SLD2_SCHPO
ID SLD2_SCHPO Reviewed; 337 AA.
AC O14216;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=DNA replication regulator sld2;
DE AltName: Full=DNA replication and checkpoint protein 1;
GN Name=drc1; Synonyms=sld2; ORFNames=SPAC6B12.11;
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 RAD4, SUBCELLULAR LOCATION, PHOSPHORYLATION AT
RP THR-60; THR-74; SER-87; THR-99 AND THR-154, AND MUTAGENESIS OF THR-60;
RP THR-74; SER-87; THR-99 AND THR-154.
RX PubMed=11937031; DOI=10.1016/s0960-9822(02)00739-x;
RA Noguchi E., Shanahan P., Noguchi C., Russell P.;
RT "CDK phosphorylation of Drc1 regulates DNA replication in fission yeast.";
RL Curr. Biol. 12:599-605(2002).
RN [3]
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, 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).
CC -!- FUNCTION: Has a role in the initiation of DNA replication. Required at
CC S-phase checkpoint. {ECO:0000269|PubMed:11937031}.
CC -!- SUBUNIT: Interacts with rad4. {ECO:0000269|PubMed:11937031}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- PTM: Phosphorylated by cdc2 at the onset of S-phase.
CC {ECO:0000269|PubMed:11937031, ECO:0000269|PubMed:18257517}.
CC -!- SIMILARITY: Belongs to the SLD2 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; CU329670; CAB11071.1; -; Genomic_DNA.
DR PIR; T39018; T39018.
DR RefSeq; NP_593766.1; NM_001019196.2.
DR AlphaFoldDB; O14216; -.
DR SMR; O14216; -.
DR BioGRID; 279734; 10.
DR IntAct; O14216; 1.
DR MINT; O14216; -.
DR STRING; 4896.SPAC6B12.11.1; -.
DR iPTMnet; O14216; -.
DR MaxQB; O14216; -.
DR PaxDb; O14216; -.
DR PRIDE; O14216; -.
DR EnsemblFungi; SPAC6B12.11.1; SPAC6B12.11.1:pep; SPAC6B12.11.
DR GeneID; 2543310; -.
DR KEGG; spo:SPAC6B12.11; -.
DR PomBase; SPAC6B12.11; drc1.
DR VEuPathDB; FungiDB:SPAC6B12.11; -.
DR HOGENOM; CLU_824276_0_0_1; -.
DR InParanoid; O14216; -.
DR OMA; WEHEFSH; -.
DR PhylomeDB; O14216; -.
DR PRO; PR:O14216; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031261; C:DNA replication preinitiation complex; IBA:GO_Central.
DR GO; GO:0043596; C:nuclear replication fork; ISO:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0003688; F:DNA replication origin binding; IBA:GO_Central.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0006270; P:DNA replication initiation; IBA:GO_Central.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IBA:GO_Central.
DR GO; GO:1902975; P:mitotic DNA replication initiation; EXP:PomBase.
DR GO; GO:1902977; P:mitotic DNA replication preinitiation complex assembly; IMP:PomBase.
DR InterPro; IPR021110; DNA_rep_checkpnt_protein.
DR InterPro; IPR040203; Sld2.
DR PANTHER; PTHR28124; PTHR28124; 1.
DR Pfam; PF11719; Drc1-Sld2; 2.
PE 1: Evidence at protein level;
KW Cell cycle; Cytoplasm; DNA replication; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..337
FT /note="DNA replication regulator sld2"
FT /id="PRO_0000116666"
FT REGION 71..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 60
FT /note="Phosphothreonine; by cdc2"
FT /evidence="ECO:0000269|PubMed:11937031"
FT MOD_RES 74
FT /note="Phosphothreonine; by cdc2"
FT /evidence="ECO:0000269|PubMed:11937031"
FT MOD_RES 87
FT /note="Phosphoserine; by cdc2"
FT /evidence="ECO:0000269|PubMed:11937031"
FT MOD_RES 99
FT /note="Phosphothreonine; by cdc2"
FT /evidence="ECO:0000269|PubMed:11937031"
FT MOD_RES 154
FT /note="Phosphothreonine; by cdc2"
FT /evidence="ECO:0000269|PubMed:11937031"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MUTAGEN 60
FT /note="T->A: Decrease in phosphorylation by cdc2; no
FT interaction with rad4."
FT /evidence="ECO:0000269|PubMed:11937031"
FT MUTAGEN 74
FT /note="T->A: Decrease in phosphorylation by cdc2; no
FT interaction with rad4."
FT /evidence="ECO:0000269|PubMed:11937031"
FT MUTAGEN 87
FT /note="S->A: Decrease in phosphorylation by cdc2; no
FT interaction with rad4."
FT /evidence="ECO:0000269|PubMed:11937031"
FT MUTAGEN 99
FT /note="T->A: Decrease in phosphorylation by cdc2; no
FT interaction with rad4."
FT /evidence="ECO:0000269|PubMed:11937031"
FT MUTAGEN 154
FT /note="T->A: Decrease in phosphorylation by cdc2; no
FT interaction with rad4."
FT /evidence="ECO:0000269|PubMed:11937031"
SQ SEQUENCE 337 AA; 38685 MW; 30A532A8C6322B1C CRC64;
MHDESRTKQI SSIKALLKKW EHEYVHTNNC KPSKEDVKKQ PEIALLYKQY YELKRESSIT
PKKAKTKVDF KFQTPTKQRA ETEANESPKA PRNDYLQVTP KTVDKSLLGP TPQLSRRVLN
LLEDMSPIAD SHVDQISDIK HNTSEISSTM IPTTPSKNPE PVAQHTPTVL ETPSSYRLQV
YTSPNLLRVN APCRKSLSEM LRELKDIEDD YGSNEEKILQ EFESFSSSSS ESLVDRDISQ
PMKKKIKRQN RLVKLPPSMN LSKSHLEGLP EIDEDAENGI DDNEDTTASK DSSPFLDLQS
ERQNKKIMRN GLVIGKQVSQ NYSSYKLKKR KFRRHRS
