TPM2_RAT
ID TPM2_RAT Reviewed; 284 AA.
AC P58775; P02560; P06395;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Tropomyosin beta chain;
DE AltName: Full=Beta-tropomyosin;
DE AltName: Full=Tropomyosin-2;
GN Name=Tpm2;
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 [GENOMIC DNA] (ISOFORMS 1 AND 2).
RX PubMed=3840484; DOI=10.1016/s0021-9258(17)38588-5;
RA Yamawaki-Kataoka Y., Helfman D.M.;
RT "Rat embryonic fibroblast tropomyosin 1. cDNA and complete primary amino
RT acid sequence.";
RL J. Biol. Chem. 260:14440-14445(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
RX PubMed=2432392; DOI=10.1128/mcb.6.11.3582-3595.1986;
RA Helfman D.M., Cheley S., Kuismanen E., Finn L.A., Yamawaki-Kataoka Y.;
RT "Nonmuscle and muscle tropomyosin isoforms are expressed from a single gene
RT by alternative RNA splicing and polyadenylation.";
RL Mol. Cell. Biol. 6:3582-3595(1986).
RN [3]
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 [4]
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61; SER-206; SER-215;
RP THR-252; TYR-261 AND SER-271, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
RP SER-210 (ISOFORM 2), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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. The
CC non-muscle isoform may have a role in agonist-mediated receptor
CC internalization (By similarity). {ECO:0000250|UniProtKB:P58774,
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). {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=2;
CC Name=1; Synonyms=Skeletal muscle;
CC IsoId=P58775-1; Sequence=Displayed;
CC Name=2; Synonyms=non-muscle, Fibroblast, Embryonic fibroblast TM-1;
CC IsoId=P58775-2; Sequence=VSP_006599, VSP_006600;
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 on Ser-61 by PIK3CG. Phosphorylation on Ser-61 is
CC required for ADRB2 internalization (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the tropomyosin family. {ECO:0000305}.
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DR EMBL; L00381; AAA42288.1; -; Genomic_DNA.
DR EMBL; L00372; AAA42288.1; JOINED; Genomic_DNA.
DR EMBL; L00373; AAA42288.1; JOINED; Genomic_DNA.
DR EMBL; L00374; AAA42288.1; JOINED; Genomic_DNA.
DR EMBL; L00375; AAA42288.1; JOINED; Genomic_DNA.
DR EMBL; L00376; AAA42288.1; JOINED; Genomic_DNA.
DR EMBL; L00378; AAA42288.1; JOINED; Genomic_DNA.
DR EMBL; L00379; AAA42288.1; JOINED; Genomic_DNA.
DR EMBL; L00380; AAA42288.1; JOINED; Genomic_DNA.
DR EMBL; L00382; AAA42289.1; -; Genomic_DNA.
DR EMBL; L00372; AAA42289.1; JOINED; Genomic_DNA.
DR EMBL; L00373; AAA42289.1; JOINED; Genomic_DNA.
DR EMBL; L00374; AAA42289.1; JOINED; Genomic_DNA.
DR EMBL; L00375; AAA42289.1; JOINED; Genomic_DNA.
DR EMBL; L00376; AAA42289.1; JOINED; Genomic_DNA.
DR EMBL; L00377; AAA42289.1; JOINED; Genomic_DNA.
DR EMBL; L00379; AAA42289.1; JOINED; Genomic_DNA.
DR EMBL; L00380; AAA42289.1; JOINED; Genomic_DNA.
DR PIR; A02981; TMRTF1.
DR PIR; B25073; B25073.
DR RefSeq; NP_001019516.1; NM_001024345.2. [P58775-2]
DR RefSeq; NP_001288164.1; NM_001301235.1. [P58775-1]
DR AlphaFoldDB; P58775; -.
DR SMR; P58775; -.
DR BioGRID; 271758; 1.
DR STRING; 10116.ENSRNOP00000022801; -.
DR iPTMnet; P58775; -.
DR PhosphoSitePlus; P58775; -.
DR jPOST; P58775; -.
DR PRIDE; P58775; -.
DR Ensembl; ENSRNOT00000022801; ENSRNOP00000022801; ENSRNOG00000016731. [P58775-1]
DR Ensembl; ENSRNOT00000049000; ENSRNOP00000044473; ENSRNOG00000016731. [P58775-2]
DR GeneID; 500450; -.
DR KEGG; rno:500450; -.
DR UCSC; RGD:1559479; rat. [P58775-1]
DR CTD; 7169; -.
DR RGD; 1559479; Tpm2.
DR eggNOG; KOG1003; Eukaryota.
DR GeneTree; ENSGT01030000234542; -.
DR HOGENOM; CLU_055027_0_0_1; -.
DR InParanoid; P58775; -.
DR OMA; FYDADQT; -.
DR OrthoDB; 1576041at2759; -.
DR PhylomeDB; P58775; -.
DR Reactome; R-RNO-390522; Striated Muscle Contraction.
DR Reactome; R-RNO-445355; Smooth Muscle Contraction.
DR PRO; PR:P58775; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000016731; Expressed in skeletal muscle tissue and 19 other tissues.
DR ExpressionAtlas; P58775; baseline and differential.
DR Genevisible; P58775; RN.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; ISO:RGD.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
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:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR GO; GO:0043462; P:regulation of ATP-dependent activity; ISO:RGD.
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 Acetylation; Actin-binding; Alternative splicing; Coiled coil; Cytoplasm;
KW Cytoskeleton; Muscle protein; Phosphoprotein; Reference proteome.
FT CHAIN 1..284
FT /note="Tropomyosin beta chain"
FT /id="PRO_0000205629"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..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:P58776"
FT MOD_RES 53
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07951"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 79
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07951"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06753"
FT MOD_RES 108
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07951"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07951"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 252
FT /note="Phosphothreonine"
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:0007744|PubMed:22673903"
FT MOD_RES 282
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07951"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07951"
FT VAR_SEQ 189..213
FT /note="KCGDLEEELKIVTNNLKSLEAQADK -> RARQLEEELRTMDQALKSLIASE
FT EE (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_006599"
FT VAR_SEQ 258..284
FT /note="DEVYAQKMKYKAISEELDNALNDITSL -> ETLASAKEENVEIHQTLDQTL
FT LELNNL (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_006600"
FT MOD_RES P58775-2:210
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 284 AA; 32837 MW; F95D2BF6250F40AE CRC64;
MDAIKKKMQM LKLDKENAID RAEQAEADKK QAEDRCKQLE EEQQALQKKL KGTEDEVEKY
SESVKDAQEK LEQAEKKATD AEADVASLNR RIQLVEEELD RAQERLATAL QKLEEAEKAA
DESERGMKVI ENRAMKDEEK MELQEMQLKE AKHIAEDSDR KYEEVARKLV ILEGELERSE
ERAEVAESKC GDLEEELKIV TNNLKSLEAQ ADKYSTKEDK YEEEIKLLEE KLKEAETRAE
FAERSVAKLE KTIDDLEDEV YAQKMKYKAI SEELDNALND ITSL
