TPM3_MOUSE
ID TPM3_MOUSE Reviewed; 285 AA.
AC P21107; Q09021; Q60606; Q80SW6; Q9EPW3;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 3.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Tropomyosin alpha-3 chain;
DE AltName: Full=Gamma-tropomyosin;
DE AltName: Full=Tropomyosin-3;
GN Name=Tpm3; Synonyms=Tpm-5, Tpm5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=BALB/cJ;
RX PubMed=2400784; DOI=10.1016/0167-4781(90)90129-p;
RA Takenaga K., Nakamura Y., Kageyama H., Sakiyama S.;
RT "Nucleotide sequence of cDNA for nonmuscle tropomyosin 5 of mouse
RT fibroblast.";
RL Biochim. Biophys. Acta 1087:101-103(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Diaphragm;
RA Hailstones D.L.;
RT "Regulation of non-muscle isoforms of contractile proteins dring
RT myogenesis.";
RL Thesis (1993), University of Sydney, Australia.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-285 (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Skeletal muscle;
RX PubMed=10889038; DOI=10.1021/bi000047x;
RA Pieples K., Wieczorek D.F.;
RT "Tropomyosin 3 increases striated muscle isoform diversity.";
RL Biochemistry 39:8291-8297(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=NOD; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 244-285 (ISOFORM 1).
RC STRAIN=ICR;
RX PubMed=8491774; DOI=10.1083/jcb.121.4.811;
RA Schevzov G., Lloyd C., Hailstones D.L., Gunning P.;
RT "Differential regulation of tropomyosin isoform organization and gene
RT expression in response to altered actin gene expression.";
RL J. Cell Biol. 121:811-821(1993).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272 AND SER-284, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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: [Isoform 2]: Cytoplasm, cytoskeleton.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=Skeletal muscle;
CC IsoId=P21107-1; Sequence=Displayed;
CC Name=2; Synonyms=Cytoskeletal;
CC IsoId=P21107-2; Sequence=VSP_006608, VSP_006609, VSP_006610;
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}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator.
CC {ECO:0000305}.
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DR EMBL; X53753; CAA37782.1; -; mRNA.
DR EMBL; U04541; AAA03725.1; -; mRNA.
DR EMBL; AF317223; AAG38596.1; -; mRNA.
DR EMBL; AK088111; BAC40150.1; -; mRNA.
DR EMBL; AK088902; BAC40643.1; -; mRNA.
DR EMBL; X72633; CAA51209.1; -; mRNA.
DR CCDS; CCDS57223.1; -. [P21107-2]
DR PIR; I48852; I48852.
DR PIR; S11390; S11390.
DR RefSeq; NP_001240667.1; NM_001253738.1. [P21107-2]
DR RefSeq; NP_001280677.2; NM_001293748.1. [P21107-1]
DR AlphaFoldDB; P21107; -.
DR SMR; P21107; -.
DR BioGRID; 208522; 25.
DR DIP; DIP-32061N; -.
DR IntAct; P21107; 8.
DR MINT; P21107; -.
DR STRING; 10090.ENSMUSP00000113978; -.
DR iPTMnet; P21107; -.
DR PhosphoSitePlus; P21107; -.
DR SwissPalm; P21107; -.
DR COMPLUYEAST-2DPAGE; P21107; -.
DR REPRODUCTION-2DPAGE; P21107; -.
DR SWISS-2DPAGE; P21107; -.
DR EPD; P21107; -.
DR jPOST; P21107; -.
DR MaxQB; P21107; -.
DR PeptideAtlas; P21107; -.
DR PRIDE; P21107; -.
DR ProteomicsDB; 259062; -. [P21107-1]
DR ProteomicsDB; 259063; -. [P21107-2]
DR Antibodypedia; 1682; 240 antibodies from 33 providers.
DR DNASU; 59069; -.
DR Ensembl; ENSMUST00000029549; ENSMUSP00000029549; ENSMUSG00000027940. [P21107-2]
DR GeneID; 59069; -.
