ID   TPM_HOMAM               Reviewed;         284 AA.
AC   O44119; O44120;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=Tropomyosin;
DE   AltName: Allergen=Hom a 1;
GN   Name=TM1;
OS   Homarus americanus (American lobster).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Astacidea;
OC   Nephropoidea; Nephropidae; Homarus.
OX   NCBI_TaxID=6706;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS FAST MUSCLE TYPE AND SLOW MUSCLE 1).
RC   TISSUE=Skeletal muscle;
RX   PubMed=9536438; DOI=10.1023/a:1005352410725;
RA   Mykles D.L., Cotton J.L.S., Taniguchi H., Sano K., Maeda Y.;
RT   "Cloning of tropomyosins from lobster (Homarus americanus) striated
RT   muscles: fast and slow isoforms may be generated from the same
RT   transcript.";
RL   J. Muscle Res. Cell Motil. 19:105-115(1998).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX   PubMed=8843164; DOI=10.1016/0014-5793(96)00949-0;
RA   Miegel A., Sano K., Yamamoto K., Maeda K., Maeda Y., Taniguchi H., Yao M.,
RA   Wakatsuki S.;
RT   "Production and crystallization of lobster muscle tropomyosin expressed in
RT   Sf9 cells.";
RL   FEBS Lett. 394:201-205(1996).
CC   -!- FUNCTION: Tropomyosin, in association with the troponin complex, plays
CC       a central role in the calcium dependent regulation of muscle
CC       contraction.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Slow muscle 1; Synonyms=STM1;
CC         IsoId=O44119-1; Sequence=Displayed;
CC       Name=Fast muscle type; Synonyms=FTM;
CC         IsoId=O44119-2; Sequence=VSP_006615;
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   -!- ALLERGEN: Causes an allergic reaction in human.
CC   -!- SIMILARITY: Belongs to the tropomyosin family. {ECO:0000305}.
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DR   EMBL; AF034953; AAC48287.1; -; mRNA.
DR   EMBL; AF034954; AAC48288.1; -; mRNA.
DR   PIR; S74168; S74168.
DR   AlphaFoldDB; O44119; -.
DR   SMR; O44119; -.
DR   Allergome; 3320; Hom a 1.0101.
DR   Allergome; 3321; Hom a 1.0102.
DR   Allergome; 410; Hom a 1.
DR   EnsemblMetazoa; XM_042385142.1; XP_042241076.1; LOC121878757. [O44119-2]
DR   EnsemblMetazoa; XM_042385144.1; XP_042241078.1; LOC121878757. [O44119-1]
DR   EnsemblMetazoa; XM_042385153.1; XP_042241087.1; LOC121878757. [O44119-2]
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   Allergen; Alternative splicing; Coiled coil; Repeat.
FT   CHAIN           1..284
FT                   /note="Tropomyosin"
FT                   /id="PRO_0000205674"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1..284
FT   VAR_SEQ         39..79
FT                   /note="TEEEIRITHKKMQQVENELDQVQEQLSLANTKLEEKEKALQ -> SEEEVHN
FT                   LQKRMQQLENDLDQVQESLLKANTQLEEKDKALS (in isoform Fast muscle
FT                   type)"
FT                   /evidence="ECO:0000303|PubMed:9536438"
FT                   /id="VSP_006615"
SQ   SEQUENCE   284 AA;  32907 MW;  C238DDB4E693243A CRC64;
     MDAIKKKMQA MKLEKDNAMD RADTLEQQNK EANIRAEKTE EEIRITHKKM QQVENELDQV
     QEQLSLANTK LEEKEKALQN AEGEVAALNR RIQLLEEDLE RSEERLNTAT TKLAEASQAA
     DESERMRKVL ENRSLSDEER MDALENQLKE ARFLAEEADR KYDEVARKLA MVEADLERAE
     ERAETGESKI VELEEELRVV GNNLKSLEVS EEKANQREEA YKEQIKTLAN KLKAAEARAE
     FAERSVQKLQ KEVDRLEDEL VNEKEKYKSI TDELDQTFSE LSGY
//