TPM2_CHICK
ID TPM2_CHICK Reviewed; 284 AA.
AC P19352; P04267; P19353;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Tropomyosin beta chain;
DE AltName: Full=Beta-tropomyosin;
DE AltName: Full=Tropomyosin-2;
GN Name=TPM2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=6548747; DOI=10.1016/s0021-9258(18)89867-2;
RA Helfman D.M., Feramisco J.R., Ricci W.M., Hughes S.H.;
RT "Isolation and sequence of a cDNA clone that contains the entire coding
RT region for chicken smooth-muscle alpha-tropomyosin.";
RL J. Biol. Chem. 259:14136-14143(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
RX PubMed=2927392; DOI=10.1128/mcb.9.1.185-192.1989;
RA Bradac J.A., Gruber C.E., Forry-Schaudies S., Hughes S.H.;
RT "Isolation and characterization of related cDNA clones encoding skeletal
RT muscle beta-tropomyosin and a low-molecular-weight nonmuscle tropomyosin
RT isoform.";
RL Mol. Cell. Biol. 9:185-192(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
RX PubMed=2914939; DOI=10.1016/s0021-9258(19)81702-7;
RA Libri D., Lemonnier M., Meinnel T., Fiszman M.Y.;
RT "A single gene codes for the beta subunits of smooth and skeletal muscle
RT tropomyosin in the chicken.";
RL J. Biol. Chem. 264:2935-2944(1989).
RN [4]
RP PROTEIN SEQUENCE (ISOFORM 2).
RX PubMed=3997867; DOI=10.1016/s0021-9258(17)39602-3;
RA Sanders C., Smillie L.B.;
RT "Amino acid sequence of chicken gizzard beta-tropomyosin. Comparison of the
RT chicken gizzard, rabbit skeletal, and equine platelet tropomyosins.";
RL J. Biol. Chem. 260:7264-7275(1985).
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. {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=3;
CC Name=1; Synonyms=Skeletal muscle;
CC IsoId=P19352-1; Sequence=Displayed;
CC Name=2; Synonyms=Smooth muscle, Gizzard;
CC IsoId=P19352-2; Sequence=VSP_006602, VSP_006603;
CC Name=3; Synonyms=Fibroblast, 3b;
CC IsoId=P19352-3; Sequence=VSP_006601, VSP_006602, VSP_006603;
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; K02446; AAA49109.1; -; mRNA.
DR EMBL; M21226; AAA49116.1; -; Genomic_DNA.
DR EMBL; M21223; AAA49116.1; JOINED; Genomic_DNA.
DR EMBL; M21224; AAA49116.1; JOINED; Genomic_DNA.
DR EMBL; M21225; AAA49116.1; JOINED; Genomic_DNA.
DR EMBL; M23081; AAA49117.1; -; mRNA.
DR EMBL; M23082; AAA49112.1; -; mRNA.
DR PIR; A30125; A30125.
DR PIR; A92462; TMCHS1.
DR PIR; B30125; B30125.
DR RefSeq; XP_015132746.1; XM_015277260.1. [P19352-2]
DR RefSeq; XP_015132749.1; XM_015277263.1. [P19352-1]
DR RefSeq; XP_015132753.1; XM_015277267.1. [P19352-3]
DR PDB; 3U59; X-ray; 2.50 A; A/B/C/D=1-98.
DR PDBsum; 3U59; -.
DR AlphaFoldDB; P19352; -.
DR SMR; P19352; -.
DR IntAct; P19352; 1.
DR MINT; P19352; -.
DR STRING; 9031.ENSGALP00000041062; -.
DR PRIDE; P19352; -.
DR GeneID; 396430; -.
DR CTD; 7169; -.
DR VEuPathDB; HostDB:geneid_396430; -.
DR eggNOG; KOG1003; Eukaryota.
DR InParanoid; P19352; -.
DR OrthoDB; 1576041at2759; -.
DR PhylomeDB; P19352; -.
DR PRO; PR:P19352; -.
DR Proteomes; UP000000539; Unplaced.
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 InterPro; IPR000533; Tropomyosin.
DR Pfam; PF00261; Tropomyosin; 1.
DR PRINTS; PR00194; TROPOMYOSIN.
DR PROSITE; PS00326; TROPOMYOSIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Alternative splicing;
KW Coiled coil; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Muscle protein; Reference proteome.
FT CHAIN 1..284
FT /note="Tropomyosin beta chain"
FT /id="PRO_0000205631"
FT REGION 22..66
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"
FT VAR_SEQ 1..80
FT /note="MEAIKKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQGLQKKLKG
FT TEDEVEKYSESVKEAQEKLEQAEKKATD -> MAGISSIDAVKKKIQSLQQVADEAEER
FT AEHLQREADAERQARER (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:2927392"
FT /id="VSP_006601"
FT VAR_SEQ 189..213
FT /note="KCGDLEEELKIVTNNLKSLEAQADK -> RVRQLEEELRTMDQSLKSLIASE
FT EE (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:2927392,
FT ECO:0000303|PubMed:3997867, ECO:0000303|PubMed:6548747"
FT /id="VSP_006602"
FT VAR_SEQ 258..284
FT /note="DEVYAQKMKYKAISEELDNALNDITSL -> ESLASAKEENVGIHQVLDQTL
FT LELNNL (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:2927392,
FT ECO:0000303|PubMed:3997867, ECO:0000303|PubMed:6548747"
FT /id="VSP_006603"
FT HELIX 1..95
FT /evidence="ECO:0007829|PDB:3U59"
SQ SEQUENCE 284 AA; 32777 MW; D1898F7C698F6F71 CRC64;
MEAIKKKMQM LKLDKENAID RAEQAEADKK QAEDRCKQLE EEQQGLQKKL KGTEDEVEKY
SESVKEAQEK LEQAEKKATD AEAEVASLNR RIQLVEEELD RAQERLATAL QKLEEAEKAA
DESERGMKVI ENRAMKDEEK MELQEMQLKE AKHIAEEADR KYEEVARKLV VLEGELERSE
ERAEVAESKC GDLEEELKIV TNNLKSLEAQ ADKYSTKEDK YEEEIKLLGE KLKEAETRAE
FAERSVAKLE KTIDDLEDEV YAQKMKYKAI SEELDNALND ITSL
