SLF1_BOVIN
ID SLF1_BOVIN Reviewed; 1055 AA.
AC A6QR20;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=SMC5-SMC6 complex localization factor protein 1 {ECO:0000250|UniProtKB:Q9BQI6};
DE AltName: Full=Ankyrin repeat domain-containing protein 32;
DE AltName: Full=BRCT domain-containing protein 1;
GN Name=SLF1 {ECO:0000250|UniProtKB:Q9BQI6}; Synonyms=ANKRD32, BRCTD1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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 N-terminus) with SLF2; this interaction links
CC RAD18 to the SMC5-SMC6 complex. Interacts (via BRCT domains) with
CC RAD18; this interaction occurs in a SLF2-independent manner. Interacts
CC with SMC6. 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. {ECO:0000250|UniProtKB:Q8R3P9,
CC ECO:0000250|UniProtKB:Q9BQI6}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BQI6}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8R3P9}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q8R3P9}.
CC Note=Relocalizes with RAD18 to nuclear foci in response to DNA damage.
CC Colocalizes with RAD18 in the nucleus and to centrosomes. 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:Q8R3P9, ECO:0000250|UniProtKB:Q9BQI6}.
CC -!- DOMAIN: BRCT domains are necessary for its targeting to ionizing
CC radiation-induced nuclear foci. {ECO:0000250|UniProtKB:Q8R3P9}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI50080.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC150079; AAI50080.1; ALT_INIT; mRNA.
DR RefSeq; NP_001095528.2; NM_001102058.2.
DR AlphaFoldDB; A6QR20; -.
DR SMR; A6QR20; -.
DR STRING; 9913.ENSBTAP00000008026; -.
DR PaxDb; A6QR20; -.
DR PRIDE; A6QR20; -.
DR Ensembl; ENSBTAT00000008026; ENSBTAP00000008026; ENSBTAG00000006107.
DR GeneID; 520250; -.
DR KEGG; bta:520250; -.
DR CTD; 84250; -.
DR VEuPathDB; HostDB:ENSBTAG00000006107; -.
DR VGNC; VGNC:52883; SLF1.
DR eggNOG; KOG0504; Eukaryota.
DR eggNOG; KOG1929; Eukaryota.
DR GeneTree; ENSGT00940000158953; -.
DR InParanoid; A6QR20; -.
DR OMA; MLLEIFW; -.
DR OrthoDB; 1003628at2759; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000006107; Expressed in semen and 107 other tissues.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042405; C:nuclear inclusion body; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0000786; C:nucleosome; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS: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; 2.
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 2: Evidence at transcript level;
KW ANK repeat; Cytoplasm; Cytoskeleton; DNA damage; DNA repair;
KW Isopeptide bond; Nucleus; Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..1055
FT /note="SMC5-SMC6 complex localization factor protein 1"
FT /id="PRO_0000342340"
FT DOMAIN 2..80
FT /note="BRCT 1"
FT DOMAIN 121..199
FT /note="BRCT 2"
FT REPEAT 804..834
FT /note="ANK 1"
FT REPEAT 838..867
FT /note="ANK 2"
FT REPEAT 872..901
FT /note="ANK 3"
FT REGION 312..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 929
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BQI6"
SQ SEQUENCE 1055 AA; 121017 MW; 7ED68E2FC51953E9 CRC64;
MEDDAPKHII QMTGFKVEEK EALGKLLLKL DCTFIKSEKY KNCTHLIAER LCKSEKFLAA
CAAGKWVLTK DYIIHSAQSG RWLDETTYEW GYKIEKDSHY SPQMQSAPKR WREELKRTGA
PGAFHKWKVV LLVRADKRSD SLVRVLEAGK ANVILPKNSP TGITHVIASN ARIKAEQEKD
DFKAPFYPIQ YLEDFLLEKE IHNDEDSQTN STWKNHSSQE KSNDFRENMG FLEMKGTLKE
TMCRTQKEMK NHDEDVTISS ILTEHQSKER FRDSRKNLKF VKMRNALGRH TYRNQEMKKK
DEDIQSIYTL RKKRKKEKER DSRKDIEHDR STLRKHIYRD QKERKNSVFA GHAKESKTKD
IRTNVDIVDL KNALRKHIYR AQAVRYRGIR IDKQPAYNVE VKNAEFPRGI LNLIESLIEG
QFFKEAIEEL SSLQAHYIPP VYLLHALLEN ILQDNIDTFS GRYFHILSAL LHLHPPWKSP
AMSTYYLELF QCPTCMKGTW SLIEVLIRSC LFNESFCHQI SENIIGSKVL HLTLLKFFFN
LIESEVRHLS QKLYDWSDSQ SLKITGKAVL LEIFWSGNET SGLLTKPVNM LLEWTIYSHK
EKCKSNDVFR HELAYLLTGI LGAAIDYWIV LGLNMGRNVM RHMSDDVGSY VSLSCDDFSS
QDLEIFISSF SSSWLQMFVA EAVFKKLCLQ NSISISSEPL SLQKMVYSYL PALGKTGVRG
TRKMQKPKKI GLRPCFESQR ALIMLNGAKQ KQGEGLPEIP ELNLAKCSSS LKRLKKKSEG
ELSCSKENCP SLVTKINFHK TNLKGETALH RACINNQVDR LILLLSMPGI DINVKDNAGW
TPLHEACNYG NTVCVQEILQ RCPEVDLLTQ VDGVTPLHDA LSNGHVEIGK LLLQHGGPVL
LQQRNSKGEL PLDYVVSSQI KEELFAITKI EDTVENFHAQ AEKHFYHQQL EFGSFLLSRM
LLNFCSIFGL SSESLAFKGL THLSELLIAC QNYKETTSVH TDWLLDLYAR NIMTLQKLPN
ALKELPENVK VCPGVHTEAL LVTLEVMCRS VTEIS
