CDC11_SCHPO
ID CDC11_SCHPO Reviewed; 1045 AA.
AC O74473;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Septation initiation network scaffold protein cdc11;
DE Short=SIN scaffold protein cdc11;
DE AltName: Full=Cell division control protein 11;
GN Name=cdc11; ORFNames=SPCC1739.11c;
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 [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 [2]
RP FUNCTION, INTERACTION WITH SID4, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND
RP MUTAGENESIS OF ASN-767; ARG-947 AND THR-1041.
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 [3]
RP INTERACTION WITH BYR4, PHOSPHORYLATION BY CDC7, AND DEPHOSPHORYLATION BY
RP PAR1.
RX PubMed=12546793; DOI=10.1016/s0960-9822(02)01417-3;
RA Krapp A., Cano E., Simanis V.;
RT "Mitotic hyperphosphorylation of the fission yeast SIN scaffold protein
RT cdc11p is regulated by the protein kinase cdc7p.";
RL Curr. Biol. 13:168-172(2003).
RN [4]
RP FUNCTION, INTERACTION WITH SPG1; SID2, CDC13 AND CDC16, SUBCELLULAR
RP LOCATION, PHOSPHORYLATION BY CDCK1, AND MUTAGENESIS OF SER-98; SER-103;
RP SER-136; SER-199; SER-208; SER-360; SER-393 AND SER-558.
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 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).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360 AND SER-558, 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: Essential for the onset of septum formation. Involved in the
CC organization of astral microtubules during mitosis. Acts as a bridge
CC between sid4 and the other SIN proteins mediating their association
CC with the spindle pole body (SPB). The sid4-cdc11 complex organizes a
CC signaling hub on the SPB which coordinates cell and nuclear division.
CC {ECO:0000269|PubMed:11676915, ECO:0000269|PubMed:15062098}.
CC -!- SUBUNIT: Interacts with sid4. When hyperphosphorylated, interacts with
CC byr4. Also interacts with spg1, sid2, cdc13 and cdc16.
CC {ECO:0000269|PubMed:11676915, ECO:0000269|PubMed:12546793,
CC ECO:0000269|PubMed:15062098}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, microtubule
CC organizing center, spindle pole body. Note=Localizes at the spindle
CC pole body and the barrier septum.
CC -!- PTM: Phosphorylated by cdc7 and cdk1. Hyperphosphorylated during
CC anaphase. Dephosphorylated by par1. {ECO:0000269|PubMed:11676915,
CC ECO:0000269|PubMed:12546793, ECO:0000269|PubMed:15062098,
CC ECO:0000269|PubMed:18257517}.
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DR EMBL; CU329672; CAA20785.1; -; Genomic_DNA.
DR PIR; T41119; T41119.
DR RefSeq; NP_588419.1; NM_001023410.2.
DR AlphaFoldDB; O74473; -.
DR SMR; O74473; -.
DR BioGRID; 275721; 52.
DR IntAct; O74473; 3.
DR STRING; 4896.SPCC1739.11c.1; -.
DR iPTMnet; O74473; -.
DR MaxQB; O74473; -.
DR PaxDb; O74473; -.
DR PRIDE; O74473; -.
DR EnsemblFungi; SPCC1739.11c.1; SPCC1739.11c.1:pep; SPCC1739.11c.
DR GeneID; 2539149; -.
DR KEGG; spo:SPCC1739.11c; -.
DR PomBase; SPCC1739.11c; cdc11.
DR VEuPathDB; FungiDB:SPCC1739.11c; -.
DR eggNOG; KOG0531; Eukaryota.
DR HOGENOM; CLU_291889_0_0_1; -.
DR InParanoid; O74473; -.
DR OMA; PVARDIF; -.
DR PRO; PR:O74473; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0032991; C:protein-containing complex; IDA:PomBase.
DR GO; GO:0035591; F:signaling adaptor activity; EXP:PomBase.
DR GO; GO:0140278; P:mitotic division septum assembly; IMP:PomBase.
DR GO; GO:1902412; P:regulation of mitotic cytokinesis; IMP:PomBase.
DR GO; GO:0031028; P:septation initiation signaling; IMP:PomBase.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF13855; LRR_8; 1.
DR SMART; SM00369; LRR_TYP; 6.
DR PROSITE; PS51450; LRR; 12.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Leucine-rich repeat; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..1045
FT /note="Septation initiation network scaffold protein cdc11"
FT /id="PRO_0000339131"
FT REPEAT 604..625
FT /note="LRR 1"
FT REPEAT 627..646
FT /note="LRR 2"
FT REPEAT 647..668
FT /note="LRR 3"
FT REPEAT 669..690
FT /note="LRR 4"
FT REPEAT 691..712
FT /note="LRR 5"
FT REPEAT 713..734
FT /note="LRR 6"
FT REPEAT 736..757
FT /note="LRR 7"
FT REPEAT 758..779
FT /note="LRR 8"
FT REPEAT 780..801
FT /note="LRR 9"
FT REPEAT 802..822
FT /note="LRR 10"
FT REPEAT 846..867
FT /note="LRR 11"
FT REPEAT 868..889
FT /note="LRR 12"
FT REPEAT 892..913
FT /note="LRR 13"
FT REPEAT 914..935
FT /note="LRR 14"
FT REPEAT 940..962
FT /note="LRR 15"
FT DOMAIN 1005..1043
FT /note="LRRCT"
FT REGION 1..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 558
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MUTAGEN 98
FT /note="S->A: No phosphorylation by cdk1."
