SLF2_MOUSE
ID SLF2_MOUSE Reviewed; 1278 AA.
AC Q6P9P0; Q8C041; Q8C0J5;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=SMC5-SMC6 complex localization factor protein 2 {ECO:0000250|UniProtKB:Q8IX21};
GN Name=Slf2 {ECO:0000250|UniProtKB:Q8IX21}; Synonyms=Fam178a;
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] OF 614-1273.
RC STRAIN=C57BL/6J; TISSUE=Olfactory bulb, and Thymus;
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] OF 761-1273.
RC STRAIN=C57BL/6J; 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 CONCEPTUAL TRANSLATION.
RA Blatter M.-C.;
RL Unpublished observations (JUL-2005).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC27192.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK030951; BAC27192.1; ALT_INIT; mRNA.
DR EMBL; AK032405; BAC27854.1; -; mRNA.
DR EMBL; BC060679; AAH60679.1; -; mRNA.
DR EMBL; AK031688; -; NOT_ANNOTATED_CDS; Transcribed_RNA.
DR RefSeq; XP_017173653.1; XM_017318164.1.
DR AlphaFoldDB; Q6P9P0; -.
DR BioGRID; 230481; 1.
DR STRING; 10090.ENSMUSP00000093758; -.
DR iPTMnet; Q6P9P0; -.
DR PhosphoSitePlus; Q6P9P0; -.
DR jPOST; Q6P9P0; -.
DR MaxQB; Q6P9P0; -.
DR PaxDb; Q6P9P0; -.
DR PRIDE; Q6P9P0; -.
DR ProteomicsDB; 261078; -.
DR MGI; MGI:1924968; Slf2.
DR eggNOG; ENOG502QW1I; Eukaryota.
DR InParanoid; Q6P9P0; -.
DR BioGRID-ORCS; 226151; 4 hits in 109 CRISPR screens.
DR ChiTaRS; Fam178a; mouse.
DR PRO; PR:Q6P9P0; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q6P9P0; protein.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS: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; ISO:MGI.
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..1278
FT /note="SMC5-SMC6 complex localization factor protein 2"
FT /id="PRO_0000089779"
FT REGION 1..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 798..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..227
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 282..296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..491
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..640
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..697
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 591
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IX21"
FT MOD_RES 708
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IX21"
FT MOD_RES 712
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IX21"
FT MOD_RES 719
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IX21"
FT CONFLICT 761..762
FT /note="MK -> YM (in Ref. 1; BAC27192)"
FT /evidence="ECO:0000305"
FT CONFLICT 788
FT /note="D -> H (in Ref. 1; BAC27854)"
FT /evidence="ECO:0000305"
FT CONFLICT 945
FT /note="F -> I (in Ref. 1; BAC27854)"
FT /evidence="ECO:0000305"
FT CONFLICT 1096
FT /note="S -> G (in Ref. 1; BAC27192)"
FT /evidence="ECO:0000305"
FT CONFLICT 1139
FT /note="P -> T (in Ref. 1; BAC27854)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1278 AA; 143970 MW; 74A2B84B7A0C3E07 CRC64;
MTRRCMPARP GFPSSPAPGS SPPRCHLRPG STAPAAAGKR TESPGDRKQS IIDFFKPAAK
QDKHMLDSPQ KSNIKYRGNG LSITGTEQFE RKLSSPKKLK PKRMSSEESP ILEAFMKGGK
EHHKDRGVHE SRRPCMSLSK YLPKGAGIYA PSSYRLPKEI KAQKKKHQSP ERRKSLFIHE
SNREKNDRDR GKNSEDSRKQ ATATEGDIFK HSSRSISSRS SLSRHHPGES TLGARFQLSL
ASYWREREQK KLRKEQMEQR INSENSFSEA SNLSLKSSGV GKNCKPRHEH SKHTEAVPGK
SNLSTLENGH LSRKRSSSDS WELSGSKQNK FSDKRTEELC GLRPEKHKRT YHTKSKRVLS
REAPRHIPSE RKVYQTHCTE DSWWCSALGR HSQGAGKTVS RGMSIASTLR LYLGRVISQL
WKMDISQEKD HLQTRGNFQA LNRINSPTKE QRNSVDSDLK STKEPIIPKA RESFLEKRPD
TSHQREKFIR HIALKTPGGV LRLEDIAKEP EDETDRSSAD SAPSNAGHHS SRNSDQVHSA
STKETKIQKP HLPLPQEKST IKRASNLQKN KPAGSVTSKE TKLPLLSHVP SAVSSRVPLN
AKNCTLPVPK KDKERSSSKE RSGHSTESSK HKEHRAKTIK AVSNESSGKN SGGSLHSEYA
PPTASPPAAL EVVPSVPSPA APSDKESSGN SNAGSNALKR KFRGDFDSDE ESLGYTLESD
EEEETLKSLE EIMALNFSRT PTTSGKPPAV SKGLRSQSSD MKEYAQSGTY TNTLERLVKE
MEDTQRLDEL QKKLQEDIRQ GRGIKSPLRT GDQDSTDDGD GLLEEHREFL KKFSVTVDAI
PDHHPGEEIF NFLNSGKIFN QYTLDLRDSG FIGESAVEKL ILKSGKTDQI FLTTQGFLTT
AYHYVQCPVP VLKWLFRMMS VHTDCIVSVQ ILSTLMEITI RNDTFSDSPV WPWIPSLSDI
AAVFFNMGVG FGSLFPLETL QPDFNEENLI SETQKTLGGK ESEDSPYSPV FSALPETNIL
NVVKFLGLCT SIHPEGYQDG ELMLLILMLF KMSLEKELKQ IPLVDFQSLL INLMKNIRDW
NTKVHELCLG INELSSHPHN LLWLVQLVPN WTSRGRQLRQ CLSLVMMSKL LDEKHEDIPN
ANNLQISVLH RYLVQMKPSD LLKKMVLKKR AEQPNETIDD SLHLELEKQA YYLTYILLHL
VGEVSCSHSL SSGQRKHFVL LCGALEKHVK CDIREDARLF YRTKVKDLVA RIHGKWQEII
QNCRPTQGQL HDFWVPDS
