TPM1_COTJA
ID TPM1_COTJA Reviewed; 284 AA.
AC P58773; P02559; P08942; P18442; P49437;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Tropomyosin alpha-1 chain;
DE AltName: Full=Alpha-tropomyosin;
DE AltName: Full=Tropomyosin-1;
GN Name=TPM1;
OS Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Perdicinae; Coturnix.
OX NCBI_TaxID=93934;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
RX PubMed=2701936; DOI=10.1093/nar/17.5.2099;
RA Lindquester G.J., Flach J.E., Fleenor D.E., Hickman K.H., Devlin R.B.;
RT "Avian tropomyosin gene expression.";
RL Nucleic Acids Res. 17:2099-2118(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
RX PubMed=2445743; DOI=10.1016/s0021-9258(18)47688-0;
RA Pearson-White S.H., Emerson C.P. Jr.;
RT "A novel hybrid alpha-tropomyosin in fibroblasts is produced by alternative
RT splicing of transcripts from the skeletal muscle alpha-tropomyosin gene.";
RL J. Biol. Chem. 262:15998-16010(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=3786149; DOI=10.1093/nar/14.22.9193;
RA Flach J.E., Lindquester G.J., Berish S., Hickman K.H., Devlin R.;
RT "Analysis of tropomyosin cDNAs isolated from skeletal and smooth muscle
RT mRNA.";
RL Nucleic Acids Res. 14:9193-9211(1986).
RN [4]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
RX PubMed=3818657; DOI=10.1016/s0021-9258(18)61393-6;
RA Hallauer P.L., Hastings K.E.M., Baldwin A.S. Jr., Pearson-White S.H.,
RA Merrifield P.A., Emerson C.P. Jr.;
RT "Closely related alpha-tropomyosin mRNAs in quail fibroblasts and skeletal
RT muscle cells.";
RL J. Biol. Chem. 262:3590-3596(1987).
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.
CC {ECO:0000250|UniProtKB:P04268, ECO:0000250|UniProtKB:P04692}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P04692}. Note=Associates with F-actin stress
CC fibers. {ECO:0000250|UniProtKB:P04692}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=Skeletal muscle, cC402, SK74;
CC IsoId=P58773-1; Sequence=Displayed;
CC Name=2; Synonyms=Smooth muscle;
CC IsoId=P58773-2; Sequence=VSP_006592, VSP_006593;
CC Name=3; Synonyms=Fibroblast, cC401;
CC IsoId=P58773-3; Sequence=VSP_006593;
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; X16230; CAA34344.1; -; Genomic_DNA.
DR EMBL; X16236; CAA34344.1; JOINED; Genomic_DNA.
DR EMBL; X16237; CAA34344.1; JOINED; Genomic_DNA.
DR EMBL; X16238; CAA34344.1; JOINED; Genomic_DNA.
DR EMBL; X16239; CAA34344.1; JOINED; Genomic_DNA.
DR EMBL; X16240; CAA34344.1; JOINED; Genomic_DNA.
DR EMBL; X16230; CAA34343.1; -; Genomic_DNA.
DR EMBL; X16236; CAA34343.1; JOINED; Genomic_DNA.
DR EMBL; X16237; CAA34343.1; JOINED; Genomic_DNA.
DR EMBL; X16238; CAA34343.1; JOINED; Genomic_DNA.
DR EMBL; X16241; CAA34343.1; JOINED; Genomic_DNA.
DR EMBL; X04690; CAA28393.1; -; mRNA.
DR EMBL; M15043; AAA49511.1; -; mRNA.
DR EMBL; M17914; AAA49510.1; -; mRNA.
DR EMBL; M15044; AAA49508.1; -; mRNA.
DR PIR; A28499; A28499.
DR PIR; B28499; A26113.
DR PIR; S05445; S05445.
DR AlphaFoldDB; P58773; -.
DR SMR; P58773; -.
DR Proteomes; UP000694412; Unplaced.
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 2: Evidence at transcript level;
KW Actin-binding; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Muscle protein; Reference proteome.
FT CHAIN 1..284
FT /note="Tropomyosin alpha-1 chain"
FT /id="PRO_0000205626"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1..284
FT /evidence="ECO:0000250"
FT VAR_SEQ 42..80
FT /note="ELVALQKKLKGTEDELDKYSESLKDAQEKLELADKKATD -> DIVQLEKQL
FT RVTEDSRDQVLEELHKSEDSLLSAEEIAAK (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_006592"
FT VAR_SEQ 258..284
FT /note="DELYAQKLKYKAISEELDHALNDMTSI -> EKVAHAKEENLNMHQMLDQTL
FT LELNNM (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:2445743"
FT /id="VSP_006593"
SQ SEQUENCE 284 AA; 32766 MW; DBBBD3DB7F36DACB CRC64;
MDAIKKKMQM LKLDKENALD RAEQAEADKK AAEERSKQLE DELVALQKKL KGTEDELDKY
SESLKDAQEK LELADKKATD AESEVASLNR RIQLVEEELD RAQERLATAL QKLEEAEKAA
DESERGMKVI ENRAQKDEEK MEIQEIQLKE AKHIAEEADR KYEEVARKLV IIEGDLERAE
ERAELSESKC AELEEELKTV TNNLKSLEAQ AEKYSQKEDK YEEEIKVLTD KLKEAETRAE
FAERSVTKLE KSIDDLEDEL YAQKLKYKAI SEELDHALND MTSI
