RESF1_MOUSE
ID RESF1_MOUSE Reviewed; 1521 AA.
AC Q5DTW7; Q5FWH0; Q7TNT1; Q8CCW3; Q8CCZ9; Q9CSA5; Q9CU82;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Retroelement silencing factor 1 {ECO:0000305};
GN Name=Resf1 {ECO:0000312|MGI:MGI:1914496}; Synonyms=Kiaa1551;
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] (ISOFORM 1).
RC TISSUE=Brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. the
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1173 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo, Head, and Medulla oblongata;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1109-1521 (ISOFORM 2), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1128-1521 (ISOFORM 1).
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-910, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, INTERACTION WITH SETDB1, AND SUBCELLULAR LOCATION.
RX PubMed=29728365; DOI=10.1101/gr.227280.117;
RA Fukuda K., Okuda A., Yusa K., Shinkai Y.;
RT "A CRISPR knockout screen identifies SETDB1-target retroelement silencing
RT factors in embryonic stem cells.";
RL Genome Res. 28:846-858(2018).
CC -!- FUNCTION: Plays a role in the regulation of imprinted gene expression,
CC regulates repressive epigenetic modifications associated with SETDB1.
CC Required for the recruitment or accumulation of SETDB1 to the
CC endogenous retroviruses (ERVs) and maintenance of repressive chromatin
CC configuration, contributing to a subset of the SETDB1-dependent ERV
CC silencing in embryonic stem cells. {ECO:0000269|PubMed:29728365}.
CC -!- SUBUNIT: Interacts with SETDB1. {ECO:0000269|PubMed:29728365}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29728365}.
CC Note=Localizes around gamma-tubulin during M phase.
CC {ECO:0000269|PubMed:29728365}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5DTW7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5DTW7-3; Sequence=VSP_026863;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH89381.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB28838.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC27639.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC27639.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAD90453.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK220403; BAD90453.1; ALT_INIT; mRNA.
DR EMBL; AK013408; BAB28838.1; ALT_FRAME; mRNA.
DR EMBL; AK017376; BAB30717.1; -; mRNA.
DR EMBL; AK031797; BAC27553.2; -; mRNA.
DR EMBL; AK031989; BAC27639.1; ALT_SEQ; mRNA.
DR EMBL; BC055761; AAH55761.1; -; mRNA.
DR EMBL; BC089381; AAH89381.1; ALT_FRAME; mRNA.
DR CCDS; CCDS20717.1; -. [Q5DTW7-1]
DR RefSeq; NP_001276590.1; NM_001289661.1. [Q5DTW7-1]
DR RefSeq; NP_001276591.1; NM_001289662.1. [Q5DTW7-1]
DR RefSeq; NP_080330.1; NM_026054.3. [Q5DTW7-1]
DR RefSeq; XP_006507144.1; XM_006507081.3. [Q5DTW7-1]
DR RefSeq; XP_006507146.1; XM_006507083.3. [Q5DTW7-1]
DR RefSeq; XP_006507147.1; XM_006507084.3. [Q5DTW7-1]
DR RefSeq; XP_011239924.1; XM_011241622.2. [Q5DTW7-1]
DR AlphaFoldDB; Q5DTW7; -.
DR BioGRID; 212044; 1.
DR IntAct; Q5DTW7; 1.
DR STRING; 10090.ENSMUSP00000041180; -.
DR iPTMnet; Q5DTW7; -.
DR PhosphoSitePlus; Q5DTW7; -.
DR jPOST; Q5DTW7; -.
DR MaxQB; Q5DTW7; -.
DR PaxDb; Q5DTW7; -.
DR PRIDE; Q5DTW7; -.
DR ProteomicsDB; 269158; -. [Q5DTW7-1]
DR ProteomicsDB; 269159; -. [Q5DTW7-3]
DR Antibodypedia; 2871; 27 antibodies from 11 providers.
DR DNASU; 67246; -.
DR Ensembl; ENSMUST00000046689; ENSMUSP00000041180; ENSMUSG00000032712. [Q5DTW7-1]
DR Ensembl; ENSMUST00000100765; ENSMUSP00000098328; ENSMUSG00000032712. [Q5DTW7-1]
DR Ensembl; ENSMUST00000189932; ENSMUSP00000140026; ENSMUSG00000032712. [Q5DTW7-1]
DR GeneID; 67246; -.
DR KEGG; mmu:67246; -.
DR UCSC; uc009eub.2; mouse. [Q5DTW7-1]
DR CTD; 55196; -.
DR MGI; MGI:1914496; Resf1.
DR VEuPathDB; HostDB:ENSMUSG00000032712; -.
DR eggNOG; ENOG502S9FU; Eukaryota.
DR GeneTree; ENSGT00390000018491; -.
DR HOGENOM; CLU_002739_0_0_1; -.
DR InParanoid; Q5DTW7; -.
DR OMA; MYMEKRS; -.
DR PhylomeDB; Q5DTW7; -.
DR TreeFam; TF336094; -.
DR BioGRID-ORCS; 67246; 4 hits in 71 CRISPR screens.
DR ChiTaRS; 2810474O19Rik; mouse.
DR PRO; PR:Q5DTW7; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q5DTW7; protein.
DR Bgee; ENSMUSG00000032712; Expressed in animal zygote and 250 other tissues.
DR ExpressionAtlas; Q5DTW7; baseline and differential.
