TPM1_RAT
ID TPM1_RAT Reviewed; 284 AA.
AC P04692; P06469; P18342; P18343; P18344; P19354; Q53X09; Q63582; Q63608;
AC Q63609;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 3.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Tropomyosin alpha-1 chain;
DE AltName: Full=Alpha-tropomyosin;
DE AltName: Full=Tropomyosin-1;
GN Name=Tpm1; Synonyms=Alpha-tm, Tpma;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX PubMed=3838802; DOI=10.1038/315067a0;
RA Ruiz-Opazo N., Weinberger J., Nadal-Ginard B.;
RT "Comparison of alpha-tropomyosin sequences from smooth and striated
RT muscle.";
RL Nature 315:67-70(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RX PubMed=3558368; DOI=10.1016/s0021-9258(18)61260-8;
RA Ruiz-Opazo N., Nadal-Ginard B.;
RT "Alpha-tropomyosin gene organization. Alternative splicing of duplicated
RT isotype-specific exons accounts for the production of smooth and striated
RT muscle isoforms.";
RL J. Biol. Chem. 262:4755-4765(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RX PubMed=3352602; DOI=10.1128/mcb.8.2.679-694.1988;
RA Wieczorek D.F., Smith C.W., Nadal-Ginard B.;
RT "The rat alpha-tropomyosin gene generates a minimum of six different mRNAs
RT coding for striated, smooth, and nonmuscle isoforms by alternative
RT splicing.";
RL Mol. Cell. Biol. 8:679-694(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 3; 4 AND 5).
RC TISSUE=Brain;
RX PubMed=2320008; DOI=10.1128/mcb.10.4.1729-1742.1990;
RA Lees-Miller J.P., Goodwin L.O., Helfman D.M.;
RT "Three novel brain tropomyosin isoforms are expressed from the rat alpha-
RT tropomyosin gene through the use of alternative promoters and alternative
RT RNA processing.";
RL Mol. Cell. Biol. 10:1729-1742(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 6; 7 AND 8).
RX PubMed=2022655; DOI=10.1016/s0021-9258(18)92990-x;
RA Goodwin L.O., Lees-Miller J.P., Leonard M.A., Cheley S.B., Helfman D.M.;
RT "Four fibroblast tropomyosin isoforms are expressed from the rat alpha-
RT tropomyosin gene via alternative RNA splicing and the use of two
RT promoters.";
RL J. Biol. Chem. 266:8408-8415(1991).
RN [6]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=6179945; DOI=10.1016/s0021-9258(18)33935-8;
RA Garfinkel L.I., Periasamy M., Nadal-Ginard B.;
RT "Cloning and characterization of cDNA sequences corresponding to myosin
RT light chains 1, 2, and 3, troponin-C, troponin-T, alpha-tropomyosin, and
RT alpha-actin.";
RL J. Biol. Chem. 257:11078-11086(1982).
RN [7]
RP PROTEIN SEQUENCE OF 92-101; 141-149; 218-226 AND 251-270, PARTIAL PROTEIN
RP SEQUENCE (ISOFORMS 4/5/7/8), AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Diao W., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [8]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=7568216; DOI=10.1073/pnas.92.21.9776;
RA Gimona M., Watakabe A., Helfman D.M.;
RT "Specificity of dimer formation in tropomyosins: influence of alternatively
RT spliced exons on homodimer and heterodimer assembly.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:9776-9780(1995).
RN [9]
RP FUNCTION, AND SUBUNIT.
RX PubMed=22812662; DOI=10.1021/bi300340r;
RA Kalyva A., Schmidtmann A., Geeves M.A.;
RT "In vitro formation and characterization of the skeletal muscle alpha.beta
RT tropomyosin heterodimers.";
RL Biochemistry 51:6388-6399(2012).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-174; SER-252 AND
RP TYR-261, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Binds to actin filaments in muscle and non-muscle cells
CC (PubMed:7568216, PubMed:22812662). Plays a central role, in association
CC with the troponin complex, in the calcium dependent regulation of
CC vertebrate striated muscle contraction (PubMed:22812662). Smooth muscle
CC contraction is regulated by interaction with caldesmon. In non-muscle
CC cells is implicated in stabilizing cytoskeleton actin filaments.
CC {ECO:0000269|PubMed:22812662, ECO:0000269|PubMed:7568216}.
