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TPM2_BOMMO
ID   TPM2_BOMMO              Reviewed;         285 AA.
AC   Q1HPQ0; P82201; P82203; Q1HPP9; Q1HPU1;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   25-MAY-2022, entry version 49.
DE   RecName: Full=Tropomyosin-2;
OS   Bombyx mori (Silk moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Bombycidae; Bombycinae; Bombyx.
OX   NCBI_TaxID=7091;
RN   [1] {ECO:0000312|EMBL:ABF51441.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
RA   Niu B.L., Meng Z.Q., Weng H.B., Shen W.F., He L.H., Zheng K.F., Ye S.T.,
RA   Lin T.B., Chen J.E.;
RT   "Blast silkworm EST database for functional genes.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 21-40 AND 36-55.
RC   STRAIN=Xinhang X Keming {ECO:0000269|PubMed:11280994};
RC   TISSUE=Body wall {ECO:0000269|PubMed:11280994}, and
RC   Fat body {ECO:0000269|PubMed:11280994};
RX   PubMed=11280994;
RA   Zhong B.-X.;
RT   "Protein database for several tissues derived from five instar of
RT   silkworm.";
RL   Yi Chuan Xue Bao 28:217-224(2001).
CC   -!- FUNCTION: Tropomyosin, in association with the troponin complex, plays
CC       a central role in the calcium dependent regulation of muscle
CC       contraction. {ECO:0000305}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P15846}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1 {ECO:0000269|Ref.1};
CC         IsoId=Q1HPQ0-1; Sequence=Displayed;
CC       Name=2 {ECO:0000269|Ref.1};
CC         IsoId=Q1HPQ0-2; Sequence=VSP_052286, VSP_052287, VSP_052290;
CC       Name=3 {ECO:0000269|Ref.1}; Synonyms=6 {ECO:0000269|Ref.1};
CC         IsoId=Q1HPQ0-3; Sequence=VSP_052288, VSP_052289;
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   -!- SIMILARITY: Belongs to the tropomyosin family. {ECO:0000255}.
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DR   EMBL; DQ443311; ABF51400.1; -; mRNA.
DR   EMBL; DQ443352; ABF51441.1; -; mRNA.
DR   EMBL; DQ443353; ABF51442.1; -; mRNA.
DR   RefSeq; NP_001040465.1; NM_001047000.1. [Q1HPQ0-2]
DR   RefSeq; NP_001103782.1; NM_001110312.1. [Q1HPQ0-1]
DR   AlphaFoldDB; Q1HPQ0; -.
DR   SMR; Q1HPQ0; -.
DR   STRING; 7091.BGIBMGA001582-TA; -.
DR   Allergome; 4112; Bomb m 7.
DR   Allergome; 4113; Bomb m 7.0101.
DR   Allergome; 4143; Bomb m 7.0103.
DR   GeneID; 100101174; -.
DR   KEGG; bmor:100101174; -.
DR   eggNOG; KOG1003; Eukaryota.
DR   Proteomes; UP000005204; Unassembled WGS sequence.
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   Alternative splicing; Coiled coil; Direct protein sequencing;
KW   Reference proteome; Repeat.
FT   CHAIN           1..285
FT                   /note="Tropomyosin-2"
FT                   /id="PRO_0000274258"
FT   REGION          103..133
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1..277
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        118..133
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         126..163
FT                   /note="ARKVLENRSLADEERMDALENQLKEARFLAEEADKKYD -> IRKALENRTN
FT                   MEDDRVAILEAQLSQAKLIAEESDKKYE (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_052286"
FT   VAR_SEQ         215..231
FT                   /note="NQREEEYKNQIKTLTTR -> TKREETYETHLKLLDAQ (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_052287"
FT   VAR_SEQ         221..227
FT                   /note="YKNQIKT -> SKIQIKN (in isoform 3)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_052288"
FT   VAR_SEQ         244..285
FT                   /note="RSVQKLQKEVDRLEDELVAEKEKYKDIGDDLDTAFVELILKE -> KTVKKL
FT                   QKEVDRLEDELGINKDRYKSLADEMDSTFAELAGY (in isoform 3)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_052289"
FT   VAR_SEQ         259..285
FT                   /note="ELVAEKEKYKDIGDDLDTAFVELILKE -> DLVAEREKSKLLQEEMEATLH
FT                   DIQNM (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_052290"
FT   CONFLICT        24
FT                   /note="M -> L (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        42
FT                   /note="E -> Q (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        53
FT                   /note="I -> V (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   285 AA;  32786 MW;  833EFD4BCFA75A60 CRC64;
     MDAIKKKMQA MKLEKDNALD RAAMCEQQAK DANLRAEKAE EEARQLQKKI QTIENELDQT
     QESLMQVNGK LEEKEKALQN AESEVAALNR RIQLLEEDLE RSEERLATAT AKLSEASQAA
     DESERARKVL ENRSLADEER MDALENQLKE ARFLAEEADK KYDEVARKLA MVEADLERAE
     ERAESGESKI VELEEELRVV GNNLKSLEVS EEKANQREEE YKNQIKTLTT RLKEAEARAE
     FAERSVQKLQ KEVDRLEDEL VAEKEKYKDI GDDLDTAFVE LILKE
 
 
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