ID TPM1_CHICK Reviewed; 284 AA. AC P04268; P02559; P08942; P18441; P18442; P49436; P49438; P49439; Q540N4; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 13-AUG-1987, sequence version 2. DT 27-MAR-2024, entry version 168. DE RecName: Full=Tropomyosin alpha-1 chain; DE AltName: Full=Alpha-tropomyosin; DE AltName: Full=Tropomyosin-1; GN Name=TPM1; 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 PROTEIN SEQUENCE (ISOFORM 1), AND ACETYLATION AT MET-1. RX PubMed=3997866; DOI=10.1016/s0021-9258(17)39601-1; RA Lau S.Y.M., Sanders C., Smillie L.B.; RT "Amino acid sequence of chicken gizzard gamma-tropomyosin."; RL J. Biol. Chem. 260:7257-7263(1985). RN [2] RP NUCLEOTIDE SEQUENCE (ISOFORM 1). RX PubMed=3671073; DOI=10.1093/nar/15.19.8105; RA Gooding C., Reinach F.C., Macleod A.R.; RT "Complete nucleotide sequence of the fast-twitch isoform of chicken RT skeletal muscle alpha-tropomyosin."; RL Nucleic Acids Res. 15:8105-8105(1987). RN [3] RP NUCLEOTIDE SEQUENCE (ISOFORMS 1; 2; 4; 5; 6 AND 7). RX PubMed=1748294; DOI=10.1016/0378-1119(91)90323-4; RA Lemonnier M., Balvay L., Mouly V., Libri D., Fiszman M.Y.; RT "The chicken gene encoding the alpha isoform of tropomyosin of fast-twitch RT muscle fibers: organization, expression and identification of the major RT proteins synthesized."; RL Gene 107:229-240(1991). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4). RC TISSUE=Body wall; RX PubMed=7820856; DOI=10.1002/cm.970290104; RA Fanning A.S., Wolenski J.S., Mooseker M.S., Izant J.G.; RT "Differential regulation of skeletal muscle myosin-II and brush border RT myosin-I enzymology and mechanochemistry by bacterially produced RT tropomyosin isoforms."; RL Cell Motil. Cytoskeleton 29:29-45(1994). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Heart, and Skeletal muscle; RA Denz C.R., Zajdel R.W., Dube S., Dube D.K.; RT "Identification, characterization, and expression of a novel alpha- RT tropomyosin isoform in cardiac tissues in developing chicken."; RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Red jungle fowl; RX PubMed=15592404; DOI=10.1038/nature03154; RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P., RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B., RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C., RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V., RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O., RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W., RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D., RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K., RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L., RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B., RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M., RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K., RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E., RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M., RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M., RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S., RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M., RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M., RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A., RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S., RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J., RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J., RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E., RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M., RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A., RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M., RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O., RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E., RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S., RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E., RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R., RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R., RA Wilson R.K.; RT "Sequence and comparative analysis of the chicken genome provide unique RT perspectives on vertebrate evolution."; RL Nature 432:695-716(2004). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 24-284 (ISOFORM 1). RX PubMed=7128591; DOI=10.1111/j.1432-1033.1982.tb06778.x; RA McLeod A.R.; RT "Distinct alpha-tropomyosin mRNA sequences in chicken skeletal muscle."; RL Eur. J. Biochem. 