CC -!- SUBUNIT: Homodimer (PubMed:7568216, PubMed:22812662). Heterodimer of an
CC alpha (TPM1, TPM3 or TPM4) and a beta (TPM2) chain (PubMed:7568216,
CC PubMed:22812662). 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 (By similarity). Interacts
CC (via N-terminus) with LMOD2 (via N-terminus) and TMOD1 (via N-terminus)
CC (By similarity). {ECO:0000250|UniProtKB:P04268,
CC ECO:0000250|UniProtKB:P09493, ECO:0000269|PubMed:22812662,
CC ECO:0000269|PubMed:7568216}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:7568216}. Note=Associates with F-actin stress
CC fibers (PubMed:7568216). {ECO:0000269|PubMed:7568216}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=Skeletal muscle;
CC IsoId=P04692-1; Sequence=Displayed;
CC Name=2; Synonyms=Smooth muscle;
CC IsoId=P04692-2; Sequence=VSP_006582, VSP_006584;
CC Name=3; Synonyms=Brain TMBr-1;
CC IsoId=P04692-3; Sequence=VSP_006585;
CC Name=4; Synonyms=Brain TMBr-2;
CC IsoId=P04692-4; Sequence=VSP_006581, VSP_006586;
CC Name=5; Synonyms=Brain TMBr-3;
CC IsoId=P04692-5; Sequence=VSP_006581, VSP_006585;
CC Name=6; Synonyms=Fibroblast TM-2;
CC IsoId=P04692-6; Sequence=VSP_006584;
CC Name=7; Synonyms=Fibroblast 5a;
CC IsoId=P04692-7; Sequence=VSP_006581, VSP_006584;
CC Name=8; Synonyms=Fibroblast 5b;
CC IsoId=P04692-8; Sequence=VSP_006581, VSP_006583, VSP_006584;
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 -!- SIMILARITY: Belongs to the tropomyosin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION: [Isoform 2]:
CC Sequence=CAA26258.1; Type=Miscellaneous discrepancy; Note=miscellaneous discrepancy.; Evidence={ECO:0000305};
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DR EMBL; M15474; AAA21801.1; -; Genomic_DNA.
DR EMBL; M15472; AAA21801.1; JOINED; Genomic_DNA.
DR EMBL; M15473; AAA21801.1; JOINED; Genomic_DNA.
DR EMBL; M16432; AAA21801.1; JOINED; Genomic_DNA.
DR EMBL; M16433; AAA21801.1; JOINED; Genomic_DNA.
DR EMBL; M18135; AAA21803.1; ALT_TERM; Genomic_DNA.
DR EMBL; M16432; AAA21803.1; JOINED; Genomic_DNA.
DR EMBL; M15472; AAA21803.1; JOINED; Genomic_DNA.
DR EMBL; M16433; AAA21803.1; JOINED; Genomic_DNA.
DR EMBL; M15473; AAA21803.1; JOINED; Genomic_DNA.
DR EMBL; M18135; AAA21804.1; -; Genomic_DNA.
DR EMBL; M16432; AAA21804.1; JOINED; Genomic_DNA.
DR EMBL; M16433; AAA21804.1; JOINED; Genomic_DNA.
DR EMBL; M18135; AAA21805.1; -; Genomic_DNA.
DR EMBL; M16432; AAA21805.1; JOINED; Genomic_DNA.
DR EMBL; M15472; AAA21805.1; JOINED; Genomic_DNA.
DR EMBL; M16433; AAA21805.1; JOINED; Genomic_DNA.
DR EMBL; X02411; CAA26258.1; ALT_SEQ; mRNA.
DR EMBL; M34135; AAA42252.1; -; mRNA.
DR EMBL; M34134; AAA42253.1; -; mRNA.
DR EMBL; M34136; AAA42254.1; -; mRNA.
DR EMBL; M34137; AAA40773.1; -; Genomic_DNA.
DR EMBL; M34138; AAA40774.1; -; Genomic_DNA.
DR EMBL; M60666; AAA42290.1; -; mRNA.
DR EMBL; M60668; AAA18098.1; -; mRNA.
DR EMBL; M60669; AAA18099.1; -; mRNA.
DR EMBL; X02412; CAA26259.1; -; mRNA.
