ID   TPM_PENMO               Reviewed;         284 AA.
AC   A1KYZ2;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Tropomyosin {ECO:0000303|Ref.3, ECO:0000312|EMBL:AAX37288.1};
DE   AltName: Full=Major allergen Pen m 1 {ECO:0000303|PubMed:23840718};
DE   AltName: Full=Tropomyosin, fast isoform {ECO:0000303|PubMed:17263503, ECO:0000312|EMBL:BAF47262.1};
DE            Short=Tm-Penm-fast {ECO:0000312|EMBL:BAF47262.1};
DE   AltName: Allergen=Pen m 1.0101 {ECO:0000305};
GN   Name=TM1 {ECO:0000250|UniProtKB:O44119};
OS   Penaeus monodon (Giant tiger prawn).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC   Penaeoidea; Penaeidae; Penaeus.
OX   NCBI_TaxID=6687;
RN   [1] {ECO:0000312|EMBL:AAX37288.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Chew F.T., Nah H.L.;
RT   "Cloning of tropomyosin from Penaeus monodon.";
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000312|EMBL:BAF47262.1}
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   [3] {ECO:0000305}
RP   PROTEIN SEQUENCE, TISSUE SPECIFICITY, ALLERGEN, AND ACETYLATION AT MET-1.
RC   TISSUE=Muscle {ECO:0000269|Ref.3};
RX   DOI=10.1002/rcm.4664;
RA   Abdel Rahman A.M., Kamath S., Lopata A.L., Helleur R.J.;
RT   "Analysis of the allergenic proteins in black tiger prawn (Penaeus monodon)
RT   and characterization of the major allergen tropomyosin using mass
RT   spectrometry.";
RL   Rapid Commun. Mass Spectrom. 24:2462-2470(2010).
RN   [4]
RP   ALLERGEN.
RX   PubMed=23840718; DOI=10.1371/journal.pone.0067487;
RA   Abramovitch J.B., Kamath S., Varese N., Zubrinich C., Lopata A.L.,
RA   O'Hehir R.E., Rolland J.M.;
RT   "IgE Reactivity of Blue Swimmer Crab (Portunus pelagicus) Tropomyosin, Por
RT   p 1, and Other Allergens; Cross-Reactivity with Black Tiger Prawn and
RT   Effects of Heating.";
RL   PLoS ONE 8:E67487-E67487(2013).
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 muscle (at protein level).
CC       {ECO:0000269|PubMed:17263503, ECO:0000269|Ref.3}.
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   -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE of
CC       patients allergic to crustaceans (PubMed:17263503, Ref.3,
CC       PubMed:23840718). Heating increases IgE-binding activity. Cross-reacts
CC       with blue swimmer crab tropomyosin allergen Por p 1.0101. Recombinant
CC       protein causes activation of basophils (PubMed:23840718).
CC       {ECO:0000269|PubMed:17263503, ECO:0000269|PubMed:23840718,
CC       ECO:0000269|Ref.3}.
CC   -!- SIMILARITY: Belongs to the tropomyosin family. {ECO:0000255}.
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; AY827100; AAX37288.1; -; mRNA.
DR   EMBL; AB270629; BAF47262.1; -; mRNA.
DR   AlphaFoldDB; A1KYZ2; -.
DR   SMR; A1KYZ2; -.
DR   Allergome; 3410; Pen m 1.0101.
DR   Allergome; 972; Pen m 1.
DR   EnsemblMetazoa; XM_037944040.1; XP_037799968.1; LOC119594951.
DR   EnsemblMetazoa; XM_037944042.1; XP_037799970.1; LOC119594951.
DR   EnsemblMetazoa; XM_037944043.1; XP_037799971.1; LOC119594951.
DR   EnsemblMetazoa; XM_037944044.1; XP_037799972.1; LOC119594951.
DR   EnsemblMetazoa; XM_037944045.1; XP_037799973.1; LOC119594951.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0040011; P:locomotion; ISS:UniProtKB.
DR   GO; GO:0003012; P:muscle system process; IEP:UniProtKB.
DR   GO; GO:0006937; P:regulation of muscle contraction; ISS:UniProtKB.
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:SF45; TROPOMYOSIN-1, ISOFORMS 33_34; 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   Acetylation; Allergen; Coiled coil; Direct protein sequencing;
KW   Muscle protein; Repeat.
FT   CHAIN           1..284
FT                   /note="Tropomyosin"
FT                   /id="PRO_0000398788"
FT   REGION          1..51
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|Ref.3"
SQ   SEQUENCE   284 AA;  32849 MW;  BE53B602C37E85E2 CRC64;
     MDAIKKKMQA MKLEKDNAMD RADTLEQQNK EANNRAEKSE EEVHNLQKRM QQLENDLDQV
     QESLLKANIQ LVEKDKALSN AEGEVAALNR RIQLLEEDLE RSEERLNTAT TKLAEASQAA
     DESERMRKVL ENRSLSDEER MDALENQLKE ARFLAEEADR KYDEVARKLA MVEADLERAE
     ERAETGESKI VELEEELRVV GNNLKSLEVS EEKANQREEA YKEQIKTLTN KLKAAEARAE
     FAERSVQKLQ KEVDRLEDEL VNEKEKYKSI TDELDQTFSE LSGY
//