ID   TPM4_MOUSE              Reviewed;         248 AA.
AC   Q6IRU2;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 139.
DE   RecName: Full=Tropomyosin alpha-4 chain;
DE   AltName: Full=Tropomyosin-4;
GN   Name=Tpm4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Binds to actin filaments in muscle and non-muscle cells.
CC       Plays a central role, in association with the troponin complex, in the
CC       calcium dependent regulation of vertebrate striated muscle contraction.
CC       Smooth muscle contraction is regulated by interaction with caldesmon.
CC       In non-muscle cells is implicated in stabilizing cytoskeleton actin
CC       filaments. Binds calcium. {ECO:0000250|UniProtKB:P09495,
CC       ECO:0000250|UniProtKB:P67936}.
CC   -!- SUBUNIT: Homodimer. Heterodimer of an alpha (TPM1, TPM3 or TPM4) and a
CC       beta (TPM2) chain. {ECO:0000250|UniProtKB:P09495}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:P09495}. Note=Associates with F-actin stress
CC       fibers. {ECO:0000250|UniProtKB:P09495}.
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; BC023701; AAH23701.1; -; mRNA.
DR   EMBL; BC023827; AAH23827.1; -; mRNA.
DR   EMBL; BC070421; AAH70421.1; -; mRNA.
DR   CCDS; CCDS22408.1; -.
DR   RefSeq; NP_001001491.1; NM_001001491.1.
DR   AlphaFoldDB; Q6IRU2; -.
DR   SMR; Q6IRU2; -.
DR   BioGRID; 236471; 27.
DR   IntAct; Q6IRU2; 13.
DR   STRING; 10090.ENSMUSP00000003575; -.
DR   GlyGen; Q6IRU2; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q6IRU2; -.
DR   PhosphoSitePlus; Q6IRU2; -.
DR   SwissPalm; Q6IRU2; -.
DR   EPD; Q6IRU2; -.
DR   jPOST; Q6IRU2; -.
DR   MaxQB; Q6IRU2; -.
DR   PaxDb; 10090-ENSMUSP00000003575; -.
DR   PeptideAtlas; Q6IRU2; -.
DR   ProteomicsDB; 260729; -.
DR   Pumba; Q6IRU2; -.
DR   Antibodypedia; 27276; 202 antibodies from 28 providers.
DR   DNASU; 326618; -.
DR   Ensembl; ENSMUST00000003575.11; ENSMUSP00000003575.10; ENSMUSG00000031799.11.
DR   GeneID; 326618; -.
DR   KEGG; mmu:326618; -.
DR   UCSC; uc009mfi.1; mouse.
DR   AGR; MGI:2449202; -.
DR   CTD; 7171; -.
DR   MGI; MGI:2449202; Tpm4.
DR   VEuPathDB; HostDB:ENSMUSG00000031799; -.
DR   eggNOG; KOG1003; Eukaryota.
DR   GeneTree; ENSGT01030000234542; -.
DR   HOGENOM; CLU_055027_3_0_1; -.
DR   InParanoid; Q6IRU2; -.
DR   OMA; EDEWAHE; -.
DR   OrthoDB; 5398117at2759; -.
DR   PhylomeDB; Q6IRU2; -.
DR   TreeFam; TF351519; -.
DR   Reactome; R-MMU-390522; Striated Muscle Contraction.
DR   Reactome; R-MMU-445355; Smooth Muscle Contraction.
DR   Reactome; R-MMU-9013424; RHOV GTPase cycle.
DR   BioGRID-ORCS; 326618; 1 hit in 78 CRISPR screens.
DR   ChiTaRS; Tpm4; mouse.
DR   PRO; PR:Q6IRU2; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q6IRU2; Protein.
DR   Bgee; ENSMUSG00000031799; Expressed in undifferentiated genital tubercle and 248 other cell types or tissues.
DR   ExpressionAtlas; Q6IRU2; baseline and differential.
DR   GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
DR   GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR   GO; GO:0030863; C:cortical cytoskeleton; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0002102; C:podosome; IDA:MGI.
DR   GO; GO:0001725; C:stress fiber; ISO:MGI.
DR   GO; GO:0051015; F:actin filament binding; IDA:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS: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; Q6IRU2; MM.
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:0000250|UniProtKB:P67936"
FT   CHAIN           2..248
FT                   /note="Tropomyosin alpha-4 chain"
FT                   /id="PRO_0000205636"
FT   REGION          18..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          78..97
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   COMPBIAS        79..97
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P67936"
FT   MOD_RES         6
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09495"
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;  28468 MW;  2B6C388008A6AF1B CRC64;
     MAGLNSLEAV KRKIQALQQQ ADDAEDRAQG LQRELDGERE RREKAEGDAA ALNRRIQLLE
     EELDRAQEQL ATALQNLEEA EKAADESERG MKVIENRAMK DEEKMEILEM QLKEAKHITD
     EADRKYEEVA RKLVILEGEL KRAEERAEVS ELKCGDLEEE LKNVTNNLKS LEAASEKYSE
     KEDKYEEEIK LLSDKLKEAE TRAEFAERTV SKLEKTIDDL EEKLAQAKEE NVGLHQTLDQ
     TLNELNCI
//