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Tropomyosin beta chain (Beta-tropomyosin) (Tropomyosin-2)

 TPM2_RAT                Reviewed;         284 AA.
P58775; P02560; P06395;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
22-NOV-2017, entry version 112.
RecName: Full=Tropomyosin beta chain;
AltName: Full=Beta-tropomyosin;
AltName: Full=Tropomyosin-2;
Name=Tpm2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
PubMed=3840484;
Yamawaki-Kataoka Y., Helfman D.M.;
"Rat embryonic fibroblast tropomyosin 1. cDNA and complete primary
amino acid sequence.";
J. Biol. Chem. 260:14440-14445(1985).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
PubMed=2432392; DOI=10.1128/MCB.6.11.3582;
Helfman D.M., Cheley S., Kuismanen E., Finn L.A., Yamawaki-Kataoka Y.;
"Nonmuscle and muscle tropomyosin isoforms are expressed from a single
gene by alternative RNA splicing and polyadenylation.";
Mol. Cell. Biol. 6:3582-3595(1986).
[3]
FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=7568216; DOI=10.1073/pnas.92.21.9776;
Gimona M., Watakabe A., Helfman D.M.;
"Specificity of dimer formation in tropomyosins: influence of
alternatively spliced exons on homodimer and heterodimer assembly.";
Proc. Natl. Acad. Sci. U.S.A. 92:9776-9780(1995).
[4]
FUNCTION, AND SUBUNIT.
PubMed=22812662; DOI=10.1021/bi300340r;
Kalyva A., Schmidtmann A., Geeves M.A.;
"In vitro formation and characterization of the skeletal muscle
alpha.beta tropomyosin heterodimers.";
Biochemistry 51:6388-6399(2012).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61; SER-206; SER-215;
THR-252; TYR-261 AND SER-271, PHOSPHORYLATION [LARGE SCALE ANALYSIS]
AT SER-210 (ISOFORM 2), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Binds to actin filaments in muscle and non-muscle cells
(PubMed:7568216, PubMed:22812662). Plays a central role, in
association with the troponin complex, in the calcium dependent
regulation of vertebrate striated muscle contraction
(PubMed:22812662). Smooth muscle contraction is regulated by
interaction with caldesmon. In non-muscle cells is implicated in
stabilizing cytoskeleton actin filaments. The non-muscle isoform
may have a role in agonist-mediated receptor internalization (By
similarity). {ECO:0000250|UniProtKB:P58774,
ECO:0000269|PubMed:22812662, ECO:0000269|PubMed:7568216}.
-!- SUBUNIT: Homodimer (PubMed:7568216, PubMed:22812662). Heterodimer
of an alpha (TPM1, TPM3 or TPM4) and a beta (TPM2) chain
(PubMed:7568216, PubMed:22812662). {ECO:0000269|PubMed:22812662,
ECO:0000269|PubMed:7568216}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:7568216}. Note=Associates with F-actin stress
fibers (PubMed:7568216). {ECO:0000269|PubMed:7568216}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Skeletal muscle;
IsoId=P58775-1; Sequence=Displayed;
Name=2; Synonyms=non-muscle, Fibroblast, Embryonic fibroblast
TM-1;
IsoId=P58775-2; Sequence=VSP_006599, VSP_006600;
Note=Contains a phosphoserine at position 210.
{ECO:0000244|PubMed:22673903};
-!- DOMAIN: The molecule is in a coiled coil structure that is formed
by 2 polypeptide chains. The sequence exhibits a prominent seven-
residues periodicity.
-!- PTM: Phosphorylated on Ser-61 by PIK3CG. Phosphorylation on Ser-61
is required for ADRB2 internalization (By similarity).
{ECO:0000250}.
-!- SIMILARITY: Belongs to the tropomyosin family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; L00381; AAA42288.1; -; Genomic_DNA.
EMBL; L00372; AAA42288.1; JOINED; Genomic_DNA.
EMBL; L00373; AAA42288.1; JOINED; Genomic_DNA.
EMBL; L00374; AAA42288.1; JOINED; Genomic_DNA.
EMBL; L00375; AAA42288.1; JOINED; Genomic_DNA.
EMBL; L00376; AAA42288.1; JOINED; Genomic_DNA.
EMBL; L00378; AAA42288.1; JOINED; Genomic_DNA.
EMBL; L00379; AAA42288.1; JOINED; Genomic_DNA.
EMBL; L00380; AAA42288.1; JOINED; Genomic_DNA.
EMBL; L00382; AAA42289.1; -; Genomic_DNA.
EMBL; L00372; AAA42289.1; JOINED; Genomic_DNA.
