TPM1_MOUSE
ID TPM1_MOUSE Reviewed; 284 AA.
AC P58771; P02558; P19354; P46902; P99034;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Tropomyosin alpha-1 chain;
DE AltName: Full=Alpha-tropomyosin;
DE AltName: Full=Tropomyosin-1;
GN Name=Tpm1; Synonyms=Tpm-1, Tpma;
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] (ISOFORM 1).
RC STRAIN=A2G; TISSUE=Fast-twitch skeletal muscle;
RX PubMed=7522680; DOI=10.1016/0960-8966(94)90021-3;
RA Schleef M., Zuehlke C., Schoeffl F., Jockusch H.;
RT "Subtractive cDNA cloning as a tool to analyse secondary effects of a
RT muscle disease. Characterization of affected genes in the myotonic ADR
RT mouse.";
RL Neuromuscul. Disord. 4:205-217(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=3244365; DOI=10.1128/mcb.8.12.5561-5565.1988;
RA Takenaga K., Nakamura Y., Tokunaga K., Kageyama H., Sakiyama S.;
RT "Isolation and characterization of a cDNA that encodes mouse fibroblast
RT tropomyosin isoform 2.";
RL Mol. Cell. Biol. 8:5561-5565(1988).
RN [3]
RP INDUCTION.
RX PubMed=2521606; DOI=10.1016/0014-4827(89)90080-3;
RA Ryseck R.P., MacDonald-Bravo H., Zerial M., Bravo R.;
RT "Coordinate induction of fibronectin, fibronectin receptor, tropomyosin,
RT and actin genes in serum-stimulated fibroblasts.";
RL Exp. Cell Res. 180:537-545(1989).
RN [4]
RP IDENTIFICATION BY 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 SER-174; SER-186; SER-206;
RP SER-252; SER-271 AND SER-283, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC 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: Binds to actin filaments in muscle and non-muscle cells.
CC Plays a central role, in association with the troponin complex, in the
CC calcium dependent regulation of vertebrate striated muscle contraction.
CC Smooth muscle contraction is regulated by interaction with caldesmon.
CC In non-muscle cells is implicated in stabilizing cytoskeleton actin
CC filaments. {ECO:0000250|UniProtKB:P09493}.
CC -!- SUBUNIT: Homodimer. Heterodimer of an alpha (TPM1, TPM3 or TPM4) and a
CC beta (TPM2) chain. Interacts with HRG (via the HRR domain); the
CC interaction contributes to the antiangiogenic properties of the
CC histidine/proline-rich region (HRR) of HRG. Interacts (via N-terminus)
CC with LMOD2 (via N-terminus) and TMOD1 (via N-terminus).
CC {ECO:0000250|UniProtKB:P04268, ECO:0000250|UniProtKB:P04692,
CC ECO:0000250|UniProtKB:P09493}.
CC -!- INTERACTION:
CC P58771; P68135: ACTA1; Xeno; NbExp=2; IntAct=EBI-298478, EBI-367540;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P04692}. Note=Associates with F-actin stress
CC fibers. {ECO:0000250|UniProtKB:P04692}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=Skeletal muscle;
CC IsoId=P58771-1; Sequence=Displayed;
CC Name=2; Synonyms=Fibroblast;
CC IsoId=P58771-2; Sequence=VSP_006580;
CC -!- INDUCTION: Induced in stimulated quiescent cells.
CC {ECO:0000269|PubMed:2521606}.
CC -!- DOMAIN: The molecule is in a coiled coil structure that is formed by 2
CC polypeptide chains. The sequence exhibits a prominent seven-residues
CC periodicity.
CC -!- PTM: Phosphorylated at Ser-283 by DAPK1 in response to oxidative stress
CC and this phosphorylation enhances stress fiber formation in endothelial
CC cells. {ECO:0000250}.
CC -!- MISCELLANEOUS: The sequences of cardiac and skeletal muscles are
CC identical.
CC -!- SIMILARITY: Belongs to the tropomyosin family. {ECO:0000305}.
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DR EMBL; X64831; CAA46043.1; -; mRNA.
DR EMBL; M22479; AAA40483.1; -; mRNA.
DR CCDS; CCDS23311.1; -. [P58771-2]
DR CCDS; CCDS52845.1; -. [P58771-1]
DR PIR; A31380; A60597.
DR RefSeq; NP_001157720.1; NM_001164248.1. [P58771-1]
DR RefSeq; NP_077745.2; NM_024427.4. [P58771-2]
DR PDB; 7NEP; EM; 10.20 A; P/Q/T/U=11-261.
DR PDBsum; 7NEP; -.
DR AlphaFoldDB; P58771; -.
DR SMR; P58771; -.
DR BioGRID; 204291; 108.
DR DIP; DIP-300N; -.
DR IntAct; P58771; 107.
DR MINT; P58771; -.
DR STRING; 10090.ENSMUSP00000109337; -.
DR iPTMnet; P58771; -.