DR KEGG; mmu:59069; -.
DR UCSC; uc008qbf.3; mouse. [P21107-1]
DR CTD; 7170; -.
DR MGI; MGI:1890149; Tpm3.
DR VEuPathDB; HostDB:ENSMUSG00000027940; -.
DR GeneTree; ENSGT01030000234542; -.
DR HOGENOM; CLU_055027_3_0_1; -.
DR InParanoid; P21107; -.
DR Reactome; R-MMU-390522; Striated Muscle Contraction.
DR Reactome; R-MMU-445355; Smooth Muscle Contraction.
DR Reactome; R-MMU-9013424; RHOV GTPase cycle.
DR BioGRID-ORCS; 59069; 4 hits in 70 CRISPR screens.
DR ChiTaRS; Tpm3; mouse.
DR PRO; PR:P21107; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P21107; protein.
DR Bgee; ENSMUSG00000027940; Expressed in soleus muscle and 172 other tissues.
DR ExpressionAtlas; P21107; baseline and differential.
DR Genevisible; P21107; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0032154; C:cleavage furrow; IDA:MGI.
DR GO; GO:0030863; C:cortical cytoskeleton; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030426; C:growth cone; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0002102; C:podosome; IDA:MGI.
DR GO; GO:0001725; C:stress fiber; ISO:MGI.
DR GO; GO:0051015; F:actin filament binding; IDA:MGI.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
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 Acetylation; Actin-binding; Alternative splicing; Coiled coil; Cytoplasm;
KW Cytoskeleton; Muscle protein; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P58776"
FT CHAIN 2..285
FT /note="Tropomyosin alpha-3 chain"
FT /id="PRO_0000205633"
FT COILED 1..285
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P58776"
FT MOD_RES 54
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07951"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P58774"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06753"
FT MOD_RES 109
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07951"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07951"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P58775"
FT MOD_RES 253
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07951"
FT MOD_RES 262
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P58775"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 283
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07951"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..81
FT /note="MMEAIKKKMQMLKLDKENVLDRAEQAEAEQKQAEERSKQLEDELATMQKKLK
FT GTEDELDKYSEALKDAQEKLELAEKKAAD -> MAGTTTIEAVKRKIQVLQQQADDAEE
FT RAERLQREVEGERRAREQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:2400784"
FT /id="VSP_006608"
FT VAR_SEQ 190..212
FT /note="KCSELEEELKNVTNNLKSLEAQA -> RCREMDEQIRLMDQNLKCLSAAE
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:2400784"
FT /id="VSP_006609"
FT VAR_SEQ 260..285
FT /note="ELYAQKLKYKAISDELDHALNDMTSI -> KLKCTKEEHLCTQRMLDQTLLD
FT LNEM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:2400784"
FT /id="VSP_006610"
FT CONFLICT 19
FT /note="V -> F (in Ref. 2; AAA03725)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="Q -> R (in Ref. 2; AAA03725)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="E -> G (in Ref. 2; AAA03725)"
FT /evidence="ECO:0000305"
FT INIT_MET P21107-2:1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT MOD_RES P21107-2:2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000305"
FT MOD_RES P21107-2:228
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000305"
SQ SEQUENCE 285 AA; 32994 MW; F4407C132303002C CRC64;
MMEAIKKKMQ MLKLDKENVL DRAEQAEAEQ KQAEERSKQL EDELATMQKK LKGTEDELDK
YSEALKDAQE KLELAEKKAA DAEAEVASLN RRIQLVEEEL DRAQERLATA LQKLEEAEKA
ADESERGMKV IENRALKDEE KMELQEIQLK EAKHIAEEAD RKYEEVARKL VIIEGDLERT
EERAELAESK CSELEEELKN VTNNLKSLEA QAEKYSQKED KYEEEIKILT DKLKEAETRA
EFAERSVAKL EKTIDDLEDE LYAQKLKYKA ISDELDHALN DMTSI
