TPM_SCHPO
ID TPM_SCHPO Reviewed; 161 AA.
AC Q02088;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Tropomyosin;
GN Name=cdc8; ORFNames=SPAC27F1.02c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=1436080; DOI=10.1038/360084a0;
RA Balasubramanian M.K., Helfman D.M., Hemmingsen S.M.;
RT "A new tropomyosin essential for cytokinesis in the fission yeast S.
RT pombe.";
RL Nature 360:84-87(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: Forms part of the F-actin contractile ring during
CC cytokinesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
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.
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DR EMBL; L04126; AAA35349.1; -; Genomic_DNA.
DR EMBL; CU329670; CAA93291.2; -; Genomic_DNA.
DR PIR; S27127; S27127.
DR RefSeq; NP_594530.1; NM_001019959.2.
DR AlphaFoldDB; Q02088; -.
DR SMR; Q02088; -.
DR BioGRID; 278427; 22.
DR STRING; 4896.SPAC27F1.02c.1; -.
DR iPTMnet; Q02088; -.
DR MaxQB; Q02088; -.
DR PaxDb; Q02088; -.
DR PRIDE; Q02088; -.
DR EnsemblFungi; SPAC27F1.02c.1; SPAC27F1.02c.1:pep; SPAC27F1.02c.
DR GeneID; 2541940; -.
DR KEGG; spo:SPAC27F1.02c; -.
DR PomBase; SPAC27F1.02c; cdc8.
DR VEuPathDB; FungiDB:SPAC27F1.02c; -.
DR eggNOG; KOG1003; Eukaryota.
DR HOGENOM; CLU_104738_0_1_1; -.
DR InParanoid; Q02088; -.
DR OMA; AKYEEMA; -.
DR PhylomeDB; Q02088; -.
DR Reactome; R-SPO-9013424; RHOV GTPase cycle.
DR PRO; PR:Q02088; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0030479; C:actin cortical patch; IDA:PomBase.
DR GO; GO:0005884; C:actin filament; IDA:PomBase.
DR GO; GO:1990819; C:actin fusion focus; IDA:PomBase.
DR GO; GO:0005826; C:actomyosin contractile ring; IBA:GO_Central.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0070648; C:formin-nucleated actin cable; IDA:PomBase.
DR GO; GO:0043332; C:mating projection tip; IDA:PomBase.
DR GO; GO:0110085; C:mitotic actomyosin contractile ring; IDA:PomBase.
DR GO; GO:0051015; F:actin filament binding; IDA:PomBase.
DR GO; GO:0003786; F:actin lateral binding; IDA:PomBase.
DR GO; GO:0044396; P:actin cortical patch organization; IMP:PomBase.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:1903475; P:mitotic actomyosin contractile ring assembly; IMP:PomBase.
DR GO; GO:1902404; P:mitotic actomyosin contractile ring contraction; IMP:PomBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:PomBase.
DR GO; GO:1904530; P:negative regulation of actin filament binding; IDA:PomBase.
DR GO; GO:0030835; P:negative regulation of actin filament depolymerization; IDA:PomBase.
DR GO; GO:0030837; P:negative regulation of actin filament polymerization; IDA:PomBase.
DR GO; GO:1903919; P:negative regulation of actin filament severing; IDA:PomBase.
DR GO; GO:0034316; P:negative regulation of Arp2/3 complex-mediated actin nucleation; IDA:PomBase.
DR GO; GO:0032220; P:plasma membrane fusion involved in cytogamy; IMP:PomBase.
DR GO; GO:1904618; P:positive regulation of actin binding; IDA:PomBase.
DR GO; GO:0110056; P:positive regulation of actin filament annealing; IDA:PomBase.
DR GO; GO:1903116; P:positive regulation of actin filament-based movement; IDA:PomBase.
DR InterPro; IPR000533; Tropomyosin.
DR Pfam; PF12718; Tropomyosin_1; 1.
DR PRINTS; PR00194; TROPOMYOSIN.
PE 3: Inferred from homology;
KW Coiled coil; Cytoplasm; Cytoskeleton; Reference proteome; Repeat.
FT CHAIN 1..161
FT /note="Tropomyosin"
FT /id="PRO_0000205694"
FT REGION 40..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1..161
FT /evidence="ECO:0000250"
SQ SEQUENCE 161 AA; 18964 MW; 44CB359FA6A4096E CRC64;
MDKLREKINA ARAETDEAVA RAEAAEAKLK EVELQLSLKE QEYESLSRKS EAAESQLEEL
EEETKQLRLK ADNEDIQKTE AEQLSRKVEL LEEELETNDK LLRETTEKMR QTDVKAEHFE
RRVQSLERER DDMEQKLEEM TDKYTKVKAE LDEVHQALED L
