ID   SLX1_RAT                Reviewed;         271 AA.
AC   Q5PQP5;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Structure-specific endonuclease subunit SLX1 {ECO:0000255|HAMAP-Rule:MF_03100};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03100};
DE   AltName: Full=GIY-YIG domain-containing protein 1 {ECO:0000255|HAMAP-Rule:MF_03100};
GN   Name=Slx1b; Synonyms=Giyd1, Giyd2, Slx1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Catalytic 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 5'-flap
CC       structures, and promotes symmetrical cleavage of static and migrating
CC       Holliday junctions (HJs). Resolves HJs by generating two pairs of
CC       ligatable, nicked duplex products. {ECO:0000255|HAMAP-Rule:MF_03100}.
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03100};
CC   -!- SUBUNIT: Forms a heterodimer with SLX4. {ECO:0000255|HAMAP-
CC       Rule:MF_03100}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03100}.
CC   -!- SIMILARITY: Belongs to the SLX1 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03100}.
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DR   EMBL; BC087090; AAH87090.1; -; mRNA.
DR   RefSeq; NP_001009292.1; NM_001009292.1.
DR   AlphaFoldDB; Q5PQP5; -.
DR   SMR; Q5PQP5; -.
DR   STRING; 10116.ENSRNOP00000026231; -.
DR   PhosphoSitePlus; Q5PQP5; -.
DR   PaxDb; Q5PQP5; -.
DR   Ensembl; ENSRNOT00000026231; ENSRNOP00000026231; ENSRNOG00000019369.
DR   GeneID; 293489; -.
DR   KEGG; rno:293489; -.
DR   UCSC; RGD:1311568; rat.
DR   CTD; 79008; -.
DR   RGD; 1311568; Slx1b.
DR   eggNOG; KOG3005; Eukaryota.
DR   GeneTree; ENSGT00390000013368; -.
DR   HOGENOM; CLU_030739_0_0_1; -.
DR   InParanoid; Q5PQP5; -.
DR   OMA; LQFEHAW; -.
DR   OrthoDB; 844266at2759; -.
DR   PhylomeDB; Q5PQP5; -.
DR   TreeFam; TF352344; -.
DR   Reactome; R-RNO-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
DR   Reactome; R-RNO-6783310; Fanconi Anemia Pathway.
DR   PRO; PR:Q5PQP5; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000019369; Expressed in pancreas and 19 other tissues.
DR   ExpressionAtlas; Q5PQP5; baseline and differential.
DR   Genevisible; Q5PQP5; RN.
DR   GO; GO:0033557; C:Slx1-Slx4 complex; ISO:RGD.
DR   GO; GO:0017108; F:5'-flap endonuclease activity; ISO:RGD.
DR   GO; GO:0008821; F:crossover junction endodeoxyribonuclease activity; ISO:RGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0010792; P:DNA double-strand break processing involved in repair via single-strand annealing; ISO:RGD.
DR   GO; GO:0006281; P:DNA repair; ISO:RGD.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; ISO:RGD.
DR   GO; GO:1904357; P:negative regulation of telomere maintenance via telomere lengthening; ISO:RGD.
DR   GO; GO:1904431; P:positive regulation of t-circle formation; ISO:RGD.
DR   GO; GO:0090656; P:t-circle formation; ISO:RGD.
DR   GO; GO:0010833; P:telomere maintenance via telomere lengthening; ISO:RGD.
DR   GO; GO:0061820; P:telomeric D-loop disassembly; ISO:RGD.
DR   Gene3D; 3.30.40.10; -; 1.
DR   Gene3D; 3.40.1440.10; -; 1.
DR   HAMAP; MF_03100; Endonuc_su_Slx1; 1.
DR   InterPro; IPR000305; GIY-YIG_endonuc.
DR   InterPro; IPR035901; GIY-YIG_endonuc_sf.
DR   InterPro; IPR027520; Slx1.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF01541; GIY-YIG; 1.
DR   SMART; SM00465; GIYc; 1.
DR   SUPFAM; SSF82771; SSF82771; 1.
DR   PROSITE; PS50164; GIY_YIG; 1.
PE   2: Evidence at transcript level;
KW   DNA damage; DNA recombination; DNA repair; Endonuclease; Hydrolase;
KW   Metal-binding; Nuclease; Nucleus; Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..271
FT                   /note="Structure-specific endonuclease subunit SLX1"
FT                   /id="PRO_0000332122"
FT   DOMAIN          9..94
FT                   /note="GIY-YIG"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
FT   ZN_FING         182..234
FT                   /note="SLX1-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
SQ   SEQUENCE   271 AA;  30746 MW;  A6B6F5BB87969433 CRC64;
     MGHAARPGRF FGVYLLYCQN PRHRGRVYVG FTVNPARRVR QHNAGRKKGG AWRTSGRGPW
     DMVLILHGFP SAVAALRFEW AWQHPQASRR LTHVGPRLRS EASFTFHLRV LAHMLRVPPW
     VRLPLTVRWL RPDFRHELCP APPPHMPIAF GPPPPQPLVP KRPAASEADS ERRLDLGAKA
     SCTLCARMLQ DEEGPLCCPH PGCPLRAHII CLAEEFLQEE PGQLLPLEGH CPSCKKSLLW
     GNLVGQCHED TEEEEVDLEL EEEHWTDLLE T