IFFO1_MOUSE
ID IFFO1_MOUSE Reviewed; 562 AA.
AC Q8BXL9; Q3TQI1; Q6PFE6; Q8BXS3; Q8C1D6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Non-homologous end joining factor IFFO1 {ECO:0000303|PubMed:31548606};
DE Short=NHEJ factor IFFO1 {ECO:0000303|PubMed:31548606};
DE AltName: Full=Intermediate filament family orphan 1 {ECO:0000303|PubMed:31548606};
GN Name=Iffo1 {ECO:0000312|MGI:MGI:2444516}; Synonyms=Iffo;
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] (ISOFORMS 1; 2; 3 AND 6).
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, Head, and Retina;
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] (ISOFORM 4).
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 FUNCTION.
RX PubMed=31548606; DOI=10.1038/s41556-019-0388-0;
RA Li W., Bai X., Li J., Zhao Y., Liu J., Zhao H., Liu L., Ding M., Wang Q.,
RA Shi F.Y., Hou M., Ji J., Gao G., Guo R., Sun Y., Liu Y., Xu D.;
RT "The nucleoskeleton protein IFFO1 immobilizes broken DNA and suppresses
RT chromosome translocation during tumorigenesis.";
RL Nat. Cell Biol. 21:1273-1285(2019).
CC -!- FUNCTION: Nuclear matrix protein involved in the immobilization of
CC broken DNA ends and the suppression of chromosome translocation during
CC DNA double-strand breaks (DSBs) (PubMed:31548606). Interacts with the
CC nuclear lamina component LMNA, resulting in the formation of a
CC nucleoskeleton that will relocalize to the DSB sites in a XRCC4-
CC dependent manner and promote the immobilization of the broken ends,
CC thereby preventing chromosome translocation (PubMed:31548606). Acts as
CC a scaffold that allows the DNA repair protein XRCC4 and LMNA to
CC assemble into a complex at the DSB sites (PubMed:31548606).
CC {ECO:0000269|PubMed:31548606}.
CC -!- SUBUNIT: Forms a heterotetramer with XRCC4 (By similarity). The
CC interaction with XRCC4 is direct, involves LIG4-free XRCC4 and leads to
CC relocalization of IFFO1 at the double-strand break (DSB) sites (By
CC similarity). Interacts with LMNA; the interaction forms an interior
CC nucleoskeleton and the recruitment to DNA double-strand breaks (By
CC similarity). {ECO:0000250|UniProtKB:Q0D2I5}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q0D2I5}. Nucleus,
CC nucleoplasm {ECO:0000250|UniProtKB:Q0D2I5}. Nucleus inner membrane
CC {ECO:0000250|UniProtKB:Q0D2I5}. Nucleus matrix
CC {ECO:0000250|UniProtKB:Q0D2I5}. Note=Mainly soluble, the remaining is
CC localized in the nuclear matrix. Localized at double-strand break (DSB)
CC sites near the lamina and nuclear matrix structures.
CC {ECO:0000250|UniProtKB:Q0D2I5}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q8BXL9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BXL9-2; Sequence=VSP_030786;
CC Name=3;
CC IsoId=Q8BXL9-3; Sequence=VSP_030785, VSP_030787;
CC Name=4;
CC IsoId=Q8BXL9-4; Sequence=VSP_030785, VSP_030788;
CC Name=5;
CC IsoId=Q8BXL9-5; Sequence=VSP_030787;
CC Name=6;
CC IsoId=Q8BXL9-6; Sequence=VSP_030788;
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK028273; BAC25852.1; -; mRNA.
DR EMBL; AK044382; BAC31894.1; -; mRNA.
DR EMBL; AK044728; BAC32053.1; -; mRNA.
DR EMBL; AK163571; BAE37401.1; -; mRNA.
DR EMBL; BC057601; AAH57601.2; -; mRNA.
DR CCDS; CCDS39634.1; -. [Q8BXL9-1]
DR CCDS; CCDS39635.1; -. [Q8BXL9-5]
DR RefSeq; NP_001034758.1; NM_001039669.3. [Q8BXL9-1]
DR RefSeq; NP_001289707.1; NM_001302778.1.
DR RefSeq; NP_001289708.1; NM_001302779.1.
DR RefSeq; NP_848902.4; NM_178787.6. [Q8BXL9-5]
DR AlphaFoldDB; Q8BXL9; -.
DR SMR; Q8BXL9; -.
DR BioGRID; 236208; 9.
DR STRING; 10090.ENSMUSP00000056373; -.
DR iPTMnet; Q8BXL9; -.
DR PhosphoSitePlus; Q8BXL9; -.
DR MaxQB; Q8BXL9; -.
DR PaxDb; Q8BXL9; -.
DR PRIDE; Q8BXL9; -.
DR ProteomicsDB; 267266; -. [Q8BXL9-1]
DR ProteomicsDB; 267267; -. [Q8BXL9-2]
DR ProteomicsDB; 267268; -. [Q8BXL9-3]
DR ProteomicsDB; 267269; -. [Q8BXL9-4]
DR ProteomicsDB; 267270; -. [Q8BXL9-5]
DR ProteomicsDB; 267271; -. [Q8BXL9-6]
DR Antibodypedia; 22511; 65 antibodies from 17 providers.
