SSM4_SCHPO
ID SSM4_SCHPO Reviewed; 670 AA.
AC O42667;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 138.
DE RecName: Full=Microtubule-associated protein ssm4;
GN Name=ssm4; ORFNames=SPAC27D7.13c, SPAC637.01c;
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].
RX PubMed=9167972; DOI=10.1046/j.1365-2443.1997.1100307.x;
RA Yamashita A., Watanabe Y., Yamamoto M.;
RT "Microtubule-associated coiled-coil protein Ssm4 is involved in the meiotic
RT development in fission yeast.";
RL Genes Cells 2:155-166(1997).
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).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460 AND THR-606, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Binds to nuclear microtubules with the effect of either
CC modifying their structure or function. This then promotes meiotic
CC nuclear division.
CC -!- INTERACTION:
CC O42667; O13290: dhc1; NbExp=2; IntAct=EBI-1556587, EBI-1112490;
CC O42667; Q9UTS6: dlc1; NbExp=3; IntAct=EBI-1556587, EBI-1542278;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle. Note=Mitotic
CC spindle.
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DR EMBL; AB000269; BAA31857.1; -; Genomic_DNA.
DR EMBL; CU329670; CAA15832.1; -; Genomic_DNA.
DR PIR; T38446; T38446.
DR PIR; T38993; T38993.
DR RefSeq; NP_594619.1; NM_001020047.1.
DR AlphaFoldDB; O42667; -.
DR SMR; O42667; -.
DR BioGRID; 278546; 80.
DR IntAct; O42667; 4.
DR STRING; 4896.SPAC27D7.13c.1; -.
DR iPTMnet; O42667; -.
DR PaxDb; O42667; -.
DR EnsemblFungi; SPAC27D7.13c.1; SPAC27D7.13c.1:pep; SPAC27D7.13c.
DR GeneID; 2542069; -.
DR KEGG; spo:SPAC27D7.13c; -.
DR PomBase; SPAC27D7.13c; ssm4.
DR VEuPathDB; FungiDB:SPAC27D7.13c; -.
DR eggNOG; KOG4568; Eukaryota.
DR HOGENOM; CLU_410015_0_0_1; -.
DR InParanoid; O42667; -.
DR OMA; DELMCEN; -.
DR PhylomeDB; O42667; -.
DR PRO; PR:O42667; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0051285; C:cell cortex of cell tip; IDA:PomBase.
DR GO; GO:0051286; C:cell tip; IBA:GO_Central.
DR GO; GO:1903754; C:cortical microtubule plus-end; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005881; C:cytoplasmic microtubule; IDA:PomBase.
DR GO; GO:0005869; C:dynactin complex; TAS:PomBase.
DR GO; GO:0035974; C:meiotic spindle pole body; IDA:PomBase.
DR GO; GO:0005875; C:microtubule associated complex; IBA:GO_Central.
DR GO; GO:0015630; C:microtubule cytoskeleton; HDA:PomBase.
DR GO; GO:0035371; C:microtubule plus-end; IBA:GO_Central.
DR GO; GO:0072686; C:mitotic spindle; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0110092; C:nucleus leading edge; IDA:PomBase.
DR GO; GO:0005819; C:spindle; IBA:GO_Central.
DR GO; GO:0005816; C:spindle pole body; IBA:GO_Central.
DR GO; GO:0051010; F:microtubule plus-end binding; IBA:GO_Central.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR GO; GO:0030989; P:dynein-driven meiotic oscillatory nuclear movement; IMP:PomBase.
DR GO; GO:0007127; P:meiosis I; IGI:PomBase.
DR GO; GO:0000743; P:nuclear migration involved in conjugation with cellular fusion; IMP:PomBase.
DR Gene3D; 2.30.30.190; -; 1.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR Pfam; PF01302; CAP_GLY; 1.
DR SMART; SM01052; CAP_GLY; 1.
DR SUPFAM; SSF74924; SSF74924; 1.
DR PROSITE; PS00845; CAP_GLY_1; 1.
DR PROSITE; PS50245; CAP_GLY_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Meiosis; Microtubule; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..670
FT /note="Microtubule-associated protein ssm4"
FT /id="PRO_0000083532"
FT DOMAIN 23..65
FT /note="CAP-Gly"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
FT COILED 209..254
FT /evidence="ECO:0000255"
FT COILED 404..582
FT /evidence="ECO:0000255"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 606
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 670 AA; 77106 MW; 011B7D740211B57C CRC64;
MSYLSVGDEV LIRGELGIVR FAGSTDFESG IWLGVELLNG KGKNDGSVKG KRYFSCEKGK
GIFVRACSSN VMKRPSVVKS RKKGSENISN FMEKTKAIKQ KSRREPSKFE RSLARPLCIT
PIDSSTPTKT ATFYTSSTTE NLDELNFSTE ELSSFDTTLL NSDTSKLSGL DDSSFMEEEF
VWQVDNVLQE CEKKFTPHSK GSYLKENLKS ELRKGRLDEL MCENTALKEK IDKLNKELEK
VEPQLTFLRS KNSIEKPRNF RREKFLKKFL AMQKEIKYLR KRKLQIRKIP NYKYSDRSLN
SKTPKSQDNW TTQVTPSSLL GVSEVSKVLQ LKQVQVDITE LVKIPKNPFS EKLTISNVNR
YLNIVPGSLD LQFSLTNENF VHWNSTVYQE LLNLKSNNSS VDGVKTRRQL LEENALLSHK
VLKLTEEIQD LETLNQLNTE IEARQSEKLN EVQEETQRLS QLLISSQPAL TEVKHLKLCL
SDSQEELLQL NAKLEKANIV IDELNSAKLK LSKQVEEESS MKDDLTEMNQ RLKEQIESYE
NEVNSEITSR TLKEFETLKT QYEKNLCNLR EQLKTARMKL ADKYPQGDNT SENIDWLKHS
LRDSNTENSI PSPLTFACKE IRKLVADIKP VSVEKQLALN WKKDIERPSF HHNQQLFNYC
QLTDILSKKC
