TPM2_RABIT
ID TPM2_RABIT Reviewed; 284 AA.
AC P58776; P02560;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Tropomyosin beta chain;
DE AltName: Full=Beta-tropomyosin;
DE AltName: Full=Tropomyosin-2;
GN Name=TPM2;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP PROTEIN SEQUENCE, AND ACETYLATION AT MET-1.
RX PubMed=7364764; DOI=10.1016/s0021-9258(19)85753-8;
RA Mak A.S., Smillie L.B., Steward G.R.;
RT "A comparison of the amino acid sequences of rabbit skeletal muscle
RT alpha- and beta-tropomyosins.";
RL J. Biol. Chem. 255:3647-3655(1980).
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. {ECO:0000250|UniProtKB:P58774,
CC ECO:0000250|UniProtKB:P58775}.
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 -!- 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 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the tropomyosin family. {ECO:0000305}.
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DR PIR; A02980; TMRBB.
DR RefSeq; XP_017194790.1; XM_017339301.1.
DR AlphaFoldDB; P58776; -.
DR SMR; P58776; -.
DR IntAct; P58776; 1.
DR MINT; P58776; -.
DR STRING; 9986.ENSOCUP00000022333; -.
DR iPTMnet; P58776; -.
DR GeneID; 100125984; -.
DR CTD; 7169; -.
DR eggNOG; KOG1003; Eukaryota.
DR HOGENOM; CLU_055027_0_0_1; -.
DR InParanoid; P58776; -.
DR OMA; FYDADQT; -.
DR OrthoDB; 1576041at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR ExpressionAtlas; P58776; baseline.
DR GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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 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; Coiled coil; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Muscle protein; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..284
FT /note="Tropomyosin beta chain"
FT /id="PRO_0000205630"
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:0000269|PubMed:7364764"
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:0000250|UniProtKB:P58774"
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:0000250|UniProtKB:P07951"
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
