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TPM2_BOVIN
ID   TPM2_BOVIN              Reviewed;         284 AA.
AC   Q5KR48; Q3SX28;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Tropomyosin beta chain;
DE   AltName: Full=Beta-tropomyosin;
DE   AltName: Full=Tropomyosin-2;
GN   Name=TPM2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Skeletal muscle;
RA   Oe M., Nakajima I., Muroya S., Chikuni K.;
RT   "Bovine tropomyosin isoforms.";
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5KR48-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5KR48-2; Sequence=VSP_026156;
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 (By similarity). {ECO:0000250}.
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   EMBL; AB198071; BAD86591.1; -; mRNA.
DR   EMBL; BC104538; AAI04539.1; -; mRNA.
DR   RefSeq; NP_001010995.2; NM_001010995.2. [Q5KR48-2]
DR   RefSeq; XP_005210124.1; XM_005210067.1. [Q5KR48-1]
DR   AlphaFoldDB; Q5KR48; -.
DR   SMR; Q5KR48; -.
DR   STRING; 9913.ENSBTAP00000043502; -.
DR   PeptideAtlas; Q5KR48; -.
DR   PRIDE; Q5KR48; -.
DR   Ensembl; ENSBTAT00000015186; ENSBTAP00000015186; ENSBTAG00000011424. [Q5KR48-1]
DR   Ensembl; ENSBTAT00000046179; ENSBTAP00000043502; ENSBTAG00000011424. [Q5KR48-2]
DR   GeneID; 497015; -.
DR   KEGG; bta:497015; -.
DR   CTD; 7169; -.
DR   VEuPathDB; HostDB:ENSBTAG00000011424; -.
DR   eggNOG; KOG1003; Eukaryota.
DR   GeneTree; ENSGT01030000234542; -.
DR   HOGENOM; CLU_055027_0_0_1; -.
DR   InParanoid; Q5KR48; -.
DR   OMA; FYDADQT; -.
DR   OrthoDB; 1576041at2759; -.
DR   TreeFam; TF351519; -.
DR   Reactome; R-BTA-390522; Striated Muscle Contraction.
DR   Proteomes; UP000009136; Chromosome 8.
DR   Bgee; ENSBTAG00000011424; Expressed in laryngeal cartilage and 106 other tissues.
DR   GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
DR   GO; GO:0005884; C:actin filament; IBA:GO_Central.
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   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; IEA:Ensembl.
DR   InterPro; IPR000533; Tropomyosin.
DR   Pfam; PF00261; Tropomyosin; 1.
DR   PRINTS; PR00194; TROPOMYOSIN.
DR   PROSITE; PS00326; TROPOMYOSIN; 1.
PE   2: Evidence at transcript 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_0000289992"
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: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"
FT   VAR_SEQ         189..213
FT                   /note="KCGDLEEELKIVTNNLKSLEAQADK -> RARQLEEELRTMDQALKSLMASE
FT                   EE (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_026156"
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
 
 
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