SLX1_CAEEL
ID SLX1_CAEEL Reviewed; 443 AA.
AC P91351;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Structure-specific endonuclease subunit SLX1 homolog {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=slx-1 {ECO:0000312|WormBase:F56A3.2};
GN Synonyms=giyd-1 {ECO:0000255|HAMAP-Rule:MF_03100};
GN ORFNames=F56A3.2 {ECO:0000312|WormBase:F56A3.2};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, INTERACTION WITH HIM-18, AND DISRUPTION PHENOTYPE.
RX PubMed=22927825; DOI=10.1371/journal.pgen.1002888;
RA Saito T.T., Mohideen F., Meyer K., Harper J.W., Colaiacovo M.P.;
RT "SLX-1 is required for maintaining genomic integrity and promoting meiotic
RT noncrossovers in the Caenorhabditis elegans germline.";
RL PLoS Genet. 8:E1002888-E1002888(2012).
RN [3]
RP FUNCTION, INTERACTION WITH HIM-18, AND DISRUPTION PHENOTYPE.
RX PubMed=23874210; DOI=10.1371/journal.pgen.1003586;
RA Saito T.T., Lui D.Y., Kim H.M., Meyer K., Colaiacovo M.P.;
RT "Interplay between structure-specific endonucleases for crossover control
RT during Caenorhabditis elegans meiosis.";
RL PLoS Genet. 9:E1003586-E1003586(2013).
CC -!- FUNCTION: Catalytic subunit of a heterodimeric 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 (Potential). Has a preference for
CC replication forks over 5' flap structures or Holliday junctions and
CC shows much lower activity toward 3' flap structures (PubMed:22927825).
CC Required for proper crossover distribution through inhibition of
CC crossover formation at the central region of chromosomes
CC (PubMed:22927825, PubMed:23874210). {ECO:0000255|HAMAP-Rule:MF_03100,
CC ECO:0000269|PubMed:22927825, ECO:0000269|PubMed:23874210}.
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 him-18/slx-4.
CC {ECO:0000269|PubMed:22927825, ECO:0000269|PubMed:23874210}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03100}.
CC -!- DOMAIN: Both the N- and C-terminal regions are required for interaction
CC with him-18. {ECO:0000269|PubMed:22927825}.
CC -!- DISRUPTION PHENOTYPE: Reduced brood size, increased embryonic lethality
CC and increased larval arrest (PubMed:22927825, PubMed:23874210).
CC Increased number of rad51 foci in meitotic and mitotic nuclei and
CC increased germ cell apoptosis (PubMed:22927825). Hypersensitivity to
CC ultraviolet C, nitrogen mustard and camptothecin but not to gamma
CC irradiation (PubMed:22927825). Increased chromosomal abnormalities
CC including increased intra- and inter-bivalent chromatin bridges
CC (PubMed:23874210). Increased meiotic crossover frequency in the center
CC of chromosomes III, IV, V and X with decreased frequency in the arm
CC regions of chromosomes III, IV, V and X (PubMed:22927825).
CC {ECO:0000269|PubMed:22927825, ECO:0000269|PubMed:23874210}.
CC -!- SIMILARITY: Belongs to the SLX1 family. {ECO:0000255|HAMAP-
CC Rule:MF_03100}.
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; FO080752; CCD66429.1; -; Genomic_DNA.
DR PIR; T29147; T29147.
DR RefSeq; NP_491541.1; NM_059140.4.
DR AlphaFoldDB; P91351; -.
DR SMR; P91351; -.
DR BioGRID; 37617; 1.
DR STRING; 6239.F56A3.2; -.
DR EPD; P91351; -.
DR PaxDb; P91351; -.
DR EnsemblMetazoa; F56A3.2.1; F56A3.2.1; WBGene00018909.
DR GeneID; 172157; -.
DR KEGG; cel:CELE_F56A3.2; -.
DR UCSC; F56A3.2; c. elegans.
DR CTD; 172157; -.
DR WormBase; F56A3.2; CE11216; WBGene00018909; slx-1.
DR eggNOG; KOG3005; Eukaryota.
DR GeneTree; ENSGT00390000013368; -.
DR HOGENOM; CLU_052232_0_0_1; -.
DR InParanoid; P91351; -.
DR OMA; SHFHSKC; -.
DR OrthoDB; 1171480at2759; -.
DR PhylomeDB; P91351; -.
DR PRO; PR:P91351; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00018909; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0033557; C:Slx1-Slx4 complex; IDA:UniProtKB.
DR GO; GO:0017108; F:5'-flap endonuclease activity; IEA:InterPro.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IGI:UniProtKB.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IGI:UniProtKB.
DR GO; GO:0036297; P:interstrand cross-link repair; IMP:UniProtKB.
DR GO; GO:0002164; P:larval development; IMP:UniProtKB.
DR GO; GO:0051307; P:meiotic chromosome separation; IMP:UniProtKB.
DR GO; GO:0000706; P:meiotic DNA double-strand break processing; IMP:UniProtKB.
DR GO; GO:0061064; P:negative regulation of nematode larval development; IMP:UniProtKB.
DR GO; GO:0040019; P:positive regulation of embryonic development; IMP:UniProtKB.
DR GO; GO:0000712; P:resolution of meiotic recombination intermediates; IGI:WormBase.
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; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF01541; GIY-YIG; 1.
DR SMART; SM00465; GIYc; 1.
DR SMART; SM00249; PHD; 1.
DR PROSITE; PS50164; GIY_YIG; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA recombination; DNA repair; Endonuclease; Hydrolase;
KW Metal-binding; Nuclease; Nucleus; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..443
FT /note="Structure-specific endonuclease subunit SLX1
FT homolog"
FT /id="PRO_0000383751"
FT DOMAIN 171..258
FT /note="GIY-YIG"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
FT ZN_FING 340..395
FT /note="SLX1-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03100"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 443 AA; 50536 MW; 06B7742BB36CEE5D CRC64;
METFILSSDS DDDSGPPPSK RRTIEGIPRS FSGDKKIRFS FGASNMSQDT TQEIIPEDTD
TVPLTIPSTP ALSGKFDSKT PKSVRRRSVS MSCFTPIVET INQPPTNQAC SSFLQKEYNF
HDLSSDEEGG DGGAGCSKDE DKIIEDNLNL RALLSPEKKK RKEKIEEVQN EFYGVYCLIS
RSDRPCYKNR CYIGYTVDPN RRIMQHNGGR DKGGAKKTDS RGPWDMVCVV HGFPNHVAAL
HFEWAWQNPL VSKSLKEKQL RKERKETPFA FQLRIACELM NSSAFCRFAL TFRWLITTEE
LPFPTSCVPP DHTKLRFGKV KKEMSLVPSK REDYLEMGEC RICGKDIEKL WSLVRCISAT
CPSHFHSKCL SENGLKLKNE HVDHVYPLKA NCPTCGQFYL WGDIIREQRR IIKISTKCAE
EFQNMVVRKE LPHREISPIS SKK