DR Genevisible; Q5DTW7; MM.
DR GO; GO:0005634; C:nucleus; IMP:UniProtKB.
DR GO; GO:1990226; F:histone methyltransferase binding; IPI:UniProtKB.
DR GO; GO:0045869; P:negative regulation of single stranded viral RNA replication via double stranded DNA intermediate; IMP:UniProtKB.
DR GO; GO:0090309; P:positive regulation of DNA methylation-dependent heterochromatin assembly; IMP:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR InterPro; IPR027866; RESF1.
DR PANTHER; PTHR21604; PTHR21604; 2.
DR Pfam; PF15395; DUF4617; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..1521
FT /note="Retroelement silencing factor 1"
FT /id="PRO_0000295243"
FT REGION 621..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1093..1147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1204..1230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1312..1335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1425..1444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1457..1485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1093..1112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1126..1143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1466..1482
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 910
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 996
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCM1"
FT MOD_RES 1142
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCM1"
FT MOD_RES 1482
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCM1"
FT MOD_RES 1514
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCM1"
FT CROSSLNK 223
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9HCM1"
FT CROSSLNK 1411
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9HCM1"
FT VAR_SEQ 1440..1441
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026863"
FT CONFLICT 14
FT /note="P -> S (in Ref. 2; BAC27639)"
FT /evidence="ECO:0000305"
FT CONFLICT 23
FT /note="I -> N (in Ref. 2; BAC27639)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="Q -> R (in Ref. 2; BAC27639)"
FT /evidence="ECO:0000305"
FT CONFLICT 1444
FT /note="S -> L (in Ref. 3; AAH55761)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1521 AA; 169044 MW; 9E32F40A89DA62F1 CRC64;
MNWNTKQENV PKPPPYSKTQ SSILQHFLMT STTSQSSFNY SPHNQEASQT SFNYSLHNQE
ACMYSGNSNS VSQPLLSGRN YITPQTQISV SNMPTRTIVA SQSSMERVVS TNGKGPQQPN
HNLQTVSSGI MQNVWLPSHT EATISHNPDG GTNMPYMHPP QNQLVTSDTY SMQLQMAPLH
SGKVPMTHQG SQGLNHFIPD QLVDWTQYTS NELSYPEYRP PPKQYSYILP ATTSLQVKNN
QLPTYTQSLQ SKHSVPLSSH QYAAEASKRL SALPYSCRYE NQHVQNAQPV SKHLPMEVPQ
SSEVHSSEKK KDTYRGFKQQ WQNPNEKVSI GQFSEVKINI KQPYSESVRP SGDGVQALVQ
NNQEKRKYTY NPNTNQVIDT NATKEKLVRD IKSLVEIKKK FSELARKIKI NKSLLMAAGC
SKTANTSYTE PIQHSEFSAK EMSAKNGNDC SMELLATCLS LWKNQPSKTT EENVPKPLEE
KQCNTSRIST TVVGSANPTN EVHVKSLCSG VGNSQKMMSS SQTVLPVLIP SCESSGVAVG
KGTELQIAVV SPLVLSDTNT LPGKDSVPEV LPETLYPVVK EGSVCSLQTQ PTETVALPFD
VIGAVASNNI SAEIPLPVDK EKQHKPIQGD PDIADSSLGK HSPLGTEVLP KPMDSTIVSG
PMLQIESICS LAEGDVSYNS QIAEIFNSVQ TEPQKPSPNQ VIDSQQEQVY DTTENKDFSL
QKDKCVQCTD VPHEVPEQPE PLQPEEPASS EYVEANREAT EESCREYTGR KESTAKDVCL
PAAIQQDPHP RETDMFSKSD HSLPAINEIN DESEPISYLH DQLSELLKEF PYGIETFNRH
EVSLDQQKTH KIVENQTGGK TSNVSGDSTD QIKITVLNSE QIKELFPEDD QPCDKLAEPE
NKEIVAEVKS PCDSQIPREE SHDLGMLDPE KDKIHCCALG WLSMVYEGVP QCHCSSTEKK
EKDQCLDINS SKQGEQPCNS GITIFEINPV SNNSKTPLTQ ATEEGHFSAV HGEKTKASKT
KDNREGQELA CHFSAKCYKK DKKGNFKIRH DTSLKMEQKL KNISSKCDIP NPSKCNKIAA
PEILHVTTSN SAKNMPFSKQ ASQESLQKKH TSQDLGPVKA PIELSSNTDP CRSNTSSVQS
VSPEKKKLKF KAGGSRLKYF EKRKTDHVII PDVEIKKKKY EKQEQNKNAG DTLKLCSILT
ESNERASVQE KTVPSPESSD PKGSSSKSTR VITVQEYLQR QKDKQITGNN ASRNICVETV
LCDSGHTKTS KHSAAVSWGK LVEGQSISAE TAKELEHNSS SHGKDFKIHH SEASRTHSVS
NNNKGKFDGK QPDKMFKNKT SMNNESNQMP LQVKEQRKQY LNRVAFKCTE RESICLTKLD
SASKKLSIEK KSGEYTSKTK DTDKPSMLEF KLCPDVLLKN TSTVDKQDCP GPGPEKEQAP
VQVSGIKSTK EDWLKCIPTR TKMPESSQRD SADSRLSKRS LSADEFEILQ NPVKESNIMF
RTYKKMYLEK RSRSLGSSPV K
