TPM2_YEAST
ID TPM2_YEAST Reviewed; 161 AA.
AC P40414; D6VVE8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Tropomyosin-2;
GN Name=TPM2; OrderedLocusNames=YIL138C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP FUNCTION, AND SUBUNIT.
RX PubMed=7844152; DOI=10.1083/jcb.128.3.383;
RA Drees B., Brown C., Barrell B.G., Bretscher A.;
RT "Tropomyosin is essential in yeast, yet the TPM1 and TPM2 products perform
RT distinct functions.";
RL J. Cell Biol. 128:383-392(1995).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55; SER-116 AND SER-157, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55 AND SER-157, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Involved in cell morphogenesis. Binds to F-actin and
CC stabilizes the actin filaments. {ECO:0000269|PubMed:7844152}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:7844152}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
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 -!- MISCELLANEOUS: Present with 11100 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z38059; CAA86140.1; -; Genomic_DNA.
DR EMBL; AY558235; AAS56561.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08414.1; -; Genomic_DNA.
DR PIR; S48396; S48396.
DR RefSeq; NP_012128.3; NM_001179486.3.
DR AlphaFoldDB; P40414; -.
DR SMR; P40414; -.
DR BioGRID; 34853; 71.
DR DIP; DIP-2201N; -.
DR IntAct; P40414; 3.
DR MINT; P40414; -.
DR STRING; 4932.YIL138C; -.
DR iPTMnet; P40414; -.
DR MaxQB; P40414; -.
DR PaxDb; P40414; -.
DR PRIDE; P40414; -.
DR EnsemblFungi; YIL138C_mRNA; YIL138C; YIL138C.
DR GeneID; 854668; -.
DR KEGG; sce:YIL138C; -.
DR SGD; S000001400; TPM2.
DR VEuPathDB; FungiDB:YIL138C; -.
DR eggNOG; KOG1003; Eukaryota.
DR GeneTree; ENSGT00940000176442; -.
DR HOGENOM; CLU_104738_1_1_1; -.
DR InParanoid; P40414; -.
DR OMA; RETTANF; -.
DR BioCyc; YEAST:G3O-31389-MON; -.
DR PRO; PR:P40414; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40414; protein.
DR GO; GO:0005884; C:actin filament; IDA:UniProtKB.
DR GO; GO:0032432; C:actin filament bundle; IDA:SGD.
DR GO; GO:0005826; C:actomyosin contractile ring; IBA:GO_Central.
DR GO; GO:0000142; C:cellular bud neck contractile ring; IDA:SGD.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0003786; F:actin lateral binding; TAS:SGD.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0051017; P:actin filament bundle assembly; IGI:SGD.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0008154; P:actin polymerization or depolymerization; TAS:SGD.
DR GO; GO:0007118; P:budding cell apical bud growth; TAS:SGD.
DR GO; GO:0007119; P:budding cell isotropic bud growth; TAS:SGD.
DR GO; GO:0030010; P:establishment of cell polarity; TAS:SGD.
DR GO; GO:0006887; P:exocytosis; TAS:SGD.
DR GO; GO:0008298; P:intracellular mRNA localization; TAS:SGD.
DR GO; GO:0000001; P:mitochondrion inheritance; TAS:SGD.
DR GO; GO:1903475; P:mitotic actomyosin contractile ring assembly; IGI:SGD.
DR GO; GO:0000281; P:mitotic cytokinesis; IBA:GO_Central.
DR GO; GO:0000011; P:vacuole inheritance; TAS:SGD.
DR GO; GO:0016192; P:vesicle-mediated transport; TAS:SGD.
DR InterPro; IPR000533; Tropomyosin.
DR Pfam; PF12718; Tropomyosin_1; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..161
FT /note="Tropomyosin-2"
FT /id="PRO_0000205693"
FT REGION 32..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1..161
FT /evidence="ECO:0000250"
FT COMPBIAS 32..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 161 AA; 19093 MW; 533FA067B0F78B59 CRC64;
MEKIKEKLNS LKLESESWQE KYEELREQLK ELEQSNTEKE NEIKSLSAKN EQLDSEVEKL
ESQLSDTKQL AEDSNNLRSN NENYTKKNQD LEQQLEDSEA KLKEAMDKLK EADLNSEQMG
RRIVALEEER DEWEKKCEEF QSKYEEAQKE LDEIANSLEN L
