SLF2_PONAB
ID SLF2_PONAB Reviewed; 1174 AA.
AC Q5REF4;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=SMC5-SMC6 complex localization factor protein 2 {ECO:0000250|UniProtKB:Q8IX21};
GN Name=SLF2 {ECO:0000250|UniProtKB:Q8IX21}; Synonyms=FAM178A;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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 the SMC5-SMC6 complex to DNA lesions.
CC {ECO:0000250|UniProtKB:Q8IX21}.
CC -!- SUBUNIT: Interacts with SLF1 (via N-terminus); this interaction links
CC RAD18 to the SMC5-SMC6 complex. Interacts with RAD18; this interaction
CC is increased in a SLF1-dependent manner. Interacts with SMC5 and SMC6.
CC {ECO:0000250|UniProtKB:Q8IX21}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8IX21}.
CC Note=Mainly localizes in the nucleus. Colocalizes with PCNA on
CC replication sites. Associates with chromatin. Accumulates with RAD18
CC and the SMC5-SMC6 complex at replication-coupled DNA interstrand repair
CC and DNA double-strand breaks (DSBs) sites on chromatin in a ubiquitin-
CC dependent manner. {ECO:0000250|UniProtKB:Q8IX21}.
CC -!- SIMILARITY: Belongs to the FAM178 family. {ECO:0000305}.
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DR EMBL; CR857575; CAH89853.1; -; mRNA.
DR RefSeq; NP_001124554.1; NM_001131082.1.
DR AlphaFoldDB; Q5REF4; -.
DR STRING; 9601.ENSPPYP00000002988; -.
DR Ensembl; ENSPPYT00000003092; ENSPPYP00000002988; ENSPPYG00000002573.
DR GeneID; 100127098; -.
DR KEGG; pon:100127098; -.
DR CTD; 55719; -.
DR eggNOG; ENOG502QW1I; Eukaryota.
DR GeneTree; ENSGT00530000064017; -.
DR InParanoid; Q5REF4; -.
DR Proteomes; UP000001595; Chromosome 10.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
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 InterPro; IPR044276; CANIN_dom.
DR InterPro; IPR026161; FAM178.
DR PANTHER; PTHR16046; PTHR16046; 1.
DR Pfam; PF14816; CANIN; 1.
PE 2: Evidence at transcript level;
KW DNA damage; DNA repair; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..1174
FT /note="SMC5-SMC6 complex localization factor protein 2"
FT /id="PRO_0000089780"
FT REGION 1..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..374
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..531
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..621
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IX21"
FT MOD_RES 604
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IX21"
FT MOD_RES 608
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IX21"
FT MOD_RES 615
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IX21"
SQ SEQUENCE 1174 AA; 132017 MW; 767D93C6FAFA25E0 CRC64;
MTRRCMPARP GFPSSPAPGS SPPRCHLRPG STAHAAAGKR TESPGDRKQS IIDFFKPASK
QGRHMLDSPQ KSNIKYGGSR LSITGTERFE RKLSSPKKSK TKRVPPEKSP IIEAFMKGVK
EHHEDHGIHE SCRPCVSLAS KYLAKGTNIY VPSSYHLAKE MKSLKKNHRS PERRKSLFIH
ENNEKNDRDR GKTNADSKKQ TTVAEADIFK NSSRSLSSRS SLSRHHPGES PLGAKFQLSL
ASYCRERELK RLRKEQMEQR INSENSFSEA SNLSLKSSSI ERKYKPRQEQ RKQNDVIPGK
NNLSNVENGH LSRKRSSSDS WEPTSAGSKQ NKFPEKRKRN SVDSDLKSTR ESMIPKARES
FLEKRPDGPH QKEKFIKHIA LKTPGDVLRL EDISKEPNDE TDCSSAGLAP SNSGSSGHHS
TRNSDQIRVA GTKETKMQKP HLPLSQEKSA IKKASNLQKN KTTSSMTKEK ETKLPLLSHV
PSAGSSLVPL NAKNCALPVS KKDKERSSSK ECSGHSTEST KHKEHKAKTN KADSNVSSGK
ISGGPLCSEY GAPTKSPPAA LEVVPCVPSP AAPSDKAPSE RESSGNSNAG SSALKRKLRG
DFDSDEESLG YNLDSDEEEE TLKSLEEIMA LNFNQTPATT GKPPALSKEL RSQSSDYTGH
DHPGTYTNTL ERLVKEMEDT QRLDELQKQL QEDIRQGRGI KSPIRIGEED STDDEDGLLE
EHKEFLKKFS VTIDAIPDHH PGEEIFNFLN SGKIFNQYTL DLRDSGFIGQ SAVEKLILKS
GKTDQIFLTT QGFLTSAYHY VQCPVPVLKW LFRMMSVHTD CIVSVQILST LMEITIRNDT
FSDSPVWPWI PSLSDVAAVF FNMGIDFRSL FPLENLQPDF NEDYLVSETQ TTSRGKESED
SSYKPIFSTL PETNILNVVK FLGLCTSIHP EGYQDREIML LILMLFKMSL EKQLKQIPLV
DFQSLLINLM KNIRDWNTKV PELCLGINEL SSHPHNLLWL VQLVPNWTSR GRQLRQCLSL
VIISKLLDEK HEDVPNASNL QVSVLHRYLV QMKPSDLLKK MVLKKKAEQP DGIIDDSLHL
ELEKQAYYLT YILLHLVGEV SCSHSFSSGQ RKHFVLLCGA LEKHVKCDIR EDARLFYRTK
VKDLVARIHG KWQEIIQNCR PTQGQLHDFW VPDS