DR PIR; A34787; A34787.
DR PIR; A39816; A39816.
DR PIR; B27407; B27407.
DR PIR; B34787; B34787.
DR PIR; C34787; C34787.
DR PIR; C39816; C39816.
DR PIR; D39816; D39816.
DR RefSeq; NP_001029241.1; NM_001034069.1.
DR RefSeq; NP_001029244.1; NM_001034072.1. [P04692-3]
DR RefSeq; NP_001029245.1; NM_001034073.1.
DR RefSeq; NP_001029246.1; NM_001034074.1.
DR RefSeq; NP_001029247.1; NM_001034075.1.
DR RefSeq; NP_001288265.1; NM_001301336.1. [P04692-1]
DR RefSeq; NP_001288665.1; NM_001301736.1. [P04692-5]
DR RefSeq; NP_062004.1; NM_019131.2. [P04692-4]
DR PDB; 1IHQ; NMR; -; A/B=206-209.
DR PDB; 1KQL; X-ray; 2.70 A; A/B=254-284.
DR PDB; 1MV4; NMR; -; A/B=251-284.
DR PDB; 1TMZ; NMR; -; A/B=1-14.
DR PDB; 2B9C; X-ray; 2.30 A; A/B=89-208.
DR PDB; 2G9J; NMR; -; A/B=1-14, C/D=251-284.
DR PDB; 3AZD; X-ray; 0.98 A; A/B=206-209.
DR PDBsum; 1IHQ; -.
DR PDBsum; 1KQL; -.
DR PDBsum; 1MV4; -.
DR PDBsum; 1TMZ; -.
DR PDBsum; 2B9C; -.
DR PDBsum; 2G9J; -.
DR PDBsum; 3AZD; -.
DR AlphaFoldDB; P04692; -.
DR BMRB; P04692; -.
DR SMR; P04692; -.
DR BioGRID; 246968; 6.
DR DIP; DIP-29020N; -.
DR IntAct; P04692; 3.
DR STRING; 10116.ENSRNOP00000024493; -.
DR iPTMnet; P04692; -.
DR PhosphoSitePlus; P04692; -.
DR SwissPalm; P04692; -.
DR jPOST; P04692; -.
DR PRIDE; P04692; -.
DR Ensembl; ENSRNOT00000048044; ENSRNOP00000048499; ENSRNOG00000018184. [P04692-1]
DR GeneID; 24851; -.
DR KEGG; rno:24851; -.
DR CTD; 7168; -.
DR RGD; 3898; Tpm1.
DR eggNOG; KOG1003; Eukaryota.
DR GeneTree; ENSGT01030000234542; -.
DR HOGENOM; CLU_055027_0_0_1; -.
DR InParanoid; P04692; -.
DR PhylomeDB; P04692; -.
DR TreeFam; TF351519; -.
DR Reactome; R-RNO-390522; Striated Muscle Contraction.
DR Reactome; R-RNO-445355; Smooth Muscle Contraction.
DR EvolutionaryTrace; P04692; -.
DR PRO; PR:P04692; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000018184; Expressed in skeletal muscle tissue and 20 other tissues.
DR ExpressionAtlas; P04692; baseline and differential.
DR Genevisible; P04692; RN.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0032059; C:bleb; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0030016; C:myofibril; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0032587; C:ruffle membrane; ISO:RGD.
DR GO; GO:0001725; C:stress fiber; ISO:RGD.
DR GO; GO:0003779; F:actin binding; IDA:RGD.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0008092; F:cytoskeletal protein binding; ISO:RGD.
DR GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; IDA:RGD.
DR GO; GO:0051693; P:actin filament capping; IDA:RGD.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0060048; P:cardiac muscle contraction; IDA:RGD.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR GO; GO:0030049; P:muscle filament sliding; IDA:BHF-UCL.
DR GO; GO:0030336; P:negative regulation of cell migration; IGI:BHF-UCL.
DR GO; GO:1904753; P:negative regulation of vascular associated smooth muscle cell migration; ISO:RGD.
DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; ISO:RGD.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; IDA:BHF-UCL.
DR GO; GO:0045785; P:positive regulation of cell adhesion; IGI:BHF-UCL.
DR GO; GO:0003065; P:positive regulation of heart rate by epinephrine; ISO:RGD.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IGI:BHF-UCL.
