SLX4_SCHPO
ID SLX4_SCHPO Reviewed; 419 AA.
AC Q9P6M0;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Structure-specific endonuclease subunit slx4 {ECO:0000303|PubMed:14528010, ECO:0000312|EMBL:CAB90772.1};
DE AltName: Full=Synthetic lethal of unknown function protein 4 {ECO:0000250|UniProtKB:Q12098};
GN Name=slx4 {ECO:0000312|EMBL:CAB90772.1}; ORFNames=SPAC688.06c;
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] {ECO:0000312|EMBL:CAB90772.1}
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] {ECO:0000305}
RP PROTEIN SEQUENCE OF 116-126; 313-323 AND 345-358, FUNCTION, ENZYMATIC
RP ACTIVITY OF THE SLX1-SLX4 COMPLEX, INTERACTION WITH SLX1, SUBCELLULAR
RP LOCATION, DELETION MUTANT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14528010; DOI=10.1091/mbc.e03-08-0586;
RA Coulon S., Gaillard P.-H.L., Chahwan C., McDonald W.H., Yates J.R. III,
RA Russell P.;
RT "Slx1-Slx4 are subunits of a structure-specific endonuclease that maintains
RT ribosomal DNA in fission yeast.";
RL Mol. Biol. Cell 15:71-80(2004).
RN [3] {ECO:0000305}
RP FUNCTION, INTERACTION WITH SLX1, AND SUBCELLULAR LOCATION.
RX PubMed=16467377; DOI=10.1091/mbc.e05-11-1006;
RA Coulon S., Noguchi E., Noguchi C., Du L.-L., Nakamura T.M., Russell P.;
RT "Rad22Rad52-dependent repair of ribosomal DNA repeats cleaved by Slx1-Slx4
RT endonuclease.";
RL Mol. Biol. Cell 17:2081-2090(2006).
RN [4] {ECO:0000305}
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).
CC -!- FUNCTION: Regulatory subunit of the slx1-slx4 structure-specific
CC endonuclease that resolves DNA secondary structures generated during
CC DNA repair and recombination. Has endonuclease activity towards
CC branched DNA substrates, introducing single-strand cuts in duplex DNA
CC close to junctions with ss-DNA. Has a preference for stem-loop (SL) and
CC splayed arm Y structures. Introduces a single-strand cut in duplex DNA
CC on the 3' side of a double-strand/single-strand junction with respect
CC to the single-strand moving 3' to 5' away from the junction. Plays a
CC critical role in maintaining the integrity of the ribosomal DNA (rDNA)
CC loci, where it has a role in re-starting stalled replication forks. The
CC complex initiates homologous recombination (HR) events, used to
CC maintain rDNA copy number, in the rDNA repeats that are processed by a
CC mechanism that requires rad22, but not rhp51. Has Holliday junction
CC resolvase activity in vitro. Slx4 is required for efficient processing
CC of DNA substrates. {ECO:0000269|PubMed:14528010,
CC ECO:0000269|PubMed:16467377}.
CC -!- SUBUNIT: Forms a heterodimer with slx1.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14528010,
CC ECO:0000269|PubMed:16467377, ECO:0000269|PubMed:16823372}.
CC Note=Associates with chromatin at rDNA repeat protrusions.
CC {ECO:0000269|PubMed:14528010, ECO:0000269|PubMed:16467377,
CC ECO:0000269|PubMed:16823372}.
CC -!- PTM: Phosphorylated in response to DNA damage. {ECO:0000250}.
CC -!- MISCELLANEOUS: Simultaneous elimination of slx4 and rqh1 is lethal.
CC {ECO:0000269|PubMed:14528010}.
CC -!- SIMILARITY: Belongs to the SLX4 family. {ECO:0000305}.
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DR EMBL; CU329670; CAB90772.1; -; Genomic_DNA.
DR RefSeq; NP_594064.1; NM_001019488.2.
DR PDB; 4ZDT; X-ray; 2.00 A; B/D=352-419.
DR PDBsum; 4ZDT; -.
DR AlphaFoldDB; Q9P6M0; -.
DR SMR; Q9P6M0; -.
DR BioGRID; 279898; 133.
DR STRING; 4896.SPAC688.06c.1; -.
DR PaxDb; Q9P6M0; -.
DR EnsemblFungi; SPAC688.06c.1; SPAC688.06c.1:pep; SPAC688.06c.
DR GeneID; 2543478; -.
DR KEGG; spo:SPAC688.06c; -.
DR PomBase; SPAC688.06c; slx4.
DR VEuPathDB; FungiDB:SPAC688.06c; -.
DR HOGENOM; CLU_655797_0_0_1; -.
DR PRO; PR:Q9P6M0; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0030875; C:rDNA protrusion; IPI:PomBase.
DR GO; GO:0033557; C:Slx1-Slx4 complex; IDA:PomBase.
DR GO; GO:0019899; F:enzyme binding; IBA:GO_Central.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; ISO:PomBase.
DR GO; GO:0036297; P:interstrand cross-link repair; IBA:GO_Central.
DR GO; GO:0043007; P:maintenance of rDNA; IGI:PomBase.
DR GO; GO:0000706; P:meiotic DNA double-strand break processing; IBA:GO_Central.
DR GO; GO:1902969; P:mitotic DNA replication; ISO:PomBase.
DR GO; GO:0031297; P:replication fork processing; TAS:PomBase.
DR GO; GO:0000712; P:resolution of meiotic recombination intermediates; IBA:GO_Central.
DR InterPro; IPR018574; Structure-sp_endonuc_su_Slx4.
DR Pfam; PF09494; Slx4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA damage; DNA recombination;
KW DNA repair; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..419
FT /note="Structure-specific endonuclease subunit slx4"
FT /id="PRO_0000349134"
FT HELIX 352..366
FT /evidence="ECO:0007829|PDB:4ZDT"
FT HELIX 371..377
FT /evidence="ECO:0007829|PDB:4ZDT"
FT HELIX 384..393
FT /evidence="ECO:0007829|PDB:4ZDT"
FT HELIX 400..410
FT /evidence="ECO:0007829|PDB:4ZDT"
SQ SEQUENCE 419 AA; 47765 MW; 00850BC9B795EA56 CRC64;
MSAEEYIEVS SSPDIFTDDD DMITIEPELN KNPKDCNSKR KRSVTECCEI RLITSKCDFE
STQQLVHHNC TGHKVHEHNL NAVDEEDFDT ENLPLLFSSF SDNESDILEP DLNTRVAEDN
DVLLSRYSKI KNSASCRNTF EHSAYHSNRE EISSSGFYYH RKPQLFEKSL EKLGNKSIEA
NRSPLIKELC ESANSTENVC FSVSTVDEIQ QRHPSAGHSI DSTCQSNSFL EGDSATHKKK
KTDNIKEFTS CEFNDRSRTL LNYAGYMDTN KNADNEAKSL KEKLENFPVE KLRAIAESYG
FKSSDSKATL IKIVESCLDA IDSRSQSKKL GKETPHDYLI TSTKTVLEFD DIVTQTHRAI
SQVVKQAKDN SVWIKILTYS AIDVEEFQLW LKRKNLNVSL DLIKSWCDKY GVLMKGSWH
