SLF1_MOUSE
ID SLF1_MOUSE Reviewed; 1054 AA.
AC Q8R3P9; Q497V2; Q5XK30; Q8BHY5; Q8BQM6; Q921Y9;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 3.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=SMC5-SMC6 complex localization factor protein 1 {ECO:0000312|MGI:MGI:2145448};
DE AltName: Full=Ankyrin repeat domain-containing protein 32;
DE AltName: Full=BRCT domain-containing protein 1;
DE AltName: Full=Protein BRCTx {ECO:0000303|PubMed:15632077};
GN Name=Slf1 {ECO:0000312|MGI:MGI:2145448};
GN Synonyms=Ankrd32, Brctd1, Brctx {ECO:0000303|PubMed:15632077};
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 429-1054 (ISOFORM 1).
RC STRAIN=FVB/N-3;
RC TISSUE=Embryonic germ cell, Mammary gland, Mammary tumor, and Placenta;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-260 AND 853-1054 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Corpus striatum, and Liver;
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 [4]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=15632077; DOI=10.1128/mcb.25.2.779-788.2005;
RA Adams D.J., van der Weyden L., Gergely F.V., Arends M.J., Ng B.L.,
RA Tannahill D., Kanaar R., Markus A., Morris B.J., Bradley A.;
RT "BRCTx is a novel, highly conserved RAD18-interacting protein.";
RL Mol. Cell. Biol. 25:779-788(2005).
RN [5]
RP INTERACTION WITH RAD18, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=22036607; DOI=10.1016/j.dnarep.2011.10.012;
RA Liu T., Chen H., Kim H., Huen M.S., Chen J., Huang J.;
RT "RAD18-BRCTx interaction is required for efficient repair of UV-induced DNA
RT damage.";
RL DNA Repair 11:131-138(2012).
CC -!- FUNCTION: Plays a role in the DNA damage response (DDR) pathway by
CC regulating postreplication repair of UV-damaged DNA and genomic
CC stability maintenance. The SLF1-SLF2 complex acts to link RAD18 with
CC the SMC5-SMC6 complex at replication-coupled interstrand cross-links
CC (ICL) and DNA double-strand breaks (DSBs) sites on chromatin during DNA
CC repair in response to stalled replication forks. Promotes the
CC recruitment of SLF2 and the SMC5-SMC6 complex to DNA lesions.
CC {ECO:0000250|UniProtKB:Q9BQI6}.
CC -!- SUBUNIT: Interacts (via BRCT domains) with RAD18 (via C-terminus and
CC phosphorylated form); this interaction is required for efficient repair
CC of UV-induced DNA damage (PubMed:15632077, PubMed:22036607). Interacts
CC (via N-terminus) with SLF2; this interaction links RAD18 to the SMC5-
CC SMC6 complex. Interacts (via BRCT domains) with RAD18; this interaction
CC occurs in a SLF2-independent manner. Interacts with SMC6.
CC {ECO:0000250|UniProtKB:Q9BQI6, ECO:0000269|PubMed:15632077,
CC ECO:0000269|PubMed:22036607}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15632077,
CC ECO:0000269|PubMed:22036607}. Cytoplasm {ECO:0000269|PubMed:15632077}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:15632077}. Note=Relocalizes with RAD18 to nuclear
CC foci in response to DNA damage (PubMed:22036607). Colocalizes with
CC RAD18 in the nucleus and to centrosomes (PubMed:15632077). Associates
CC with chromatin. Accumulates with RAD18 and the SMC5-SMC6 complex at
CC replication-coupled DNA interstrand repair and DNA double-strand breaks
CC (DSBs) sites on chromatin in a ubiquitin-dependent manner.
CC {ECO:0000250|UniProtKB:Q9BQI6, ECO:0000269|PubMed:15632077,
CC ECO:0000269|PubMed:22036607}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8R3P9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R3P9-2; Sequence=VSP_034415, VSP_034416;
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:15632077). Expressed in
CC testis (PubMed:15632077). Expressed in spermatocytes (PubMed:15632077).
