SWI1_SCHPO
ID SWI1_SCHPO Reviewed; 971 AA.
AC Q9UUM2; Q9Y7X0;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Mating-type switching protein swi1;
DE AltName: Full=Replication fork protection complex subunit swi1;
GN Name=swi1; ORFNames=SPBC216.06c;
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].
RC STRAIN=972 / ATCC 24843;
RA Schmidt H.;
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=14560029; DOI=10.1128/mcb.23.21.7861-7874.2003;
RA Noguchi E., Noguchi C., Du L.L., Russell P.;
RT "Swi1 prevents replication fork collapse and controls checkpoint kinase
RT Cds1.";
RL Mol. Cell. Biol. 23:7861-7874(2003).
RN [4]
RP FUNCTION.
RX PubMed=11030618; DOI=10.1016/s0092-8674(00)00063-5;
RA Dalgaard J.Z., Klar A.J.;
RT "swi1 and swi3 perform imprinting, pausing, and termination of DNA
RT replication in S. pombe.";
RL Cell 102:745-751(2000).
RN [5]
RP FUNCTION, INTERACTION WITH SWI3, AND SUBCELLULAR LOCATION.
RX PubMed=15367656; DOI=10.1128/mcb.24.19.8342-8355.2004;
RA Noguchi E., Noguchi C., McDonald W.H., Yates J.R. III, Russell P.;
RT "Swi1 and swi3 are components of a replication fork protection complex in
RT fission yeast.";
RL Mol. Cell. Biol. 24:8342-8355(2004).
RN [6]
RP FUNCTION, AND INTERACTION WITH SWI3.
RX PubMed=15509785; DOI=10.1128/mcb.24.22.9813-9822.2004;
RA Lee B.-S., Grewal S.I.S., Klar A.J.S.;
RT "Biochemical interactions between proteins and mat1 cis-acting sequences
RT required for imprinting in fission yeast.";
RL Mol. Cell. Biol. 24:9813-9822(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528; SER-536 AND SER-970, 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: Forms a fork protection complex (FPC) with swi3. FPC
CC coordinates leading and lagging strand synthesis and moves with the
CC replication fork. It is required for programmed fork-pausing which is
CC necessary for mating-type switching. FPC stabilizes replication forks
CC in a configuration that is recognized by replication checkpoint
CC sensors. It is involved in termination at the mat1-proximal polar-
CC terminator of replication (RTS1) and also required for activation of
CC the Rad53-like checkpoint kinase cds1. {ECO:0000269|PubMed:11030618,
CC ECO:0000269|PubMed:14560029, ECO:0000269|PubMed:15367656,
CC ECO:0000269|PubMed:15509785}.
CC -!- SUBUNIT: Fork protection complex (FPC) consisting of swi1 and swi3
CC interacts with mat1 cis-acting sequences and mat1-proximal polar-
CC terminator of replication (RTS1). {ECO:0000269|PubMed:15367656,
CC ECO:0000269|PubMed:15509785}.
CC -!- INTERACTION:
CC Q9UUM2; O14350: swi3; NbExp=5; IntAct=EBI-465942, EBI-465952;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14560029,
CC ECO:0000269|PubMed:15367656}. Note=Associated with chromatin during S
CC phase. Nuclear accumulation requires swi3.
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DR EMBL; Y19036; CAB44362.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB40166.1; -; Genomic_DNA.
DR PIR; T39912; T39912.
DR PIR; T43656; T43656.
DR RefSeq; NP_595358.1; NM_001021265.2.
DR AlphaFoldDB; Q9UUM2; -.
DR SMR; Q9UUM2; -.
DR BioGRID; 277251; 62.
DR IntAct; Q9UUM2; 4.
DR STRING; 4896.SPBC216.06c.1; -.
DR iPTMnet; Q9UUM2; -.
DR MaxQB; Q9UUM2; -.
DR PaxDb; Q9UUM2; -.
DR PRIDE; Q9UUM2; -.
DR EnsemblFungi; SPBC216.06c.1; SPBC216.06c.1:pep; SPBC216.06c.
DR GeneID; 2540728; -.
DR KEGG; spo:SPBC216.06c; -.
DR PomBase; SPBC216.06c; swi1.
DR VEuPathDB; FungiDB:SPBC216.06c; -.
