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Tropomyosin alpha-4 chain (Tropomyosin-4) (TM-4)

 TPM4_RAT                Reviewed;         248 AA.
P09495;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 126.
RecName: Full=Tropomyosin alpha-4 chain;
AltName: Full=Tropomyosin-4;
Short=TM-4;
Name=Tpm4;
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 [MRNA].
PubMed=3611091;
Yamawaki-Kataoka Y., Helfman D.M.;
"Isolation and characterization of cDNA clones encoding a low
molecular weight nonmuscle tropomyosin isoform.";
J. Biol. Chem. 262:10791-10800(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Brain, and Liver;
PubMed=2112608; DOI=10.1016/S0022-2836(05)80202-5;
Lees-Miller J.P., Yan A., Helfman D.M.;
"Structure and complete nucleotide sequence of the gene encoding rat
fibroblast tropomyosin 4.";
J. Mol. Biol. 213:399-405(1990).
[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]
ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
Lubec G., Chen W.-Q.;
Submitted (FEB-2007) to UniProtKB.
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, 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). Plays a central role, in association with the
troponin complex, in the calcium dependent regulation of
vertebrate striated muscle contraction (By similarity). Smooth
muscle contraction is regulated by interaction with caldesmon (By
similarity). In non-muscle cells is implicated in stabilizing
cytoskeleton actin filaments (By similarity). Binds calcium (By
similarity). {ECO:0000250|UniProtKB:P67936,
ECO:0000269|PubMed:7568216}.
-!- SUBUNIT: Homodimer (PubMed:7568216). Heterodimer of an alpha
(TPM1, TPM3 or TPM4) and a beta (TPM2) chain (PubMed:7568216).
{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}.
-!- DOMAIN: The molecule is in a coiled coil structure that is formed
by 2 polypeptide chains. The sequence exhibits a prominent seven-
residues periodicity.
-!- SIMILARITY: Belongs to the tropomyosin family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; J02780; AAA42291.1; -; mRNA.
EMBL; Y00169; CAA68360.1; -; Genomic_DNA.
PIR; S10623; S10623.
RefSeq; NP_036810.1; NM_012678.2.
UniGene; Rn.108199; -.
ProteinModelPortal; P09495; -.
SMR; P09495; -.
BioGrid; 246969; 1.
IntAct; P09495; 1.
STRING; 10116.ENSRNOP00000021073; -.
iPTMnet; P09495; -.
PhosphoSitePlus; P09495; -.
PaxDb; P09495; -.
PRIDE; P09495; -.
Ensembl; ENSRNOT00000021073; ENSRNOP00000021073; ENSRNOG00000015496.
GeneID; 24852; -.
KEGG; rno:24852; -.
UCSC; RGD:3899; rat.
CTD; 7171; -.
RGD; 3899; Tpm4.
eggNOG; KOG1003; Eukaryota.
eggNOG; ENOG410XR5K; LUCA.
GeneTree; ENSGT00550000074494; -.
HOGENOM; HOG000231522; -.
HOVERGEN; HBG107404; -.
InParanoid; P09495; -.
KO; K10375; -.
OMA; LQHELIT; -.
OrthoDB; EOG091G0UO7; -.
PhylomeDB; P09495; -.
TreeFam; TF351519; -.
Reactome; R-RNO-390522; Striated Muscle Contraction.
Reactome; R-RNO-445355; Smooth Muscle Contraction.
PRO; PR:P09495; -.
Proteomes; UP000002494; Chromosome 16.
Bgee; ENSRNOG00000015496; -.
ExpressionAtlas; P09495; baseline and differential.
Genevisible; P09495; RN.
GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
GO; GO:0005884; C:actin filament; IBA:GO_Central.
GO; GO:0030863; C:cortical cytoskeleton; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0031941; C:filamentous actin; IEA:Ensembl.
GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
GO; GO:0016020; C:membrane; IEA:Ensembl.
GO; GO:0005862; C:muscle thin filament tropomyosin; IBA:GO_Central.
GO; GO:0002102; C:podosome; IEA:Ensembl.
GO; GO:0001725; C:stress fiber; IEA:Ensembl.
GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; TAS:RGD.
GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
InterPro; IPR000533; Tropomyosin.
Pfam; PF00261; Tropomyosin; 1.
PRINTS; PR00194; TROPOMYOSIN.
PROSITE; PS00326; TROPOMYOSIN; 1.
1: Evidence at protein level;
Acetylation; Actin-binding; Calcium; Coiled coil; Complete proteome;
Cytoplasm; Cytoskeleton; Metal-binding; Muscle protein;
Phosphoprotein; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|Ref.4}.
CHAIN 2 248 Tropomyosin alpha-4 chain.
/FTId=PRO_0000205638.
COILED 2 248 {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine. {ECO:0000269|Ref.4}.
MOD_RES 6 6 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 177 177 N6-acetyllysine.
{ECO:0000250|UniProtKB:P67936}.
MOD_RES 215 215 N6-acetyllysine.
{ECO:0000250|UniProtKB:P67936}.
MOD_RES 216 216 Phosphothreonine.
{ECO:0000250|UniProtKB:P67936}.
SEQUENCE 248 AA; 28510 MW; 53C9327CA60CF954 CRC64;
MAGLNSLEAV KRKIQALQQQ ADDAEDRAQG LQRELDGERE RREKAEGDAA ALNRRIQLVE
EELDRAQERL ATALQKLEEA EKAADESERG MKVIENRAMK DEEKMEIQEM QLKEAKHIAE
EADRKYEEVA RKLVILEGEL ERAEERAEVS ELKSSDLEEE LKNVTNNLKS LEAASEKYSE
KEDKYEEEIK LLSDKLKEAE TRAEFAERTV SKLEKTIDDL EEKLAQAKEE NVGLHQTLDQ
TLNELNCI


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