CC {ECO:0000269|PubMed:15632077}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the developing embryo
CC (PubMed:15632077). {ECO:0000269|PubMed:15632077}.
CC -!- DOMAIN: BRCT domains are necessary for its targeting to ionizing
CC radiation-induced nuclear foci (PubMed:22036607).
CC {ECO:0000269|PubMed:22036607}.
CC -!- DISRUPTION PHENOTYPE: Mice develop normally, display no pathological
CC abnormalities and are fertile (PubMed:15632077).
CC {ECO:0000269|PubMed:15632077}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH09101.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH24900.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH83095.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC122418; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC161266; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC009101; AAH09101.1; ALT_INIT; mRNA.
DR EMBL; BC024900; AAH24900.1; ALT_INIT; mRNA.
DR EMBL; BC083095; AAH83095.1; ALT_INIT; mRNA.
DR EMBL; BC100362; AAI00363.1; -; mRNA.
DR EMBL; AK047775; BAC33152.1; -; mRNA.
DR EMBL; AK050168; BAC34106.1; -; mRNA.
DR CCDS; CCDS26657.2; -. [Q8R3P9-1]
DR RefSeq; NP_598832.3; NM_134071.3. [Q8R3P9-1]
DR RefSeq; XP_017170840.1; XM_017315351.1. [Q8R3P9-1]
DR AlphaFoldDB; Q8R3P9; -.
DR SMR; Q8R3P9; -.
DR BioGRID; 222830; 4.
DR IntAct; Q8R3P9; 3.
DR STRING; 10090.ENSMUSP00000118312; -.
DR iPTMnet; Q8R3P9; -.
DR PhosphoSitePlus; Q8R3P9; -.
DR EPD; Q8R3P9; -.
DR MaxQB; Q8R3P9; -.
DR PaxDb; Q8R3P9; -.
DR PRIDE; Q8R3P9; -.
DR ProteomicsDB; 261076; -. [Q8R3P9-1]
DR ProteomicsDB; 261077; -. [Q8R3P9-2]
DR Antibodypedia; 24952; 140 antibodies from 20 providers.
DR DNASU; 105377; -.
DR Ensembl; ENSMUST00000151524; ENSMUSP00000118312; ENSMUSG00000021597. [Q8R3P9-1]
DR GeneID; 105377; -.
DR KEGG; mmu:105377; -.
DR UCSC; uc007rgs.2; mouse. [Q8R3P9-1]
DR UCSC; uc007rgv.2; mouse. [Q8R3P9-2]
DR CTD; 84250; -.
DR MGI; MGI:2145448; Slf1.
DR VEuPathDB; HostDB:ENSMUSG00000021597; -.
DR eggNOG; KOG0504; Eukaryota.
DR eggNOG; KOG1929; Eukaryota.
DR GeneTree; ENSGT00940000158953; -.
DR HOGENOM; CLU_010529_0_0_1; -.
DR InParanoid; Q8R3P9; -.
DR OMA; MLLEIFW; -.
DR OrthoDB; 1003628at2759; -.
DR PhylomeDB; Q8R3P9; -.
DR TreeFam; TF329705; -.
DR BioGRID-ORCS; 105377; 7 hits in 75 CRISPR screens.
DR PRO; PR:Q8R3P9; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q8R3P9; protein.
DR Bgee; ENSMUSG00000021597; Expressed in spermatocyte and 251 other tissues.
DR ExpressionAtlas; Q8R3P9; baseline and differential.
DR Genevisible; Q8R3P9; MM.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0042405; C:nuclear inclusion body; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0000786; C:nucleosome; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:2000781; P:positive regulation of double-strand break repair; ISS:UniProtKB.
DR GO; GO:0034184; P:positive regulation of maintenance of mitotic sister chromatid cohesion; ISS:UniProtKB.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISS:UniProtKB.
