TPM1_BOVIN
ID TPM1_BOVIN Reviewed; 284 AA.
AC Q5KR49;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Tropomyosin alpha-1 chain;
DE AltName: Full=Alpha-tropomyosin;
DE AltName: Full=Tropomyosin-1;
GN Name=TPM1;
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].
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].
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-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. {ECO:0000250|UniProtKB:P09493}.
CC -!- SUBUNIT: Homodimer. Heterodimer of an alpha (TPM1, TPM3 or TPM4) and a
CC beta (TPM2) chain. Interacts with HRG (via the HRR domain); the
CC interaction contributes to the antiangiogenic properties of the
CC histidine/proline-rich region (HRR) of HRG. Interacts (via N-terminus)
CC with LMOD2 (via N-terminus) and TMOD1 (via N-terminus).
CC {ECO:0000250|UniProtKB:P04268, ECO:0000250|UniProtKB:P04692,
CC ECO:0000250|UniProtKB:P09493}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P04692}. Note=Associates with F-actin stress
CC fibers. {ECO:0000250|UniProtKB:P04692}.
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 at Ser-283 by DAPK1 in response to oxidative stress
CC and this phosphorylation enhances stress fiber formation in endothelial
CC cells. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the tropomyosin family. {ECO:0000305}.
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DR EMBL; AB198070; BAD86590.1; -; mRNA.
DR EMBL; BC102909; AAI02910.1; -; mRNA.
DR RefSeq; NP_001013608.1; NM_001013590.2.
DR AlphaFoldDB; Q5KR49; -.
DR SMR; Q5KR49; -.
DR IntAct; Q5KR49; 4.
DR MINT; Q5KR49; -.
DR PaxDb; Q5KR49; -.
DR PeptideAtlas; Q5KR49; -.
DR PRIDE; Q5KR49; -.
DR Ensembl; ENSBTAT00000044796; ENSBTAP00000042255; ENSBTAG00000005373.
DR GeneID; 281544; -.
DR KEGG; bta:281544; -.
DR CTD; 7168; -.
DR VEuPathDB; HostDB:ENSBTAG00000005373; -.
DR VGNC; VGNC:106994; TPM1.
DR GeneTree; ENSGT01030000234542; -.
DR InParanoid; Q5KR49; -.
DR OMA; DEASRMC; -.
DR OrthoDB; 1576041at2759; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000005373; Expressed in biceps femoris and 106 other tissues.
DR ExpressionAtlas; Q5KR49; 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:0097512; C:cardiac myofibril; IDA:CAFA.
DR GO; GO:0030016; C:myofibril; IDA:CAFA.
DR GO; GO:0030017; C:sarcomere; IDA:CAFA.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
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:0060048; P:cardiac muscle contraction; 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 2: Evidence at transcript level;
KW Acetylation; Actin-binding; Coiled coil; Cytoplasm; Cytoskeleton;
KW Muscle protein; Phosphoprotein; Reference proteome.
FT CHAIN 1..284
FT /note="Tropomyosin alpha-1 chain"
FT /id="PRO_0000283716"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..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:P09493"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04692"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09493"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P58771"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P58771"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P58771"
FT MOD_RES 261
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P04692"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P58771"
FT MOD_RES 283
FT /note="Phosphoserine; by DAPK1"
FT /evidence="ECO:0000250|UniProtKB:P09493"
SQ SEQUENCE 284 AA; 32695 MW; 18DBC129191DC4E3 CRC64;
MDAIKKKMQM LKLDKENALD RAEQAEADKK AAEDRSKQLE DELVSLQKKL KATEDELDKY
SEALKDAQEK LELAEKKATD AEADVASLNR RIQLVEEELD RAQERLATAL QKLEEAEKAA
DESERGMKVI ESRAQKDEEK MEIQEIQLKE AKHIAEDADR KYEEVARKLV IIESDLERAE
ERAELSEGKC AELEEELKTV TNNLKSLEAQ AEKYSQKEDK YEEEIKVLSD KLKEAETRAE
FAERSVTKLE KSIDDLEDEL YAQKLKYKAI SEELDHALND MTSI
