SMI1_SCHPO
ID SMI1_SCHPO Reviewed; 504 AA.
AC O14362;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Cell wall biosynthesis/cell cycle regulator smi1;
GN Name=smi1; ORFNames=SPBC30D10.17c;
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 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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-500, AND IDENTIFICATION BY
RP 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).
RN [4]
RP FUNCTION.
RX PubMed=19366728; DOI=10.1242/jcs.046466;
RA Sajiki K., Hatanaka M., Nakamura T., Takeda K., Shimanuki M., Yoshida T.,
RA Hanyu Y., Hayashi T., Nakaseko Y., Yanagida M.;
RT "Genetic control of cellular quiescence in S. pombe.";
RL J. Cell Sci. 122:1418-1429(2009).
CC -!- FUNCTION: Protein involved in the regulation of cell wall assembly and
CC 1,3-beta-glucan synthesis, possibly through the transcriptional
CC regulation of cell wall glucan and chitin synthesis (By similarity).
CC Involved in cellular response to nitrogen starvation and required for
CC quiescence-maintenance by regulating negatively G0 to G1 transition.
CC {ECO:0000250, ECO:0000269|PubMed:19366728}.
CC -!- SUBCELLULAR LOCATION: Cell septum {ECO:0000269|PubMed:16823372}.
CC Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the KNR4/SMI1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329671; CAB10812.1; -; Genomic_DNA.
DR PIR; T40179; T40179.
DR RefSeq; NP_596268.1; NM_001022189.2.
DR AlphaFoldDB; O14362; -.
DR SMR; O14362; -.
DR BioGRID; 276868; 1.
DR STRING; 4896.SPBC30D10.17c.1; -.
DR iPTMnet; O14362; -.
DR MaxQB; O14362; -.
DR PaxDb; O14362; -.
DR PRIDE; O14362; -.
DR EnsemblFungi; SPBC30D10.17c.1; SPBC30D10.17c.1:pep; SPBC30D10.17c.
DR GeneID; 2540339; -.
DR KEGG; spo:SPBC30D10.17c; -.
DR PomBase; SPBC30D10.17c; smi1.
DR VEuPathDB; FungiDB:SPBC30D10.17c; -.
DR eggNOG; ENOG502QTAZ; Eukaryota.
DR HOGENOM; CLU_024700_0_0_1; -.
DR InParanoid; O14362; -.
DR OMA; WAEENYP; -.
DR PhylomeDB; O14362; -.
DR PRO; PR:O14362; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0030428; C:cell septum; IEA:UniProtKB-SubCell.
DR GO; GO:0097708; C:intracellular vesicle; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IMP:PomBase.
DR GO; GO:0042546; P:cell wall biogenesis; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0140278; P:mitotic division septum assembly; EXP:PomBase.
DR GO; GO:0032995; P:regulation of fungal-type cell wall biogenesis; IBA:GO_Central.
DR GO; GO:1901901; P:regulation of protein localization to cell division site involved in cytokinesis; EXP:PomBase.
DR Gene3D; 3.40.1580.10; -; 1.
DR InterPro; IPR009203; Knr4/Smi1.
DR InterPro; IPR018958; Knr4/Smi1-like_dom.
DR InterPro; IPR037883; Knr4/Smi1-like_sf.
DR Pfam; PF09346; SMI1_KNR4; 1.
DR PIRSF; PIRSF017023; KNR4; 1.
DR SMART; SM00860; SMI1_KNR4; 1.
DR SUPFAM; SSF160631; SSF160631; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cell wall biogenesis/degradation; DNA-binding;
KW Mitosis; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..504
FT /note="Cell wall biosynthesis/cell cycle regulator smi1"
FT /id="PRO_0000209877"
FT REGION 17..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..473
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..504
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 500
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 504 AA; 55558 MW; 63E7BBF4BCD9BFD8 CRC64;
MSKNSFSSMA NSVTSFFQSL TTPNRHADPS FRPSRREKQS RLPTPLQSVA ASAYSGVNAS
QTGLLNDSRA NSVTNLPNSS NTSQVGLNNI SPAPVGYVPG SKTNELANNS MEMQEISPNG
SASLPPPVSE SWRRIDRWAE ENYYELYCQL CYGATVADVD SLEYELECTL PRDVRESLYI
HDGQDRGGQP TGILFGVTLL DIEEIEEESE LWRRVAQSYA EATLAGKIDQ AVASRQASFP
PGAVQCVYAH PGWIPLAKDF VGNNIAIDLA PGPAGQWGQV ILFGRDQDTK YVVARSWADF
LAIVAYDMEN GKWLVDEDDN SLRLIYGPPR EQWSYLDILK YRARKAERRK FKKRDGKRTT
RPIPKSIAKE DVTNSANSTA PSTGTTVLDD GLDNNYEDIP LYGPSKDEEL IKKEELEADT
DLGLINTSEI NQPANLPDEP TAETSNPVSA TTVEAVTTTA DNKDEEKNDH VTEDVSQNST
IAEASSLQAQ EEEKEIETTS VKQE
