TPM_TODPA
ID TPM_TODPA Reviewed; 284 AA.
AC Q2V0V2;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 36.
DE RecName: Full=Tropomyosin Tod p 1.0102 {ECO:0000305};
DE AltName: Full=Allergen Tod p 1 {ECO:0000303|PubMed:8939158};
DE AltName: Full=Allergen Tod p 1.0101 {ECO:0000305};
DE AltName: Full=Tropomyosin Tod p 1 {ECO:0000303|PubMed:25530105};
DE Short=TMTp1 {ECO:0000303|PubMed:25530105};
DE AltName: Allergen=Tod p 1.0102 {ECO:0000305};
GN Name=TM {ECO:0000305};
OS Todarodes pacificus (Japanese flying squid) (Ommastrephes pacificus).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Decapodiformes; Teuthida; Oegopsina; Ommastrephidae; Todarodes.
OX NCBI_TaxID=6637 {ECO:0000312|EMBL:BAE54431.1};
RN [1] {ECO:0000312|EMBL:BAE54431.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND ALLERGEN.
RC TISSUE=Mantle muscle {ECO:0000303|PubMed:16904802};
RX PubMed=16904802; DOI=10.1016/j.fct.2006.06.018;
RA Motoyama K., Ishizaki S., Nagashima Y., Shiomi K.;
RT "Cephalopod tropomyosins: identification as major allergens and molecular
RT cloning.";
RL Food Chem. Toxicol. 44:1997-2002(2006).
RN [2]
RP PROTEIN SEQUENCE OF 37-48; 50-76; 129-146 AND 252-264, PTM, AND ALLERGEN.
RX PubMed=8939158; DOI=10.1016/s0091-6749(96)80011-x;
RA Miyazawa H., Fukamachi H., Inagaki Y., Reese G., Daul C.B., Lehrer S.B.,
RA Inouye S., Sakaguchi M.;
RT "Identification of the first major allergen of a squid (Todarodes
RT pacificus).";
RL J. Allergy Clin. Immunol. 98:948-953(1996).
RN [3]
RP TISSUE SPECIFICITY, ALLERGEN, BIOTECHNOLOGY, AND CIRCULAR DICHROISM
RP ANALYSIS.
RX PubMed=17147442; DOI=10.1021/jf061070d;
RA Nakamura A., Sasaki F., Watanabe K., Ojima T., Ahn D.H., Saeki H.;
RT "Changes in allergenicity and digestibility of squid tropomyosin during the
RT Maillard reaction with ribose.";
RL J. Agric. Food Chem. 54:9529-9534(2006).
RN [4]
RP TISSUE SPECIFICITY, ALLERGEN, AND CIRCULAR DICHROISM ANALYSIS.
RX PubMed=25530105; DOI=10.1016/j.fct.2014.12.002;
RA Jin Y., Deng Y., Qian B., Zhang Y., Liu Z., Zhao Y.;
RT "Allergenic response to squid (Todarodes pacificus) tropomyosin Tod p1
RT structure modifications induced by high hydrostatic pressure.";
RL Food Chem. Toxicol. 76:86-93(2015).
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:0000250|UniProtKB:A2V735}.
CC -!- TISSUE SPECIFICITY: Expressed in mantle muscle (at protein level).
CC {ECO:0000269|PubMed:16904802, ECO:0000269|PubMed:17147442,
CC ECO:0000269|PubMed:25530105}.
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 -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:8939158}.
CC -!- ALLERGEN: Causes an allergic reaction in human (PubMed:16904802,
CC PubMed:8939158, PubMed:17147442, PubMed:25530105). Binds to IgE of
CC patients allergic to crustaceans (shrimp and crab) (PubMed:16904802).
CC Binds to IgE of patients residing in Japan and China allergic to squid
CC (PubMed:8939158, PubMed:17147442, PubMed:25530105). Binds to IgE of
CC American patients allergic to shrimp (PubMed:8939158). The
CC allergenicity of this protein is reduced significantly by its reaction
CC of lysines with ribose during the Maillard reaction (glycation), and to
CC a lesser extent by digestion with pepsin. On the other hand,
CC modification of the lysine residues in this protein using 2,4,6-
CC trinitrobenzenesulfonic acid (TNBS) has no effect on allergenicity
CC (PubMed:17147442). Treatment by high hydrostatic pressure (HHP) reduces
CC allergenicity (400 and 600 MPa more effectively than 200 MPa)
CC (PubMed:25530105). {ECO:0000269|PubMed:16904802,
CC ECO:0000269|PubMed:17147442, ECO:0000269|PubMed:25530105,
CC ECO:0000269|PubMed:8939158}.
CC -!- BIOTECHNOLOGY: The reaction of this protein with ribose in the Maillard
CC reaction may be useful in development of processed seafood with low
CC allergenicity. {ECO:0000305|PubMed:17147442}.
CC -!- SIMILARITY: Belongs to the tropomyosin family. {ECO:0000305}.
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DR EMBL; AB218915; BAE54431.1; -; mRNA.
DR AlphaFoldDB; Q2V0V2; -.
DR SMR; Q2V0V2; -.
DR Allergome; 4099; Tod p 1.0102.
DR Allergome; 649; Tod p 1.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0006937; P:regulation of muscle contraction; ISS:UniProtKB.
DR InterPro; IPR000533; Tropomyosin.
DR Pfam; PF00261; Tropomyosin; 1.
DR PRINTS; PR00194; TROPOMYOSIN.
PE 1: Evidence at protein level;
KW Allergen; Coiled coil; Direct protein sequencing; Muscle protein; Repeat.
FT CHAIN 1..284
FT /note="Tropomyosin Tod p 1.0102"
FT /id="PRO_0000447721"
FT REGION 103..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 15..273
FT /evidence="ECO:0000255"
SQ SEQUENCE 284 AA; 32673 MW; D9D0B3FB2999D595 CRC64;
MDAIKKKMLA MKMEKEVATD KAEQTEQSLR DLEAAKNTIE EDLSTLQKKY SNLENDFDNA
KENLTVANTN LEASEKRVNE CESEIQGLNR RIQLLEEDLE RSEERLTSAQ SKLEDASKAA
DESERGRKVL ENRSQGDEER IDLLEKQLEE AKWIAEDADR KFDEAARKLA ITEVDLERAE
ARLEAAEAKI VELEEELKVV GNNMKSLEIS EQEASQREDS YEETIRDLTH RLKEAENRAA
EAERTVSKLQ KEVDRLEDEL LAEKERYKSI SDELDQTFAE LAGY
