TPM_HOMAM
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 25-MAY-2022, entry version 68.
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 InterPro; IPR000533; Tropomyosin.
DR Pfam; PF00261; Tropomyosin; 1.
DR PRINTS; PR00194; TROPOMYOSIN.
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