TPM2_MOUSE
ID TPM2_MOUSE Reviewed; 284 AA.
AC P58774; P02560; P46901;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Tropomyosin beta chain;
DE AltName: Full=Beta-tropomyosin;
DE AltName: Full=Tropomyosin-2;
GN Name=Tpm2; Synonyms=Tpm-2;
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 [MRNA] (ISOFORM 1).
RX PubMed=2461223; DOI=10.1016/0167-4781(88)90031-0;
RA McInnes C., Leader D.P.;
RT "The tropomyosin mRNAs of mouse striated muscles: molecular cloning of
RT beta-tropomyosin.";
RL Biochim. Biophys. Acta 951:117-122(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C3H/HeJ;
RX PubMed=1733968; DOI=10.1016/s0021-9258(18)45940-6;
RA Wang Y.C., Rubenstein P.A.;
RT "Choice of 3' cleavage/polyadenylation site in beta-tropomyosin RNA
RT processing is differentiation-dependent in mouse BC3H1 muscle cells.";
RL J. Biol. Chem. 267:2728-2736(1992).
RN [3]
RP FUNCTION, PHOSPHORYLATION AT SER-61, AND MUTAGENESIS OF SER-61.
RX PubMed=16094730; DOI=10.1038/ncb1278;
RA Naga Prasad S.V., Jayatilleke A., Madamanchi A., Rockman H.A.;
RT "Protein kinase activity of phosphoinositide 3-kinase regulates beta-
RT adrenergic receptor endocytosis.";
RL Nat. Cell Biol. 7:785-796(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Pancreas, Spleen, and
RC 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. The non-muscle isoform may have a role in agonist-mediated
CC receptor internalization (PubMed:16094730).
CC {ECO:0000250|UniProtKB:P58775, ECO:0000269|PubMed:16094730}.
CC -!- SUBUNIT: Homodimer. Heterodimer of an alpha (TPM1, TPM3 or TPM4) and a
CC beta (TPM2) chain. {ECO:0000250|UniProtKB:P58775}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P58775}. Note=Associates with F-actin stress
CC fibers. {ECO:0000250|UniProtKB:P58775}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Skeletal muscle, TB1-3;
CC IsoId=P58774-1; Sequence=Displayed;
CC Name=2; Synonyms=non-muscle, Fibroblast, TM-1;
CC IsoId=P58774-2; Sequence=VSP_006597, VSP_006598;
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. {ECO:0000269|PubMed:16094730}.
CC -!- SIMILARITY: Belongs to the tropomyosin family. {ECO:0000305}.
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DR EMBL; X12650; CAA31181.1; -; mRNA.
DR EMBL; M81086; AAA40484.1; -; mRNA.
DR EMBL; X58381; CAA41271.1; -; mRNA.
DR CCDS; CCDS18100.1; -. [P58774-1]
DR CCDS; CCDS71374.1; -. [P58774-2]
DR PIR; S03838; S03838.
DR PIR; S23256; S23256.
DR RefSeq; NP_033442.2; NM_009416.4. [P58774-1]
DR AlphaFoldDB; P58774; -.
DR SMR; P58774; -.
DR BioGRID; 204292; 12.
DR DIP; DIP-628N; -.
DR IntAct; P58774; 2.
DR STRING; 10090.ENSMUSP00000030184; -.
DR iPTMnet; P58774; -.
DR PhosphoSitePlus; P58774; -.
DR SWISS-2DPAGE; P58774; -.
DR jPOST; P58774; -.
DR MaxQB; P58774; -.
DR PaxDb; P58774; -.
DR PeptideAtlas; P58774; -.
DR PRIDE; P58774; -.
DR ProteomicsDB; 259166; -. [P58774-1]
DR ProteomicsDB; 259167; -. [P58774-2]
DR DNASU; 22004; -.
DR Ensembl; ENSMUST00000107913; ENSMUSP00000103546; ENSMUSG00000028464. [P58774-1]
DR Ensembl; ENSMUST00000107914; ENSMUSP00000103547; ENSMUSG00000028464. [P58774-2]
DR GeneID; 22004; -.
DR KEGG; mmu:22004; -.
DR UCSC; uc008sqd.2; mouse. [P58774-1]
DR CTD; 7169; -.
DR MGI; MGI:98810; Tpm2.
DR VEuPathDB; HostDB:ENSMUSG00000028464; -.
DR eggNOG; KOG1003; Eukaryota.
DR GeneTree; ENSGT01030000234542; -.
DR HOGENOM; CLU_055027_0_0_1; -.
DR InParanoid; P58774; -.
DR OMA; FYDADQT; -.
DR PhylomeDB; P58774; -.
DR Reactome; R-MMU-390522; Striated Muscle Contraction.
DR Reactome; R-MMU-445355; Smooth Muscle Contraction.
DR BioGRID-ORCS; 22004; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Tpm2; mouse.
DR PRO; PR:P58774; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P58774; protein.
DR Bgee; ENSMUSG00000028464; Expressed in intercostal muscle and 262 other tissues.
DR ExpressionAtlas; P58774; baseline and differential.
DR Genevisible; P58774; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0005862; C:muscle thin filament tropomyosin; TAS:MGI.
DR GO; GO:0003779; F:actin binding; ISO:MGI.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:MGI.
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:MGI.
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_0000205628"
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; by PIK3CG"
FT /evidence="ECO:0000269|PubMed:16094730"
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:0000250|UniProtKB:P07951"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P58775"
FT MOD_RES 252
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07951"
FT MOD_RES 261
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P58775"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P58775"
FT MOD_RES 282
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07951"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 189..213
FT /note="KCGDLEEELKIVTNNLKSLEAQADK -> RARQLEEELRTMDQALKSLIASE
FT EE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1733968"
FT /id="VSP_006597"
FT VAR_SEQ 258..284
FT /note="DEVYAQKMKYKAISEELDNALNDITSL -> ETLASAKEENVEIHQTLDQTL
FT LELNNL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1733968"
FT /id="VSP_006598"
FT MUTAGEN 61
FT /note="S->A: Abolishes ADRB2 internalization."
FT /evidence="ECO:0000269|PubMed:16094730"
FT CONFLICT 23..24
FT /note="EQ -> DE (in Ref. 2; CAA41271)"
FT /evidence="ECO:0000305"
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
