SWI3_SCHPO
ID SWI3_SCHPO Reviewed; 181 AA.
AC O14350; Q6IUU5;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Swi1-interacting protein swi3;
DE AltName: Full=Replication fork protection complex subunit swi3;
GN Name=swi3; ORFNames=SPBC30D10.04;
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 [MRNA], FUNCTION, INTERACTION WITH SWI1, AND
RP 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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INTERACTION WITH SWI1.
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 [3]
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 [4]
RP SEQUENCE REVISION TO N-TERMINUS.
RA Wood V., Rajandream M.A., Barrell B.G., Lauber J., Hilbert H.,
RA Duesterhoeft A.;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Forms a fork protection complex (FPC) with swi1. 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: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 O14350; Q9UUM2: swi1; NbExp=5; IntAct=EBI-465952, EBI-465942;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15367656}.
CC Note=Nuclear throughout the cell cycle. Associated with chromatin
CC during S phase.
CC -!- SIMILARITY: Belongs to the CSM3 family. {ECO:0000305}.
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DR EMBL; AY498547; AAS77252.1; -; mRNA.
DR EMBL; AY623652; AAT44735.1; -; Genomic_DNA.
DR EMBL; CU329671; CAH17997.1; -; Genomic_DNA.
DR PIR; T40192; T40192.
DR RefSeq; NP_001018832.1; NM_001022202.2.
DR AlphaFoldDB; O14350; -.
DR SMR; O14350; -.
DR BioGRID; 280399; 113.
DR IntAct; O14350; 1.
DR STRING; 4896.SPBC30D10.04.1; -.
DR MaxQB; O14350; -.
DR PaxDb; O14350; -.
DR EnsemblFungi; SPBC30D10.04.1; SPBC30D10.04.1:pep; SPBC30D10.04.
DR GeneID; 3361323; -.
DR KEGG; spo:SPBC30D10.04; -.
DR PomBase; SPBC30D10.04; swi3.
DR VEuPathDB; FungiDB:SPBC30D10.04; -.
DR eggNOG; KOG3004; Eukaryota.
DR HOGENOM; CLU_1435204_0_0_1; -.
DR InParanoid; O14350; -.
DR PhylomeDB; O14350; -.
DR PRO; PR:O14350; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0005739; C:mitochondrion; 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:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
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:0071515; P:mating-type locus imprinting; IMP:PomBase.
DR GO; GO:0043388; P:positive regulation of DNA binding; IDA:PomBase.
DR GO; GO:0043111; P:replication fork arrest; IBA:GO_Central.
DR GO; GO:0048478; P:replication fork protection; IDA:UniProtKB.
DR InterPro; IPR012923; Csm3.
DR InterPro; IPR040038; TIPIN/Csm3/Swi3.
DR PANTHER; PTHR13220; PTHR13220; 1.
DR Pfam; PF07962; Swi3; 1.
PE 1: Evidence at protein level;
KW Cell cycle; DNA damage; DNA replication inhibitor; Nucleus;
KW Reference proteome.
FT CHAIN 1..181
FT /note="Swi1-interacting protein swi3"
FT /id="PRO_0000072350"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 181 AA; 20581 MW; 4DEC192308B23922 CRC64;
MSTAASDSGV EKLVEENKRE EVKKNEEEKE FDLGLEENPD SVKKPRKRLA KFDEERLISE
NGIPKLRKMM RKVKLKGKGH EAKDLKQLLG MYHIWTHELY PRATFDDSIS YLKTLGKHRS
VKVRRRGWIN EIAVENGSDS NASLFTGPSS NSLVNLTSGD PYVQDTADDA FVAQDNDTQL
E
