SLX1_MOUSE
ID SLX1_MOUSE Reviewed; 270 AA.
AC Q8BX32; Q9D609;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 130.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Embryonic stem cell, and Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=27010503; DOI=10.1371/journal.pone.0152278;
RA Braun J., Meixner A., Brachner A., Foisner R.;
RT "The GIY-YIG type endonuclease ankyrin repeat and LEM domain-containing
RT protein 1 (ANKLE1) is dispensable for mouse hematopoiesis.";
RL PLoS ONE 11:E0152278-E0152278(2016).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BX32-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BX32-2; Sequence=VSP_033332, VSP_033333;
CC -!- TISSUE SPECIFICITY: Expressed in testis, colon, bone marrow, brain,
CC thymus and to a lesser extent in heart, kidney, skeletal muscle and
CC spleen. {ECO:0000269|PubMed:27010503}.
CC -!- SIMILARITY: Belongs to the SLX1 family. {ECO:0000255|HAMAP-
CC Rule:MF_03100}.
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DR EMBL; AK014753; BAB29533.1; -; mRNA.
DR EMBL; AK049139; BAC33566.1; -; mRNA.
DR EMBL; BC145688; AAI45689.1; -; mRNA.
DR CCDS; CCDS21838.1; -. [Q8BX32-1]
DR RefSeq; NP_083696.2; NM_029420.4. [Q8BX32-1]
DR AlphaFoldDB; Q8BX32; -.
DR SMR; Q8BX32; -.
DR BioGRID; 217722; 1.
DR STRING; 10090.ENSMUSP00000118182; -.
DR PhosphoSitePlus; Q8BX32; -.
DR EPD; Q8BX32; -.
DR MaxQB; Q8BX32; -.
DR PaxDb; Q8BX32; -.
DR PeptideAtlas; Q8BX32; -.
DR PRIDE; Q8BX32; -.
DR ProteomicsDB; 261085; -. [Q8BX32-1]
DR ProteomicsDB; 261086; -. [Q8BX32-2]
DR DNASU; 75764; -.
DR Ensembl; ENSMUST00000144897; ENSMUSP00000118182; ENSMUSG00000059772. [Q8BX32-1]
DR GeneID; 75764; -.
DR KEGG; mmu:75764; -.
DR UCSC; uc009jsh.2; mouse. [Q8BX32-1]
DR CTD; 79008; -.
DR MGI; MGI:1915220; Slx1b.
DR VEuPathDB; HostDB:ENSMUSG00000059772; -.
DR eggNOG; KOG3005; Eukaryota.
DR GeneTree; ENSGT00390000013368; -.
DR HOGENOM; CLU_030739_0_0_1; -.
DR InParanoid; Q8BX32; -.
DR OMA; LQFEHAW; -.
DR PhylomeDB; Q8BX32; -.
DR TreeFam; TF352344; -.
DR Reactome; R-MMU-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
DR Reactome; R-MMU-6783310; Fanconi Anemia Pathway.
DR BioGRID-ORCS; 75764; 7 hits in 108 CRISPR screens.
DR ChiTaRS; Slx1b; mouse.
DR PRO; PR:Q8BX32; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8BX32; protein.
DR Bgee; ENSMUSG00000059772; Expressed in retinal neural layer and 102 other tissues.
DR ExpressionAtlas; Q8BX32; baseline and differential.
DR Genevisible; Q8BX32; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0033557; C:Slx1-Slx4 complex; ISO:MGI.
DR GO; GO:0017108; F:5'-flap endonuclease activity; ISO:MGI.
DR GO; GO:0008821; F:crossover junction endodeoxyribonuclease activity; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:1904431; P:positive regulation of t-circle formation; IMP:BHF-UCL.
DR GO; GO:0090656; P:t-circle formation; IMP:BHF-UCL.
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 Alternative splicing; DNA damage; DNA recombination; DNA repair;
KW Endonuclease; Hydrolase; Metal-binding; Nuclease; Nucleus;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..270
FT /note="Structure-specific endonuclease subunit SLX1"
FT /id="PRO_0000332121"
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"
FT VAR_SEQ 191..204
FT /note="DEEGPLCCPHPGCP -> VRAHRGGDLGLCPP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033332"
FT VAR_SEQ 205..270
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033333"
SQ SEQUENCE 270 AA; 30656 MW; B16DED3648168785 CRC64;
MDHAARPGRF FGVYLLYCQN PRHRGRVYVG FTVNPARRVR QHNAGRKKGG AWRTSGRGPW
DMVLIIHGFP SAVAALRFEW AWQHPQASRR LTHVGPRLRS EAAFAFHLRV LAHMLRVPPW
VRLPLTLRWL RPDFRHELCP APPAHMPIAF GPPPPQPLVP KRPAVSEADS ERQLDLGTKA
RCSLCARLLQ DEEGPLCCPH PGCPLRAHII CLAEEFLQEE PGQLLPLEGH CPSCKKSLLW
GNLVGQCHAD TEEEEDLELE EEHWTDLLET
