ID   SID4_SCHPO              Reviewed;         660 AA.
AC   O60187;
DT   06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Septation initiation protein sid4;
GN   Name=sid4; ORFNames=SPBC244.01c;
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], FUNCTION, SUBUNIT, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=10805785; DOI=10.1073/pnas.97.10.5249;
RA   Chang L., Gould K.L.;
RT   "Sid4p is required to localize components of the septation initiation
RT   pathway to the spindle pole body in fission yeast.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:5249-5254(2000).
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   INTERACTION WITH CDC11, AND SUBCELLULAR LOCATION.
RX   PubMed=11676915; DOI=10.1016/s0960-9822(01)00478-x;
RA   Krapp A., Schmidt S., Cano E., Simanis V.;
RT   "S. pombe cdc11p, together with sid4p, provides an anchor for septation
RT   initiation network proteins on the spindle pole body.";
RL   Curr. Biol. 11:1559-1568(2001).
RN   [4]
RP   FUNCTION, INTERACTION WITH PLO1; CDC11 AND DMA1, AND SUBCELLULAR LOCATION.
RX   PubMed=15062098; DOI=10.1016/j.cub.2004.03.036;
RA   Morrell J.L., Tomlin G.C., Rajagopalan S., Venkatram S., Feoktistova A.S.,
RA   Tasto J.J., Mehta S., Jennings J.L., Link A., Balasubramanian M.K.,
RA   Gould K.L.;
RT   "Sid4p-Cdc11p assembles the septation initiation network and its regulators
RT   at the S. pombe SPB.";
RL   Curr. Biol. 14:579-584(2004).
RN   [5]
RP   INTERACTION WITH SAD1, AND SUBCELLULAR LOCATION.
RX   PubMed=14655046; DOI=10.1007/s00438-003-0938-8;
RA   Miki F., Kurabayashi A., Tange Y., Okazaki K., Shimanuki M., Niwa O.;
RT   "Two-hybrid search for proteins that interact with Sad1 and Kms1, two
RT   membrane-bound components of the spindle pole body in fission yeast.";
RL   Mol. Genet. Genomics 270:449-461(2004).
RN   [6]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- FUNCTION: Required for activation of the spg1 GTPase signaling cascade
CC       which leads to the initiation of septation and the subsequent
CC       termination of mitosis. May act as a scaffold at the spindle pole body
CC       to which other components of the spg1 signaling cascade attach.
CC       {ECO:0000269|PubMed:10805785, ECO:0000269|PubMed:15062098}.
CC   -!- SUBUNIT: Homodimer. Interacts with cdc11, sad1, plo1 and dma1.
CC       {ECO:0000269|PubMed:10805785, ECO:0000269|PubMed:11676915,
CC       ECO:0000269|PubMed:14655046, ECO:0000269|PubMed:15062098}.
CC   -!- INTERACTION:
CC       O60187; Q10322: dma1; NbExp=2; IntAct=EBI-1125100, EBI-1125055;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, spindle pole body {ECO:0000269|PubMed:10805785,
CC       ECO:0000269|PubMed:11676915, ECO:0000269|PubMed:14655046,
CC       ECO:0000269|PubMed:15062098, ECO:0000269|PubMed:16823372}.
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DR   EMBL; AF153475; AAF69105.1; -; Genomic_DNA.
DR   EMBL; CU329671; CAA19316.1; -; Genomic_DNA.
DR   PIR; T39964; T39964.
DR   RefSeq; NP_596814.1; NM_001023834.2.
DR   AlphaFoldDB; O60187; -.
DR   BioGRID; 277175; 28.
DR   IntAct; O60187; 4.
DR   MINT; O60187; -.
DR   STRING; 4896.SPBC244.01c.1; -.
DR   iPTMnet; O60187; -.
DR   SwissPalm; O60187; -.
DR   MaxQB; O60187; -.
DR   PaxDb; O60187; -.
DR   PRIDE; O60187; -.
DR   EnsemblFungi; SPBC244.01c.1; SPBC244.01c.1:pep; SPBC244.01c.
DR   GeneID; 2540650; -.
DR   KEGG; spo:SPBC244.01c; -.
DR   PomBase; SPBC244.01c; sid4.
DR   VEuPathDB; FungiDB:SPBC244.01c; -.
DR   eggNOG; ENOG502SVAG; Eukaryota.
DR   HOGENOM; CLU_415702_0_0_1; -.
DR   OMA; LVSKQCL; -.
DR   PhylomeDB; O60187; -.
DR   PRO; PR:O60187; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0090619; C:meiotic spindle pole; EXP:PomBase.
DR   GO; GO:0044732; C:mitotic spindle pole body; IDA:PomBase.
DR   GO; GO:0061499; C:outer plaque of mitotic spindle pole body; IDA:PomBase.
DR   GO; GO:0035591; F:signaling adaptor activity; EXP:PomBase.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0031030; P:negative regulation of septation initiation signaling; IMP:PomBase.
DR   InterPro; IPR021750; Sid4-like.
DR   Pfam; PF11778; SID; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Mitosis;
KW   Reference proteome.
FT   CHAIN           1..660
FT                   /note="Septation initiation protein sid4"
FT                   /id="PRO_0000097755"
FT   REGION          79..243
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          368..396
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          459..503
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..97
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        107..141
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        151..211
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        226..243
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        382..396
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   660 AA;  74473 MW;  B7791030F3091D94 CRC64;
     MDEAFGDSLS TDYRWLGHSH FDSHPSAGDS IYFDSLDEDA DPSRTARIDR IAELLDGLND
     EQISELVNGV NSTTIKENTK KEISNPNDST RLPLEQIPGS NNLFLDPRHQ LGDNSQNAQR
     HHEPSFNSEK ASYTSTPYKN VAPKVIDSPS ARHMHSNSPS FPPSQSHTSS YDQSPKGQLR
     DNISVPNQQD GLDPEVFNQQ SKETKKSLQV PPSRNVPPPV TRPNQYNPEP NFSLSSGYPQ
     QHFSQPELQN RNVHLETVPE SYPVPPSGYP LTSSTCVSSI SQPIQSTDCQ KAQENLSNNK
     QMSSNDQDID PFKQAITDLP PSFVNIVLEM NATIQSLSNQ CQQRDKQIEN ITKQLLMNQQ
     DYCPTTMSTT VSTPLCPPKR FPKSTKDFKE QKPDTKQVRS ATISNDFNLK GNGRYNEKSQ
     IAVPSEIRVQ LSTLDAILLQ FEHLRKELTQ ARKEIQILRH TSQNGDQESN ESSKNAITTK
     TTDKGNNKEN TMLNDGSTAP AKNDIRNVIN TNNLDAKLSD ESELMIEKNK SYSTPASSTI
     PTFHTSQPLT SLNMPDSRFN LAKEKQLYYR LGLQHIDQQC SVETANMLKT VLVQLNIPFA
     IFPSTIGQVR RQLQQGRRLY QWARNIHYLI YEENMRDGLV SKQCLADMLK KIRELKKRSL