EMBL; L00373; AAA42289.1; JOINED; Genomic_DNA.
EMBL; L00374; AAA42289.1; JOINED; Genomic_DNA.
EMBL; L00375; AAA42289.1; JOINED; Genomic_DNA.
EMBL; L00376; AAA42289.1; JOINED; Genomic_DNA.
EMBL; L00377; AAA42289.1; JOINED; Genomic_DNA.
EMBL; L00379; AAA42289.1; JOINED; Genomic_DNA.
EMBL; L00380; AAA42289.1; JOINED; Genomic_DNA.
PIR; A02981; TMRTF1.
PIR; B25073; B25073.
RefSeq; NP_001019516.1; NM_001024345.2. [P58775-2]
RefSeq; NP_001288164.1; NM_001301235.1. [P58775-1]
UniGene; Rn.17580; -.
ProteinModelPortal; P58775; -.
SMR; P58775; -.
BioGrid; 271758; 1.
iPTMnet; P58775; -.
PhosphoSitePlus; P58775; -.
PRIDE; P58775; -.
Ensembl; ENSRNOT00000022801; ENSRNOP00000022801; ENSRNOG00000016731. [P58775-1]
Ensembl; ENSRNOT00000049000; ENSRNOP00000044473; ENSRNOG00000016731. [P58775-2]
GeneID; 500450; -.
KEGG; rno:500450; -.
UCSC; RGD:1559479; rat. [P58775-1]
CTD; 7169; -.
RGD; 1559479; Tpm2.
GeneTree; ENSGT00550000074494; -.
HOGENOM; HOG000231521; -.
HOVERGEN; HBG107404; -.
InParanoid; P58775; -.
KO; K10374; -.
OMA; CEGQAKD; -.
OrthoDB; EOG091G0UO7; -.
PhylomeDB; P58775; -.
Reactome; R-RNO-390522; Striated Muscle Contraction.
Reactome; R-RNO-445355; Smooth Muscle Contraction.
PRO; PR:P58775; -.
Proteomes; UP000002494; Chromosome 5.
Bgee; ENSRNOG00000016731; -.
ExpressionAtlas; P58775; baseline and differential.
Genevisible; P58775; RN.
GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
GO; GO:0005884; C:actin filament; IBA:GO_Central.
GO; GO:0005862; C:muscle thin filament tropomyosin; IBA:GO_Central.
GO; GO:0003779; F:actin binding; ISO:RGD.
GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0008307; F:structural constituent of muscle; IBA:GO_Central.
GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
GO; GO:0043462; P:regulation of ATPase activity; ISO:RGD.
InterPro; IPR000533; Tropomyosin.
Pfam; PF00261; Tropomyosin; 1.
PRINTS; PR00194; TROPOMYOSIN.
PROSITE; PS00326; TROPOMYOSIN; 1.
1: Evidence at protein level;
Acetylation; Actin-binding; Alternative splicing; Coiled coil;
Complete proteome; Cytoplasm; Cytoskeleton; Muscle protein;
Phosphoprotein; Reference proteome.
CHAIN 1 284 Tropomyosin beta chain.
/FTId=PRO_0000205629.
COILED 1 284 {ECO:0000250}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P58776}.
MOD_RES 53 53 Phosphothreonine.
{ECO:0000250|UniProtKB:P07951}.
MOD_RES 61 61 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 79 79 Phosphothreonine.
{ECO:0000250|UniProtKB:P07951}.
MOD_RES 87 87 Phosphoserine.
{ECO:0000250|UniProtKB:P06753}.
MOD_RES 108 108 Phosphothreonine.
{ECO:0000250|UniProtKB:P07951}.
MOD_RES 158 158 Phosphoserine.
{ECO:0000250|UniProtKB:P07951}.
MOD_RES 206 206 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 215 215 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 252 252 Phosphothreonine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 261 261 Phosphotyrosine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 271 271 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 282 282 Phosphothreonine.
{ECO:0000250|UniProtKB:P07951}.
MOD_RES 283 283 Phosphoserine.
{ECO:0000250|UniProtKB:P09493}.
VAR_SEQ 189 213 KCGDLEEELKIVTNNLKSLEAQADK -> RARQLEEELRTM
DQALKSLIASEEE (in isoform 2).
{ECO:0000305}.
/FTId=VSP_006599.
VAR_SEQ 258 284 DEVYAQKMKYKAISEELDNALNDITSL -> ETLASAKEEN
VEIHQTLDQTLLELNNL (in isoform 2).
{ECO:0000305}.
/FTId=VSP_006600.
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


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