DR GO; GO:1990166; P:protein localization to site of double-strand break; ISS:UniProtKB.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 3.40.50.10190; -; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR042479; Slf1.
DR PANTHER; PTHR46677; PTHR46677; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF16770; RTT107_BRCT_5; 1.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00292; BRCT; 2.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; ANK repeat; Cytoplasm; Cytoskeleton; DNA damage;
KW DNA repair; Nucleus; Reference proteome; Repeat.
FT CHAIN 1..1054
FT /note="SMC5-SMC6 complex localization factor protein 1"
FT /id="PRO_0000243907"
FT DOMAIN 2..80
FT /note="BRCT 1"
FT DOMAIN 121..199
FT /note="BRCT 2"
FT REPEAT 802..832
FT /note="ANK 1"
FT REPEAT 836..865
FT /note="ANK 2"
FT REPEAT 870..900
FT /note="ANK 3"
FT REGION 283..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 242..250
FT /note="NKMENHNKN -> VKFCELEIL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034415"
FT VAR_SEQ 251..1054
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034416"
FT CONFLICT 711
FT /note="I -> V (in Ref. 2; AAH09101/AAH24900)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1054 AA; 121004 MW; 248B6D44E221D6CF CRC64;
MEDSATKHII QMTGFKMEEK EALVKLLLKL DCTFIKSEKY KNCTHLIAER LCKSEKFLAA
CAAGKWVLTK DYIIHSAKSG RWLDETTYEW GYKIEKDSHY SPQMQSAPKR WREELKRTGA
PGAFHRWKVV LLVRADKRSD SLVRVLEAGK ANVILPKNSP SGITHVIASN ARISAEREQE
NFKAPFYPIQ YLGDFLLEKE IQNDEHSQIS PAWTKYNNQE KGNDVGFPEM KGAGENMYRT
QNKMENHNKN VSDRFVLSEH HKKKFKDFRK DIRSVKKRNT LRRHGLENQK ETKKKDKNIQ
RSYILRKKNK KEGYCKTDDA HDTIRSMLKK RGHYREQKEM KNPLLTDGTK ESKTKDVKTN
MNLIEIKNAL KKQIYKDIYR AQAVRYNCIR VDKQPVYNVE VKNSEFPRGI LNLIENLIEG
QFFKEAIEEL SSLQAHYIPP VCLLHAILEN VLQDKIDTFS GRYFHILSAL LHLHPPWKSP
AMLKYYLELF QCPTCMKGAW DFTEVLIRSC LFNEDFCHQI SENISTKVVN LTLLKFFFNL
LEGEVRHLSQ KLCDWSDSQS LKVTEKAILH EIFWSGSETS GLLTKPVNML LEWTIYSHKE
KCKSNDVFKH ELSYLLTGIL GAAVDYWIFL GIQMGRNVIR HMSDDLGSYI SLSCDDFSSK
ELEIFICSFS SSWLQMFVAE AIFKKLCLQG PTSTCTEPLS LQKIIDSYLP ILGKMDIHGA
GKMQSPKKLC QRPCLESQRA LLMLNGAKRK QAEGRPELLE LNRAKCSSSL KKLKKKSEEL
SCSKENCPSL VTKMNFHKTN LKGETALHRV CIKNQVEKLI ILLSLPGIDI NVKDNAGWTP
LHEACNYGNT ECVQEILQRC PEVDLLTQVD GVTPLHDALS NGHVEIGKLL LQRGGPELLQ
QRNSKGELPL DYVLSPKDKE ELFAITNIDD TVDNFHAKTQ KHFYHQQLEF GSFLLSRMLI
NFCSIFDLSS EFILAFKGLG HLNELLMACN SDTEASNAHT DWLLDVYARN IKTLKKLPSV
LKELPENLNV CPGVHTEALL VTLKMMCQSI TELS