DR eggNOG; KOG1974; Eukaryota.
DR HOGENOM; CLU_004390_0_0_1; -.
DR InParanoid; Q9UUM2; -.
DR OMA; WLKLYDE; -.
DR PhylomeDB; Q9UUM2; -.
DR PRO; PR:Q9UUM2; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0044732; C:mitotic spindle pole body; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0031298; C:replication fork protection complex; IDA:PomBase.
DR GO; GO:0003677; F:DNA binding; IDA:PomBase.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:PomBase.
DR GO; GO:0000403; F:Y-form DNA binding; IDA:PomBase.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0000076; P:DNA replication checkpoint signaling; IBA:GO_Central.
DR GO; GO:0007534; P:gene conversion at mating-type locus; IMP:PomBase.
DR GO; GO:0045950; P:negative regulation of mitotic recombination; IDA:PomBase.
DR GO; GO:0043388; P:positive regulation of DNA binding; IDA:PomBase.
DR GO; GO:0061806; P:regulation of DNA recombination at centromere; IMP:PomBase.
DR GO; GO:0043111; P:replication fork arrest; IDA:PomBase.
DR GO; GO:0031297; P:replication fork processing; IMP:PomBase.
DR GO; GO:0048478; P:replication fork protection; IDA:UniProtKB.
DR InterPro; IPR044998; Timeless.
DR InterPro; IPR006906; Timeless_N.
DR PANTHER; PTHR22940; PTHR22940; 1.
DR Pfam; PF04821; TIMELESS; 1.
PE 1: Evidence at protein level;
KW Cell cycle; DNA damage; DNA replication inhibitor; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..971
FT /note="Mating-type switching protein swi1"
FT /id="PRO_0000072348"
FT MOD_RES 528
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 536
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 970
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 195
FT /note="A -> R (in Ref. 1; CAB44362)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 971 AA; 112628 MW; 77A0FB265C82C2BE CRC64;
MELDEVIQGI VSAIGGFDYS DDEKVYVLGD EALACLKDLK RYLQVVDEKY KVWQIRSLLS
SLQLVTNDIC PILSDWDKDI TNYRNWRIAL ACVELLVPLT WPLETEHETF RENVDVLYNL
RQAQSNYKNS ILSYKKGSVL SAILAVLLKP LSTPAESRTL RDKGIIRIVL LLFRNILQID
ELKTKNETII SFAKAHILDL IVTLVSNLDE FEHFDVYILE IVYNLIRGCK PSALFSDASL
TNSQTELNSL LLKESTQNRY LKRNAHTRHN RFGTMLSVQT EDRRFTIASQ NIKTDGLDEL
DSHKRFRKRG TRRKHFDDIN KSFFINTEAG TALRNFAVEF LEAGFNPLFQ SLLKDLERED
PRVLPIHKMQ LLYVQSFFLE FMRFSSKPKK TEEIYSNDYS FGLAASVFDQ RALIMHNRLM
VESFEMKQWS TFQASMLSMT QLLFTLRSMT LCSSEIYQRI ADNLLSNIFY QEEILLLVYS
ALKHFKTQSF GYLDAITELT IVLLKELEKF SSAKQYLYVK KRRRNQKSVD SNVLESDEDE
ESSLINANAA VEDRLFDFGR YESRYCDNGC IDSFVLFLQC YQDLDSKQIH RAISFFYRIF
VKQKCHVYLY RLDFLRVLDK MFNDHVYFST TNSARQDFEQ FFVYYMRKLS DALKDVPALF
IELPFPKLTD TFYYLEYGKS PLFSIHGSRK GPLYETVPGL SHLEKVAAVV ACLINENKSD
LLDELKVQLN CLISERKLIT LADENKYINE GGNDGERMGK NLKGDTDSFN TALLKDGKFR
LLLELCGFEE SDNNIDVQAL WKLPNSVIID ELVEHAMLLR RFTDDPPTFE GTKPEDLLVR
KQRGNVRLPS SSEGETSDEE IEFEADDPIT FANRREALNK ITDRKRKKMK TNETIIDHTT
RKKKENHLRS AKYIVDSDDD SETDIAFFQS EAALREKNAQ KASALFKRID DLEMEGKLQE
IEQLSENSSS D
