALR DNETLMELKI DNQRQQLGTS
     VELEMAKMLE ENTNILKFGY QFTQQGPRTR AANAITKNND LVRKRRIEGD HQ