126:293-297(1982). RN [8] RP NUCLEOTIDE SEQUENCE OF 189-213 (ISOFORM 4). RC TISSUE=Muscle; RX PubMed=2762137; DOI=10.1093/nar/17.13.5400; RA Lemonnier M., Libri D., Fiszman M.Y.; RT "Chick alpha tropomyosin gene contains three sets of mutually exclusive RT alternatively spliced exons."; RL Nucleic Acids Res. 17:5400-5400(1989). RN [9] RP INTERACTION WITH HRG. RX PubMed=15313924; DOI=10.1158/0008-5472.can-04-0440; RA Donate F., Juarez J.C., Guan X., Shipulina N.V., Plunkett M.L., RA Tel-Tsur Z., Shaw D.E., Morgan W.T., Mazar A.P.; RT "Peptides derived from the histidine-proline domain of the histidine- RT proline-rich glycoprotein bind to tropomyosin and have antiangiogenic and RT antitumor activities."; RL Cancer Res. 64:5812-5817(2004). RN [10] RP INTERACTION WITH HRG. RX PubMed=15269838; DOI=10.1160/th04-02-0073; RA Guan X., Juarez J.C., Qi X., Shipulina N.V., Shaw D.E., Morgan W.T., RA McCrae K.R., Mazar A.P., Donate F.; RT "Histidine-proline rich glycoprotein (HPRG) binds and transduces anti- RT angiogenic signals through cell surface tropomyosin on endothelial cells."; RL Thromb. Haemost. 92:403-412(2004). RN [11] RP SUBUNIT. RX PubMed=23832280; DOI=10.1007/s10974-013-9353-x; RA Janco M., Suphamungmee W., Li X., Lehman W., Lehrer S.S., Geeves M.A.; RT "Polymorphism in tropomyosin structure and function."; RL J. Muscle Res. Cell Motil. 34:177-187(2013). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-81. RX PubMed=11438684; DOI=10.1073/pnas.131219198; RA Brown J.H., Kim K.H., Jun G., Greenfield N.J., Dominguez R., Volkmann N., RA Hitchcock-DeGregori S.E., Cohen C.; RT "Deciphering the design of the tropomyosin molecule."; RL Proc. Natl. Acad. Sci. U.S.A. 98:8496-8501(2001). 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 (PubMed:23832280). Heterodimer of an alpha (TPM1, CC TPM3 or TPM4) and a beta (TPM2) chain (By similarity). Interacts with CC HRG (via the HRR domain); the interaction contributes to the CC antiangiogenic properties of the histidine/proline-rich region (HRR) of CC HRG (PubMed:15269838, PubMed:15313924). {ECO:0000250|UniProtKB:P04692, CC ECO:0000269|PubMed:15269838, ECO:0000269|PubMed:15313924}. CC -!- INTERACTION: CC P04268; Q99LM3: Smtnl1; Xeno; NbExp=3; IntAct=EBI-8073544, EBI-8073484; 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=6; CC Comment=Additional isoforms seem to exist.; CC Name=1; Synonyms=Fast-twitch skeletal muscle, CTm7; CC IsoId=P04268-1; Sequence=Displayed; CC Name=2; Synonyms=Smooth muscle; CC IsoId=P04268-2; Sequence=VSP_006588, VSP_006590; CC Name=4; Synonyms=Fibroblast F1; CC IsoId=P04268-4; Sequence=VSP_006589, VSP_006590; CC Name=5; Synonyms=Fibroblast F2; CC IsoId=P04268-5; Sequence=VSP_006590; CC Name=6; Synonyms=Brain major; CC IsoId=P04268-6; Sequence=VSP_006587, VSP_006591; CC Name=7; Synonyms=Brain minor; CC IsoId=P04268-7; Sequence=VSP_006591; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M32441; AAA48610.1; -; mRNA. DR EMBL; X57991; CAA41056.1; -; Genomic_DNA. DR EMBL; X57993; CAA41056.1; JOINED; Genomic_DNA. DR EMBL; X57994; CAA41056.1; JOINED; Genomic_DNA. DR EMBL; X57995; CAA41056.1; JOINED; Genomic_DNA. DR EMBL; M69144; AAA48577.1; -; Genomic_DNA. DR EMBL; M69140; AAA48577.1; JOINED; Genomic_DNA. DR EMBL; M69142; AAA48577.1; JOINED; Genomic_DNA. DR EMBL; M69143; AAA48577.1; JOINED; Genomic_DNA. DR EMBL; X16090; CAA34217.1; ALT_SEQ; Genomic_DNA. DR EMBL; X57991; CAA41059.1; -; Genomic_DNA. DR EMBL; X57993; CAA41059.1; JOINED; Genomic_DNA. DR EMBL; X57994; CAA41059.1; JOINED; Genomic_DNA. DR EMBL; X57996; CAA41059.1; JOINED; Genomic_DNA. DR EMBL; X57991; CAA41058.1; -; Genomic_DNA. DR EMBL; X57993; CAA41058.1; JOINED; Genomic_DNA. DR EMBL; X57994; CAA41058.1; JOINED; Genomic_DNA. DR EMBL; X57996; CAA41058.1; JOINED; Genomic_DNA. DR EMBL; X57991; CAA41057.1; -; Genomic_DNA. DR EMBL; X57993; CAA41057.1; JOINED; Genomic_DNA. DR EMBL; X57994; CAA41057.1; JOINED; Genomic_DNA. DR EMBL; X57996; CAA41057.1; JOINED; Genomic_DNA. DR EMBL; M36336; AAA65120.1; -; mRNA. DR EMBL; M36337; AAA65121.1; -; mRNA. DR EMBL; AY150210; AAN75276.1; -; mRNA. DR EMBL; AADN02040437; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AADN02040438; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; J00910; AAA49113.1; -; mRNA. DR PIR; S24399; TMCHA. DR PIR; S24400; TMCHS2. DR