TPM1_CHICK
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 03-AUG-2022, entry version 160.
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.ENSGALP00000005562; -.
DR iPTMnet; P04268; -.
DR Ensembl; ENSGALT00000005572; ENSGALP00000005562; ENSGALG00000003521. [P04268-4]
DR Ensembl; ENSGALT00000083084; ENSGALP00000044392; ENSGALG00000003521. [P04268-7]
DR Ensembl; ENSGALT00000084241; ENSGALP00000062806; ENSGALG00000003521. [P04268-5]
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 OrthoDB; 1576041at2759; -.
DR PhylomeDB; P04268; -.
DR TreeFam; TF351519; -.
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 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 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 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
