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