TPM3_RAT
ID TPM3_RAT Reviewed; 248 AA.
AC Q63610; Q63599; Q63600; Q63601;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Tropomyosin alpha-3 chain;
DE AltName: Full=Gamma-tropomyosin;
DE AltName: Full=Tropomyosin-3;
DE AltName: Full=Tropomyosin-5;
GN Name=Tpm3; Synonyms=Tpm-5, Tpm5;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=Sprague-Dawley; TISSUE=Cochlea;
RX PubMed=8206382; DOI=10.1016/0378-1119(94)90105-8;
RA Beisel K.W., Kennedy J.E.;
RT "Identification of novel alternatively spliced isoforms of the tropomyosin-
RT encoding gene, TMnm, in the rat cochlea.";
RL Gene 143:251-256(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=Sprague-Dawley;
RX PubMed=9222299; DOI=10.1007/bf01438309;
RA Miyado K., Sato M., Taniguchi S.;
RT "Transformation-related expression of a low-molecular-mass tropomyosin
RT isoform TM5/TM30nm in transformed rat fibroblastic cell lines.";
RL J. Cancer Res. Clin. Oncol. 123:331-336(1997).
RN [3]
RP PROTEIN SEQUENCE OF 2-27 AND 41-65, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Fibroblast;
RA Bienvenut W.V., von Kriegsheim A., Kolch W.;
RL Submitted (JUN-2009) to UniProtKB.
RN [4]
RP PROTEIN SEQUENCE OF 13-27; 55-65; 105-113; 132-142; 182-190 AND 216-225,
RP PARTIAL PROTEIN SEQUENCE (ISOFORMS 2 AND 3), AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Hippocampus;
RA Lubec G., Chen W.-Q., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
CC -!- FUNCTION: Binds to actin filaments in muscle and non-muscle cells.
CC Plays a central role, in association with the troponin complex, in the
CC calcium dependent regulation of vertebrate striated muscle contraction.
CC Smooth muscle contraction is regulated by interaction with caldesmon.
CC In non-muscle cells is implicated in stabilizing cytoskeleton actin
CC filaments. {ECO:0000250|UniProtKB:P09493}.
CC -!- SUBUNIT: Homodimer. Heterodimer of an alpha (TPM1, TPM3 or TPM4) and a
CC beta (TPM2) chain. Interacts with TMOD1. {ECO:0000250|UniProtKB:P04692,
CC ECO:0000250|UniProtKB:P06753}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Tpm3_v1;
CC IsoId=Q63610-1; Sequence=Displayed;
CC Name=2; Synonyms=Tpm3_v3;
CC IsoId=Q63610-2; Sequence=VSP_025995, VSP_025997;
CC Name=3; Synonyms=Tpm3_v2;
CC IsoId=Q63610-3; Sequence=VSP_025995, VSP_025996;
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; L24775; AAA21721.1; -; mRNA.
DR EMBL; L24776; AAA42263.1; -; mRNA.
DR EMBL; L24777; AAA42264.1; -; mRNA.
DR EMBL; X72859; CAA51382.1; -; mRNA.
DR PIR; I53784; I53784.
DR PIR; I67849; I67849.
DR PIR; I67850; I67850.
DR PIR; S34124; S34124.
DR RefSeq; NP_001288215.1; NM_001301286.1. [Q63610-2]
DR RefSeq; NP_476556.2; NM_057208.2. [Q63610-3]
DR RefSeq; NP_775134.1; NM_173111.1. [Q63610-1]
DR AlphaFoldDB; Q63610; -.
DR SMR; Q63610; -.
DR BioGRID; 250770; 8.
DR CORUM; Q63610; -.
DR IntAct; Q63610; 5.
DR MINT; Q63610; -.
DR STRING; 10116.ENSRNOP00000023567; -.
DR iPTMnet; Q63610; -.
DR PhosphoSitePlus; Q63610; -.
DR SwissPalm; Q63610; -.
DR jPOST; Q63610; -.
DR PaxDb; Q63610; -.
DR PRIDE; Q63610; -.
DR GeneID; 117557; -.
DR KEGG; rno:117557; -.
DR UCSC; RGD:621546; rat. [Q63610-1]
DR CTD; 7170; -.
DR RGD; 621546; Tpm3.
DR VEuPathDB; HostDB:ENSRNOG00000017441; -.
DR eggNOG; KOG1003; Eukaryota.
DR HOGENOM; CLU_055027_0_0_1; -.
DR InParanoid; Q63610; -.
DR OrthoDB; 1576041at2759; -.
DR PhylomeDB; Q63610; -.
DR PRO; PR:Q63610; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000017441; Expressed in spleen and 19 other tissues.
DR ExpressionAtlas; Q63610; baseline and differential.
DR Genevisible; Q63610; RN.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0005903; C:brush border; IDA:UniProtKB.
DR GO; GO:0032154; C:cleavage furrow; ISO:RGD.
DR GO; GO:0030863; C:cortical cytoskeleton; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0030426; C:growth cone; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; ISO:RGD.
DR GO; GO:0002102; C:podosome; ISO:RGD.
DR GO; GO:0001725; C:stress fiber; ISO:RGD.
DR GO; GO:0051015; F:actin filament binding; ISO:RGD.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR Gene3D; 1.20.5.370; -; 1.
DR InterPro; IPR000533; Tropomyosin.
DR InterPro; IPR014751; XRCC4-like_C.
DR Pfam; PF00261; Tropomyosin; 1.
DR PRINTS; PR00194; TROPOMYOSIN.
DR PROSITE; PS00326; TROPOMYOSIN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Alternative splicing; Coiled coil; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Muscle protein; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.3"
FT CHAIN 2..248
FT /note="Tropomyosin alpha-3 chain"
FT /id="PRO_0000289259"
FT REGION 21..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 4..240
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.3"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06753"
FT MOD_RES 72
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07951"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P58775"
FT MOD_RES 216
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07951"
FT VAR_SEQ 153..175
FT /note="RCREMDEQIRLMDQNLKCLSAAE -> KCSELEEELKNVTNNLKSLEAQA
FT (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:8206382"
FT /id="VSP_025995"
FT VAR_SEQ 222..248
FT /note="DKLKCTKEEHLCTQRMLDQTLLDLNEM -> ERLYSQLERNRLLSNELKLTL
FT HGLCD (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8206382"
FT /id="VSP_025996"
FT VAR_SEQ 223..248
FT /note="KLKCTKEEHLCTQRMLDQTLLDLNEM -> ELYAQKLKYKAISDELDHALND
FT MTSI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8206382"
FT /id="VSP_025997"
FT CONFLICT 83
FT /note="A -> V (in Ref. 2; CAA51382)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 248 AA; 29007 MW; E3E49312A710A068 CRC64;
MAGSTTIEAV KRKIQVLQQQ ADDAEERAER LQREVEGERR AREQAEAEVA SLNRRIQLVE
EELDRAQERL ATALQKLEEA EKAADESERG MKVIENRALK DEEKMELQEI QLKEAKHIAE
EADRKYEEVA RKLVIIEGDL ERTEERAELA ESRCREMDEQ IRLMDQNLKC LSAAEEKYSQ
KEDKYEEEIK ILTDKLKEAE TRAEFAERSV AKLEKTIDDL EDKLKCTKEE HLCTQRMLDQ
TLLDLNEM
