TMOD1_MOUSE
ID TMOD1_MOUSE Reviewed; 359 AA.
AC P49813; Q3KP84; Q9ERR9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Tropomodulin-1;
DE AltName: Full=Erythrocyte tropomodulin;
DE Short=E-Tmod;
GN Name=Tmod1; Synonyms=Tmod;
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].
RX PubMed=7851652; DOI=10.1006/dbio.1995.1026;
RA Ito M., Swanson B., Sussman M.A., Kedes L., Lyons G.;
RT "Cloning of tropomodulin cDNA and localization of gene transcripts during
RT mouse embryogenesis.";
RL Dev. Biol. 167:317-328(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11054557; DOI=10.1016/s0378-1119(00)00327-9;
RA Chu X., Thompson D., Yee L.J., Sung L.A.;
RT "Genomic organization of mouse and human erythrocyte tropomodulin genes
RT encoding the pointed end capping protein for the actin filaments.";
RL Gene 256:271-281(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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: 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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P28289}. Note=In myofibrils with sarcomeric
CC structure, localizes to the pointed end of actin thin filaments.
CC {ECO:0000250|UniProtKB:P28289}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the erythrocyte, heart and
CC skeletal muscle.
CC -!- SIMILARITY: Belongs to the tropomodulin family. {ECO:0000305}.
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DR EMBL; S76831; AAB33388.1; -; mRNA.
DR EMBL; AF287746; AAF91487.1; -; Genomic_DNA.
DR EMBL; AF287738; AAF91487.1; JOINED; Genomic_DNA.
DR EMBL; AF287739; AAF91487.1; JOINED; Genomic_DNA.
DR EMBL; AF287740; AAF91487.1; JOINED; Genomic_DNA.
DR EMBL; AF287741; AAF91487.1; JOINED; Genomic_DNA.
DR EMBL; AF287742; AAF91487.1; JOINED; Genomic_DNA.
DR EMBL; AF287743; AAF91487.1; JOINED; Genomic_DNA.
DR EMBL; AF287744; AAF91487.1; JOINED; Genomic_DNA.
DR EMBL; AF287745; AAF91487.1; JOINED; Genomic_DNA.
DR EMBL; AL732615; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466565; EDL02383.1; -; Genomic_DNA.
DR EMBL; BC106849; AAI06850.1; -; mRNA.
DR EMBL; BC106850; AAI06851.1; -; mRNA.
DR CCDS; CCDS18143.1; -.
DR RefSeq; NP_068683.1; NM_021883.2.
DR AlphaFoldDB; P49813; -.
DR SMR; P49813; -.
DR BioGRID; 204233; 13.
DR IntAct; P49813; 2.
DR MINT; P49813; -.
DR STRING; 10090.ENSMUSP00000103402; -.
DR iPTMnet; P49813; -.
DR PhosphoSitePlus; P49813; -.
DR MaxQB; P49813; -.
DR PaxDb; P49813; -.
DR PeptideAtlas; P49813; -.
DR PRIDE; P49813; -.
DR ProteomicsDB; 259266; -.
DR TopDownProteomics; P49813; -.
DR Antibodypedia; 28841; 296 antibodies from 28 providers.
DR DNASU; 21916; -.
DR Ensembl; ENSMUST00000107773; ENSMUSP00000103402; ENSMUSG00000028328.
DR GeneID; 21916; -.
DR KEGG; mmu:21916; -.
DR UCSC; uc008ste.1; mouse.
DR CTD; 7111; -.
DR MGI; MGI:98775; Tmod1.
DR VEuPathDB; HostDB:ENSMUSG00000028328; -.
DR eggNOG; KOG3735; Eukaryota.
DR GeneTree; ENSGT00940000158695; -.
DR HOGENOM; CLU_031052_0_0_1; -.
DR InParanoid; P49813; -.
DR OMA; FHAENQR; -.
DR OrthoDB; 1025132at2759; -.
DR PhylomeDB; P49813; -.
DR TreeFam; TF315841; -.
DR Reactome; R-MMU-390522; Striated Muscle Contraction.
DR BioGRID-ORCS; 21916; 3 hits in 72 CRISPR screens.
DR PRO; PR:P49813; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P49813; protein.
DR Bgee; ENSMUSG00000028328; Expressed in quadriceps femoris and 243 other tissues.
DR ExpressionAtlas; P49813; baseline and differential.
DR Genevisible; P49813; MM.
DR GO; GO:0005884; C:actin filament; ISS:UniProtKB.
DR GO; GO:0008180; C:COP9 signalosome; ISO:MGI.
DR GO; GO:0030863; C:cortical cytoskeleton; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0030016; C:myofibril; IDA:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0030017; C:sarcomere; IDA:MGI.
DR GO; GO:0005865; C:striated muscle thin filament; ISO:MGI.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0005523; F:tropomyosin binding; IDA:MGI.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
DR GO; GO:0070307; P:lens fiber cell development; IGI:CACAO.
DR GO; GO:0006936; P:muscle contraction; IMP:MGI.
DR GO; GO:0030239; P:myofibril assembly; IMP:MGI.
DR GO; GO:0051694; P:pointed-end actin filament capping; IEA:InterPro.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR004934; TMOD.
DR InterPro; IPR030135; TMOD1.
DR PANTHER; PTHR10901; PTHR10901; 1.
DR PANTHER; PTHR10901:SF8; PTHR10901:SF8; 1.
DR Pfam; PF03250; Tropomodulin; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Cytoplasm; Cytoskeleton; Reference proteome.
FT CHAIN 1..359
FT /note="Tropomodulin-1"
FT /id="PRO_0000186129"
FT REGION 36..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 39..138
FT /note="Tropomyosin-binding"
FT /evidence="ECO:0000255"
FT CONFLICT 352
FT /note="I -> M (in Ref. 1; AAB33388)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 359 AA; 40466 MW; EAE340B83048823B CRC64;
MSYRRELEKY RDLDEDEILG ALTEEELRTL ENELDELDPD NALLPAGLRQ KDQTTKAPTG
PFKREELLDH LEKQAKEFKD REDLVPYTGE KRGKVWVPKQ KPMDPVLESV TLEPELEEAL
ANASDAELCD IAAILGMHTL MSNQQYYQAL GSSSIVNKEG LNSVIKPTQY KPVPDEEPNS
TDVEETLERI KNNDPELEEV NLNNIRNIPI PTLKAYAEAL KENSYVKKFS IVGTRSNDPV
AFALAEMLKV NKVLKTLNVE SNFISGAGIL RLVEALPHNT SLVELKIDNQ SQPLGNKVEM
EIVNMLEKNT TLLKFGYHFT QQGPRLRASN AMMSNNDLVR KRRLADLTGP IIPKCRSGV