FT /evidence="ECO:0000269|PubMed:15062098"
FT MUTAGEN 103
FT /note="S->A: No phosphorylation by cdk1."
FT /evidence="ECO:0000269|PubMed:15062098"
FT MUTAGEN 136
FT /note="S->A: No phosphorylation by cdk1."
FT /evidence="ECO:0000269|PubMed:15062098"
FT MUTAGEN 199
FT /note="S->A: No phosphorylation by cdk1."
FT /evidence="ECO:0000269|PubMed:15062098"
FT MUTAGEN 208
FT /note="S->A: No phosphorylation by cdk1."
FT /evidence="ECO:0000269|PubMed:15062098"
FT MUTAGEN 360
FT /note="S->A: No phosphorylation by cdk1."
FT /evidence="ECO:0000269|PubMed:15062098"
FT MUTAGEN 393
FT /note="S->A: No phosphorylation by cdk1."
FT /evidence="ECO:0000269|PubMed:15062098"
FT MUTAGEN 558
FT /note="S->A: No phosphorylation by cdk1."
FT /evidence="ECO:0000269|PubMed:15062098"
FT MUTAGEN 767
FT /note="N->M: In cdc11-136; normal interaction with sid4;
FT normal localization at the SPB."
FT /evidence="ECO:0000269|PubMed:11676915"
FT MUTAGEN 947
FT /note="R->A: In cdc11-123; no interaction with sid4; does
FT not localize at the SPB."
FT /evidence="ECO:0000269|PubMed:11676915"
FT MUTAGEN 1041
FT /note="T->I: In cdc11-123; no interaction with sid4; does
FT not localize at the SPB."
FT /evidence="ECO:0000269|PubMed:11676915"
SQ SEQUENCE 1045 AA; 118628 MW; E66CBF374B00B046 CRC64;
MEQLWLEHDL SEEWIPQPQE QGSDNSSEPP TTSNVNNTQS TGRGSSGTST EHGTFKKGRN
DAPDVPQWKQ VNAKNPVARD IFARLDLENM FEESSKQSPP SKSPTKNPSK KSSNNSSRRS
SSSVGKLSNV SNMQSSPSKD PFVSQDYEKE SISSSQFSKK YSEGSLKSQQ SNTRSNSVHE
KQNTDHASNA SSSSSVVSSP SLKPNNTSPL KLFQGASDPF TREHLNQLTQ DVKSNSFENG
EKQFSLPEPR RPQKPMRTTE RKASLNTKDL YQEVEEVMAR LRGRMPNSGR ESTIFLPRKL
SGLREEEEQD EISVEVSQED SSNAFPSLSD QLHLKSLQSM KRVTSIFNDN DDSFPSASSS
PQRQAYMTDK MPLREIDVGS SQSSSKTARL NSSPKSTLKT SSVKTRRSHS AQSSRKVSDY
PNMVVITPAD LPEGIDTTQG SMEFDRIHNR WRRKGHDSDL GFDFETDEDA SLSHPERTIL
FKAASTRHQA NNDPNNLEKQ QPHSFPLRKQ NVAQSEFPKH SLRDNSENAP QILSSFHDLS
LQNESFDEMF NGRYENGSPI PFISSGSGLK SKADKDAEYS FSVSRQSIIQ ILSDVEPYEP
FWKRIIQLDI SRRHLDSLIG LSELCPSIEE LTLEGNEIAY LTGCPVTIRD LNAVENRLSS
LTSFSNLLNL QYLDISYNQL EDLTGLSSLI HLRELKVDSN HLWSLDGIQH LDGLLKLSAC
NNRIKELSFT NSNLHRLEEL LLGNNEIEEI EEISSLQNLM VLQLDNNKLT NLKASQPMIH
LRILRISNNA IHQLEVDQFP HLRTLYMDLN RFNRPPDIRR LKRLVNFSFR TQDPEASNFV
IQPSLDIRNL YLSNNTFVTL DCKHMFLGVR YLELANVQLK EVPKYIATSM PNLRVLDLSH
NYISDIESLK PLQMIHRLYL VGNRIKKMRN LCDILANLKQ LNVLDLRMNP LNFNIYPVID
DSIYELSAAS KYQQSINQKG HHRKEDPQKQ WQEKELAFSS TLSEAWRTRR KMYAEAILLA
CPHLEWLDGS DVSQSSRAAF TKSSN