PIR; S24401; S24401. DR PIR; S24402; S24402. DR RefSeq; NP_990732.1; NM_205401.1. [P04268-4] DR RefSeq; XP_015134260.1; XM_015278774.1. [P04268-1] DR RefSeq; XP_015134264.1; XM_015278778.1. [P04268-5] DR RefSeq; XP_015134271.1; XM_015278785.1. [P04268-7] DR PDB; 1IC2; X-ray; 2.00 A; A/B/C/D=1-80. DR PDB; 3MTU; X-ray; 2.10 A; A/B/C/D=1-29, E/F=257-284. DR PDB; 3MUD; X-ray; 2.20 A; A/B=246-257, C/D=1-29. DR PDB; 3U1A; X-ray; 2.00 A; A/B/C/D=1-81. DR PDB; 3U1C; X-ray; 1.80 A; A/B=1-98. DR PDBsum; 1IC2; -. DR PDBsum; 3MTU; -. DR PDBsum; 3MUD; -. DR PDBsum; 3U1A; -. DR PDBsum; 3U1C; -. DR AlphaFoldDB; P04268; -. DR BMRB; P04268; -. DR SMR; P04268; -. DR IntAct; P04268; 1. DR MINT; P04268; -. DR STRING; 9031.ENSGALP00000056013; -. DR iPTMnet; P04268; -. DR PaxDb; 9031-ENSGALP00000005562; -. DR Ensembl; ENSGALT00010059947.1; ENSGALP00010036707.1; ENSGALG00010024570.1. [P04268-4] DR GeneID; 396366; -. DR KEGG; gga:396366; -. DR CTD; 7168; -. DR VEuPathDB; HostDB:geneid_396366; -. DR eggNOG; KOG1003; Eukaryota. DR GeneTree; ENSGT01030000234542; -. DR InParanoid; P04268; -. DR PhylomeDB; P04268; -. DR TreeFam; TF351519; -. DR Reactome; R-GGA-390522; Striated Muscle Contraction. DR Reactome; R-GGA-445355; Smooth Muscle Contraction. DR EvolutionaryTrace; P04268; -. DR PRO; PR:P04268; -. DR Proteomes; UP000000539; Chromosome 10. DR Bgee; ENSGALG00000003521; Expressed in muscle tissue and 14 other cell types or tissues. DR ExpressionAtlas; P04268; 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:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IDA:AgBase. DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB. DR GO; GO:0008092; F:cytoskeletal protein binding; IPI:AgBase. 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 Gene3D; 1.20.5.170; -; 2. DR Gene3D; 1.20.5.340; -; 1. DR InterPro; IPR000533; Tropomyosin. DR PANTHER; PTHR19269; TROPOMYOSIN; 1. DR PANTHER; PTHR19269:SF80; TROPOMYOSIN ALPHA-1 CHAIN; 1. DR Pfam; PF00261; Tropomyosin; 1. DR PRINTS; PR00194; TROPOMYOSIN. DR SUPFAM; SSF57997; Tropomyosin; 1. 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 alpha-1 chain" FT /id="PRO_0000205625" FT REGION 1..38 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:3997866" FT VAR_SEQ 1..80 FT /note="MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEERSKQLEDELVALQKKLKG FT TEDELDKYSESLKDAQEKLELADKKATD -> MAALSSLEAVRKKIRSLQEQADAAEER FT AGKLQREVDQERALREE (in isoform 6)" FT /evidence="ECO:0000305" FT /id="VSP_006587" FT VAR_SEQ 42..80 FT /note="ELVALQKKLKGTEDELDKYSESLKDAQEKLELADKKATD -> DIVQLEKQL FT RVTEDSRDQVLEELHKSEDSLLFAEENAAK (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_006588" FT VAR_SEQ 189..212 FT /note="KCAELEEELKTVTNNLKSLEAQAE -> QVRQLEEQLRIMDQTLKALMAAED FT (in isoform 4)" FT /evidence="ECO:0000303|PubMed:7820856" FT /id="VSP_006589" FT VAR_SEQ 258..284 FT /note="DELYAQKLKYKAISEELDHALNDMTSI -> EKVAHAKEENLNMHQMLDQTL FT LELNNM (in isoform 2, isoform 4 and isoform 5)" FT /evidence="ECO:0000303|PubMed:7820856" FT /id="VSP_006590" FT VAR_SEQ 259..284 FT /note="ELYAQKLKYKAISEELDHALNDMTSI -> QLYQQLEQNSRLTNELKLALNE FT D (in isoform 6 and isoform 7)" FT /evidence="ECO:0000305" FT /id="VSP_006591" FT VARIANT 171 FT /note="I -> V" FT VARIANT 175 FT /note="D -> E" FT CONFLICT 34 FT /note="E -> D (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 45 FT /note="A -> S (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 63 FT /note="S -> A (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 75 FT /note="D -> E (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 83..84 FT /note="SE -> AD (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 132 FT /note="N -> S (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 157 FT /note="E -> D (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 165 FT /note="V -> A (in Ref. 2; AAA48610)" FT /evidence="ECO:0000305" FT CONFLICT 172 FT /note="I -> L (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 174 FT /note="G -> S (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 188 FT /note="S -> G (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 229 FT /note="T -> S (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT HELIX 1..96 FT /evidence="ECO:0007829|PDB:3U1C" FT HELIX 267..283 FT /evidence="ECO:0007829|PDB:3MTU" 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 //