ID   TPM4_RAT                Reviewed;         248 AA.
AC   P09495;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 158.
DE   RecName: Full=Tropomyosin alpha-4 chain;
DE   AltName: Full=Tropomyosin-4;
DE            Short=TM-4;
GN   Name=Tpm4;
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].
RX   PubMed=3611091; DOI=10.1016/s0021-9258(18)61033-6;
RA   Yamawaki-Kataoka Y., Helfman D.M.;
RT   "Isolation and characterization of cDNA clones encoding a low molecular
RT   weight nonmuscle tropomyosin isoform.";
RL   J. Biol. Chem. 262:10791-10800(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Brain, and Liver;
RX   PubMed=2112608; DOI=10.1016/s0022-2836(05)80202-5;
RA   Lees-Miller J.P., Yan A., Helfman D.M.;
RT   "Structure and complete nucleotide sequence of the gene encoding rat
RT   fibroblast tropomyosin 4.";
RL   J. Mol. Biol. 213:399-405(1990).
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   ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RA   Lubec G., Chen W.-Q.;
RL   Submitted (FEB-2007) to UniProtKB.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND IDENTIFICATION BY MASS
RP   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). Plays a central role, in association with the
CC       troponin complex, in the calcium dependent regulation of vertebrate
CC       striated muscle contraction (By similarity). Smooth muscle contraction
CC       is regulated by interaction with caldesmon (By similarity). In non-
CC       muscle cells is implicated in stabilizing cytoskeleton actin filaments
CC       (By similarity). Binds calcium (By similarity).
CC       {ECO:0000250|UniProtKB:P67936, ECO:0000269|PubMed:7568216}.
CC   -!- SUBUNIT: Homodimer (PubMed:7568216). Heterodimer of an alpha (TPM1,
CC       TPM3 or TPM4) and a beta (TPM2) chain (PubMed:7568216).
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   -!- 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   -!- SIMILARITY: Belongs to the tropomyosin family. {ECO:0000305}.
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DR   EMBL; J02780; AAA42291.1; -; mRNA.
DR   EMBL; Y00169; CAA68360.1; -; Genomic_DNA.
DR   PIR; S10623; S10623.
DR   RefSeq; NP_036810.1; NM_012678.2.
DR   AlphaFoldDB; P09495; -.
DR   SMR; P09495; -.
DR   BioGRID; 246969; 6.
DR   IntAct; P09495; 2.
DR   MINT; P09495; -.
DR   STRING; 10116.ENSRNOP00000021073; -.
DR   iPTMnet; P09495; -.
DR   PhosphoSitePlus; P09495; -.
DR   jPOST; P09495; -.
DR   PaxDb; 10116-ENSRNOP00000021073; -.
DR   Ensembl; ENSRNOT00000089056.2; ENSRNOP00000072238.2; ENSRNOG00000015496.7.
DR   Ensembl; ENSRNOT00055017537; ENSRNOP00055014127; ENSRNOG00055010361.
DR   Ensembl; ENSRNOT00060018545; ENSRNOP00060014419; ENSRNOG00060010959.
DR   Ensembl; ENSRNOT00065037231; ENSRNOP00065030037; ENSRNOG00065021866.
DR   GeneID; 24852; -.
DR   KEGG; rno:24852; -.
DR   UCSC; RGD:3899; rat.
DR   AGR; RGD:3899; -.
DR   CTD; 7171; -.
DR   RGD; 3899; Tpm4.
DR   eggNOG; KOG1003; Eukaryota.
DR   GeneTree; ENSGT01030000234542; -.
DR   HOGENOM; CLU_055027_3_0_1; -.
DR   InParanoid; P09495; -.
DR   OMA; ISIYCAK; -.
DR   OrthoDB; 5398117at2759; -.
DR   PhylomeDB; P09495; -.
DR   TreeFam; TF351519; -.
DR   Reactome; R-RNO-390522; Striated Muscle Contraction.
DR   Reactome; R-RNO-445355; Smooth Muscle Contraction.
DR   Reactome; R-RNO-9013424; RHOV GTPase cycle.
DR   PRO; PR:P09495; -.
DR   Proteomes; UP000002494; Chromosome 16.
DR   Bgee; ENSRNOG00000015496; Expressed in lung and 19 other cell types or tissues.
DR   ExpressionAtlas; P09495; baseline and differential.
DR   GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
DR   GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR   GO; GO:0030863; C:cortical cytoskeleton; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0002102; C:podosome; ISO:RGD.
DR   GO; GO:0001725; C:stress fiber; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   Gene3D; 1.20.5.170; -; 1.
DR   Gene3D; 1.20.5.370; -; 1.
DR   InterPro; IPR000533; Tropomyosin.
DR   InterPro; IPR014751; XRCC4-like_C.
DR   PANTHER; PTHR19269; TROPOMYOSIN; 1.
DR   PANTHER; PTHR19269:SF70; TROPOMYOSIN ALPHA-4 CHAIN; 1.
DR   Pfam; PF00261; Tropomyosin; 1.
DR   PRINTS; PR00194; TROPOMYOSIN.
DR   SUPFAM; SSF57997; Tropomyosin; 1.
DR   PROSITE; PS00326; TROPOMYOSIN; 1.
DR   Genevisible; P09495; RN.
PE   1: Evidence at protein level;
KW   Acetylation; Actin-binding; Calcium; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Metal-binding; Muscle protein; Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|Ref.4"
FT   CHAIN           2..248
FT                   /note="Tropomyosin alpha-4 chain"
FT                   /id="PRO_0000205638"
FT   REGION          18..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          2..248
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        26..49
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|Ref.4"
FT   MOD_RES         6
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         177
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P67936"
FT   MOD_RES         215
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P67936"
FT   MOD_RES         216
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P67936"
SQ   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
//