DR PhosphoSitePlus; P58771; -.
DR SWISS-2DPAGE; P58771; -.
DR CPTAC; non-CPTAC-3624; -.
DR EPD; P58771; -.
DR jPOST; P58771; -.
DR PeptideAtlas; P58771; -.
DR PRIDE; P58771; -.
DR ProteomicsDB; 259060; -. [P58771-1]
DR ProteomicsDB; 259061; -. [P58771-2]
DR Antibodypedia; 635; 332 antibodies from 39 providers.
DR DNASU; 22003; -.
DR Ensembl; ENSMUST00000113685; ENSMUSP00000109315; ENSMUSG00000032366. [P58771-1]
DR Ensembl; ENSMUST00000113707; ENSMUSP00000109337; ENSMUSG00000032366. [P58771-2]
DR GeneID; 22003; -.
DR KEGG; mmu:22003; -.
DR UCSC; uc009qfq.2; mouse. [P58771-1]
DR CTD; 7168; -.
DR MGI; MGI:98809; Tpm1.
DR VEuPathDB; HostDB:ENSMUSG00000032366; -.
DR eggNOG; KOG1003; Eukaryota.
DR GeneTree; ENSGT01030000234542; -.
DR HOGENOM; CLU_055027_0_0_1; -.
DR InParanoid; P58771; -.
DR PhylomeDB; P58771; -.
DR TreeFam; TF351519; -.
DR Reactome; R-MMU-390522; Striated Muscle Contraction.
DR Reactome; R-MMU-445355; Smooth Muscle Contraction.
DR BioGRID-ORCS; 22003; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Tpm1; mouse.
DR PRO; PR:P58771; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P58771; protein.
DR Bgee; ENSMUSG00000032366; Expressed in tarsal region and 281 other tissues.
DR ExpressionAtlas; P58771; baseline and differential.
DR Genevisible; P58771; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0032059; C:bleb; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005862; C:muscle thin filament tropomyosin; TAS:MGI.
DR GO; GO:0030016; C:myofibril; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0032587; C:ruffle membrane; ISO:MGI.
DR GO; GO:0001725; C:stress fiber; ISO:MGI.
DR GO; GO:0003779; F:actin binding; ISO:MGI.
DR GO; GO:0051015; F:actin filament binding; IDA:MGI.
DR GO; GO:0008092; F:cytoskeletal protein binding; ISO:MGI.
DR GO; GO:0097718; F:disordered domain specific binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:MGI.
DR GO; GO:0051693; P:actin filament capping; ISO:MGI.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0060048; P:cardiac muscle contraction; IMP:BHF-UCL.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR GO; GO:0030049; P:muscle filament sliding; ISO:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
DR GO; GO:1904753; P:negative regulation of vascular associated smooth muscle cell migration; ISO:MGI.
DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; ISO:MGI.
DR GO; GO:0045785; P:positive regulation of cell adhesion; ISO:MGI.
DR GO; GO:0003065; P:positive regulation of heart rate by epinephrine; IMP:BHF-UCL.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:MGI.
DR GO; GO:0043462; P:regulation of ATP-dependent activity; ISO:MGI.
DR GO; GO:0008360; P:regulation of cell shape; ISO:MGI.
DR GO; GO:0031529; P:ruffle organization; ISO:MGI.
DR GO; GO:0045214; P:sarcomere organization; ISO:MGI.
DR GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IMP:BHF-UCL.
DR GO; GO:0042060; P:wound healing; ISO:MGI.
DR InterPro; IPR000533; Tropomyosin.
DR Pfam; PF00261; Tropomyosin; 1.
DR PRINTS; PR00194; TROPOMYOSIN.
DR PROSITE; PS00326; TROPOMYOSIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Alternative splicing;
KW Coiled coil; Cytoplasm; Cytoskeleton; Muscle protein; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..284
FT /note="Tropomyosin alpha-1 chain"
FT /id="PRO_0000205621"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1..284
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P09493"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04692"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 261
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P04692"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 258..284
FT /note="DELYAQKLKYKAISEELDHALNDMTSI -> EKVAHAKEENLSMHQMLDQTL
FT LELNNM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:3244365"
FT /id="VSP_006580"
SQ SEQUENCE 284 AA; 32681 MW; E25609F597A72F4D CRC64;
MDAIKKKMQM LKLDKENALD RAEQAEADKK AAEDRSKQLE DELVSLQKKL KGTEDELDKY
SEALKDAQEK LELAEKKATD AEADVASLNR RIQLVEEELD RAQERLATAL QKLEEAEKAA
DESERGMKVI ESRAQKDEEK MEIQEIQLKE AKHIAEDADR KYEEVARKLV IIESDLERAE
ERAELSEGKC AELEEELKTV TNNLKSLEAQ AEKYSQKEDK YEEEIKVLSD KLKEAETRAE
FAERSVTKLE KSIDDLEDEL YAQKLKYKAI SEELDHALND MTSI
