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TPMM_TRICO
ID   TPMM_TRICO              Reviewed;         284 AA.
AC   P15846;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Tropomyosin, muscle;
OS   Trichostrongylus colubriformis (Black scour worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC   Trichostrongyloidea; Trichostrongylidae; Trichostrongylus.
OX   NCBI_TaxID=6319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2514356; DOI=10.1016/0166-6851(89)90151-5;
RA   Frenkel M.J., Savin K.W., Bakker R.E., Ward C.W.;
RT   "Characterization of cDNA clones coding for muscle tropomyosin of the
RT   nematode Trichostrongylus colubriformis.";
RL   Mol. Biochem. Parasitol. 37:191-200(1989).
RN   [2]
RP   PARTIAL PROTEIN SEQUENCE.
RX   PubMed=2759773; DOI=10.1016/0020-7519(89)90144-6;
RA   O'Donnell I.J., Dineen J.K., Wagland B., Letho S., Werkmeister J.A.,
RA   Ward C.W.;
RT   "A novel host-protective antigen from Trichostrongylus colubriformis.";
RL   Int. J. Parasitol. 19:327-335(1989).
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.
CC   -!- DEVELOPMENTAL STAGE: Present in L3 (third stage), L4 and adult worms.
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   -!- SIMILARITY: Belongs to the tropomyosin family. {ECO:0000305}.
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DR   EMBL; J04669; AAA30103.1; -; mRNA.
DR   PIR; A44980; A44980.
DR   AlphaFoldDB; P15846; -.
DR   SMR; P15846; -.
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   Coiled coil; Direct protein sequencing; Repeat.
FT   CHAIN           1..284
FT                   /note="Tropomyosin, muscle"
FT                   /id="PRO_0000205648"
FT   REGION          116..140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1..284
FT   COMPBIAS        116..135
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        277
FT                   /note="T -> R (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   284 AA;  33051 MW;  230573B1EE2449C1 CRC64;
     MDAIKKKMQA MKIEKDNALD RADAAEEKVR QITEKLERVE EELRDTQKKM MQTENDLDKA
     QEDLAAATSQ LEEKEKKVQE AEAEVAALNR RMTLLEEELE RAEERLKIAT EKLEEATHNV
     DESERVRKVM ENGSFQDEER ANTIEAQLKE AQMLAEEADR KYDEVARKLA MVEADLERAE
     ERAEAGENKI VELEEELRVV GNNLKSLEVS EEKALQREDS YEEQIRTISS RLKEAETRAE
     FAERSVQKLQ KEVDRLEDEL VHEKERYKAI SEELDSTFQE LSGY
 
 
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