TPM_CHIOP
ID TPM_CHIOP Reviewed; 284 AA.
AC A2V735;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 32.
DE RecName: Full=Tropomyosin {ECO:0000303|PubMed:20198602};
DE AltName: Full=Tropomyosin, slow-tonic isoform {ECO:0000303|PubMed:17263503, ECO:0000312|EMBL:BAF47267.1};
DE Short=Tm-Chio-tonic {ECO:0000312|EMBL:BAF47267.1};
GN Name=TM1 {ECO:0000250|UniProtKB:O44119};
OS Chionoecetes opilio (Crab-beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Brachyura;
OC Eubrachyura; Majoidea; Majidae; Chionoecetes.
OX NCBI_TaxID=41210;
RN [1] {ECO:0000312|EMBL:BAF47267.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND ALLERGEN.
RC TISSUE=Muscle {ECO:0000269|PubMed:17263503};
RX PubMed=17263503; DOI=10.1021/jf062798x;
RA Motoyama K., Suma Y., Ishizaki S., Nagashima Y., Shiomi K.;
RT "Molecular cloning of tropomyosins identified as allergens in six species
RT of crustaceans.";
RL J. Agric. Food Chem. 55:985-991(2007).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 8-284, SUBUNIT, MASS SPECTROMETRY, ALLERGENICITY, AND
RP ACETYLATION AT MET-1.
RC TISSUE=Muscle {ECO:0000269|PubMed:20198602};
RX PubMed=20198602; DOI=10.1002/jms.1721;
RA Abdel Rahman A.M., Lopata A.L., O'Hehir R.E., Robinson J.J., Banoub J.H.,
RA Helleur R.J.;
RT "Characterization and de novo sequencing of snow crab tropomyosin enzymatic
RT peptides by both electrospary ionization and matrix-assisted laser
RT desorption ionization QqToF tandemmass spectrometry.";
RL J. Mass Spectrom. 45:372-381(2010).
CC -!- FUNCTION: Tropomyosin, in association with the troponin complex, plays
CC a central role in the calcium dependent regulation of muscle
CC contraction. {ECO:0000250|UniProtKB:Q22866}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20198602}.
CC -!- TISSUE SPECIFICITY: Expressed in leg muscle and chest protection muscle
CC (at protein level). {ECO:0000269|PubMed:17263503}.
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. {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=32733; Mass_error=6.5; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:20198602};
CC -!- ALLERGEN: Causes an allergic reaction in human.
CC {ECO:0000269|PubMed:17263503, ECO:0000269|PubMed:20198602}.
CC -!- SIMILARITY: Belongs to the tropomyosin family. {ECO:0000255}.
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DR EMBL; AB270634; BAF47267.1; -; mRNA.
DR AlphaFoldDB; A2V735; -.
DR SMR; A2V735; -.
DR Allergome; 3807; Chi o 1.
DR Allergome; 4087; Chi o 1.0101.
DR iPTMnet; A2V735; -.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
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 Acetylation; Allergen; Coiled coil; Direct protein sequencing; Repeat.
FT CHAIN 1..284
FT /note="Tropomyosin"
FT /id="PRO_0000398787"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1..284
FT /evidence="ECO:0000250|UniProtKB:O44119"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:20198602"
SQ SEQUENCE 284 AA; 32675 MW; 357A164032C6B96E CRC64;
MDAIKKKMQA MKLEKDNAMD KADTLEQQNK EANLRAEKTE EEIRANQKKS QLVENELDHA
QEQLSAATHK LVEKEKAFAN AEGEVAALNR RIQLLEEDLE RSEERLNTAT TKLAEASQAA
DESERMRKVL ENRSLSDEER MDALENQLKE ARFLAEEADR KYDEVARKLA MVEADLERAE
ERAESGESKI VELEEELRVV GNNLKSLEVS EEKANQREET YKEQIKTLAN KLKAAEARAE
FAERSVQKLQ KEVDRLEDEL VNEKEKYKNI ADEMDQAFSE LSGF