DR GO; GO:0043462; P:regulation of ATP-dependent activity; IDA:RGD.
DR GO; GO:0008360; P:regulation of cell shape; ISO:RGD.
DR GO; GO:0031529; P:ruffle organization; IGI:BHF-UCL.
DR GO; GO:0045214; P:sarcomere organization; ISO:RGD.
DR GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; ISO:RGD.
DR GO; GO:0042060; P:wound healing; IGI:BHF-UCL.
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; Direct protein sequencing;
KW Muscle protein; Phosphoprotein; Reference proteome.
FT CHAIN 1..284
FT /note="Tropomyosin alpha-1 chain"
FT /id="PRO_0000205624"
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 MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P09493"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P58771"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P58771"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 261
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P58771"
FT MOD_RES 283
FT /note="Phosphoserine; by DAPK1"
FT /evidence="ECO:0000250|UniProtKB:P09493"
FT VAR_SEQ 1..80
FT /note="MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKG
FT TEDELDKYSEALKDAQEKLELAEKKATD -> MAGSSSLEAVRRKIRSLQEQADAAEER
FT AGSLQRELDQERKLRET (in isoform 4, isoform 5, isoform 7 and
FT isoform 8)"
FT /evidence="ECO:0000303|PubMed:2022655,
FT ECO:0000303|PubMed:2320008"
FT /id="VSP_006581"
FT VAR_SEQ 41..80
FT /note="DELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATD -> EDISAKEK
FT LLRASEDERDRVLEELHKAEDSLLAADETAAK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:3838802"
FT /id="VSP_006582"
FT VAR_SEQ 189..212
FT /note="KCAELEEELKTVTNNLKSLEAQAE -> QVRQLEEQLRIMDQTLKALMAAED
FT (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:2022655"
FT /id="VSP_006583"
FT VAR_SEQ 258..284
FT /note="DELYAQKLKYKAISEELDHALNDMTSI -> EKVAHAKEENLSMHQMLHQTL
FT LELNNM (in isoform 2, isoform 6, isoform 7 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:2022655,
FT ECO:0000303|PubMed:3838802"
FT /id="VSP_006584"
FT VAR_SEQ 259..284
FT /note="ELYAQKLKYKAISEELDHALNDMTSI -> QLYHQLEQNRRLTNELKLALNE
FT D (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:2320008"
FT /id="VSP_006585"
FT VAR_SEQ 259..284
FT /note="ELYAQKLKYKAISEELDHALNDMTSI -> KFLCFSPPKTPSSSRMSHLSEL
FT CICLLSS (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:2320008"
FT /id="VSP_006586"
FT CONFLICT 52
FT /note="G -> A (in Ref. 4; AAA42252)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="N -> K (in Ref. 2; AAA21801 and 3; AAA21805)"
FT /evidence="ECO:0000305"
FT HELIX 2..14
FT /evidence="ECO:0007829|PDB:2G9J"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:2B9C"
FT HELIX 100..103
FT /evidence="ECO:0007829|PDB:2B9C"
FT TURN 104..107
FT /evidence="ECO:0007829|PDB:2B9C"
FT HELIX 108..123
FT /evidence="ECO:0007829|PDB:2B9C"
FT HELIX 125..209
FT /evidence="ECO:0007829|PDB:2B9C"
FT TURN 210..213
FT /evidence="ECO:0007829|PDB:2B9C"
FT HELIX 214..225
FT /evidence="ECO:0007829|PDB:2B9C"
FT HELIX 254..281
FT /evidence="ECO:0007829|PDB:1MV4"
FT CONFLICT P04692-2:260
FT /note="V -> G (in Ref. 1; CAA26258)"
FT /evidence="ECO:0000305"
FT CONFLICT P04692-2:275
FT /note="H -> D (in Ref. 1; CAA26258)"
FT /evidence="ECO:0000305"
FT CONFLICT P04692-6:275
FT /note="H -> D (in Ref. 5; AAA42290)"
FT /evidence="ECO:0000305"
FT CONFLICT P04692-7:239
FT /note="H -> D (in Ref. 5; AAA18098)"
FT /evidence="ECO:0000305"
FT CONFLICT P04692-8:239
FT /note="H -> D (in Ref. 5; AAA18099)"
FT /evidence="ECO:0000305"
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