DR DNASU; 320678; -.
DR Ensembl; ENSMUST00000117675; ENSMUSP00000113088; ENSMUSG00000038271. [Q8BXL9-1]
DR Ensembl; ENSMUST00000119527; ENSMUSP00000113376; ENSMUSG00000038271. [Q8BXL9-5]
DR GeneID; 320678; -.
DR KEGG; mmu:320678; -.
DR UCSC; uc009dto.2; mouse. [Q8BXL9-1]
DR UCSC; uc009dtp.2; mouse. [Q8BXL9-5]
DR UCSC; uc009dtq.2; mouse. [Q8BXL9-6]
DR CTD; 25900; -.
DR MGI; MGI:2444516; Iffo1.
DR VEuPathDB; HostDB:ENSMUSG00000038271; -.
DR eggNOG; ENOG502QRD7; Eukaryota.
DR GeneTree; ENSGT00510000046803; -.
DR HOGENOM; CLU_039629_2_1_1; -.
DR InParanoid; Q8BXL9; -.
DR OMA; NQMGSHS; -.
DR OrthoDB; 792412at2759; -.
DR PhylomeDB; Q8BXL9; -.
DR TreeFam; TF331217; -.
DR BioGRID-ORCS; 320678; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Iffo1; mouse.
DR PRO; PR:Q8BXL9; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8BXL9; protein.
DR Bgee; ENSMUSG00000038271; Expressed in retinal neural layer and 214 other tissues.
DR ExpressionAtlas; Q8BXL9; baseline and differential.
DR Genevisible; Q8BXL9; MM.
DR GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016363; C:nuclear matrix; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; ISO:MGI.
DR GO; GO:1990683; P:DNA double-strand break attachment to nuclear envelope; ISS:UniProtKB.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; ISS:UniProtKB.
DR GO; GO:1990166; P:protein localization to site of double-strand break; ISO:MGI.
DR InterPro; IPR039008; IF_rod_dom.
DR SMART; SM01391; Filament; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Coiled coil; Intermediate filament; Membrane;
KW Nucleus; Reference proteome.
FT CHAIN 1..562
FT /note="Non-homologous end joining factor IFFO1"
FT /id="PRO_0000316795"
FT DOMAIN 73..529
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 65..116
FT /note="LMNA binding"
FT /evidence="ECO:0000250|UniProtKB:Q0D2I5"
FT REGION 154..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..528
FT /note="XCCR4 binding. Required for localization to the
FT double-strand breaks (DSBs)"
FT /evidence="ECO:0000250|UniProtKB:Q0D2I5"
FT REGION 523..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 85..117
FT /evidence="ECO:0000255"
FT COILED 237..301
FT /evidence="ECO:0000255"
FT COILED 458..504
FT /evidence="ECO:0000255"
FT COMPBIAS 163..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..392
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..562
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..191
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_030785"
FT VAR_SEQ 259..562
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030786"
FT VAR_SEQ 358..360
FT /note="Missing (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030787"
FT VAR_SEQ 358
FT /note="Missing (in isoform 4 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_030788"
FT CONFLICT 291
FT /note="A -> P (in Ref. 1; BAC25852)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="C -> W (in Ref. 1; BAC25852)"
FT /evidence="ECO:0000305"
FT CONFLICT 345
FT /note="Q -> H (in Ref. 1; BAC25852)"
FT /evidence="ECO:0000305"
FT CONFLICT 454
FT /note="Q -> QQ (in Ref. 1; BAC25852 and 2; AAH57601)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 562 AA; 62415 MW; 4310CC2DEAC8B604 CRC64;
MNPLFGPNLF LLQQEQQGLA GPLGDPLGGD HFAGGGDLAS APLASAGPSA YSPPGPGPAP
PAAMALRNDL GSNINVLKTL NLRFRCFLAK VHELERRNRL LEKQLQQALE EGKQGRRGLA
RRDQAVQTGF ISPIRPLGLP LSSRPAAVCP PSARVLGSPS RSPAGPLASS AACHTSSSTS
TSTAFSSSTR FMPGTIWSFS HARRLGPGLE PTLVQGPGLS WVHPDGVGVQ IDTITPEIRA
LYNVLAKVKR ERDEYKRRWE EEYTVRIQLQ ERVTELQEEA QEADACQEEL AMKVEQLKAE
LVVFKGLMSN NLTELDTKIQ EKAMKVDMDI CRRIDITAKL CDLAQQRNCE DMIQMFQKKL
VPSMGGRKRE RKAAVEEDTS LSESDGPRQP EGAEEESTAL SINEEMQRML SQLREYDFED
DCDSLTWEET EETLLLWEDF SGYAMAAAEA QGEQEDSLEK VIKDTESLFK TREKEYQETI
DQIELELATA KNDMNRHLHE YMEMCSMKRG LDVQMETCRR LITQSGDRKS PAFTAVPLSD
PPPPPSETED SDRDVSSDSS MR
