NRIF2_MOUSE
ID NRIF2_MOUSE Reviewed; 824 AA.
AC Q921B4; Q8BJF0; Q8K1Y8;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=Neurotrophin receptor-interacting factor 2;
DE AltName: Full=Zinc finger protein 369;
GN Name=Nrif2; Synonyms=Zfp369;
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 [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INTERACTION WITH NGFR.
RX PubMed=11750124; DOI=10.1016/s0378-1119(01)00730-2;
RA Benzel I., Barde Y.A., Casademunt E.;
RT "Strain-specific complementation between NRIF1 and NRIF2, two zinc finger
RT proteins sharing structural and biochemical properties.";
RL Gene 281:19-30(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-570 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Eye;
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).
CC -!- FUNCTION: Transcription regulator which may participate in
CC NGFR/p75(NTR)-mediated apoptosis. Probably acts as a transcription
CC repressor: specifically binds to the 3'-end of zinc-finger coding genes
CC and recruiting chromatin-modifying proteins such as SETDB1 and
CC TRIM28/KAP1, leading to transcription repression (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with NGFR/p75(NTR). {ECO:0000269|PubMed:11750124}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11750124}. Nucleus
CC {ECO:0000255|PROSITE-ProRule:PRU00187, ECO:0000269|PubMed:11750124}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q921B4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q921B4-2; Sequence=VSP_040912, VSP_040913;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:11750124}.
CC -!- MISCELLANEOUS: Up-regulated in Nrif1 mutant mice in the 129/Sv
CC background, possibly complementating for the absence of Nrif1 and
CC explaining why Nrif1 mutant mice are viable in a 129/Sv background,
CC whilke they are lethal in other backgrounds.
CC {ECO:0000305|PubMed:11750124}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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; AJ319726; CAC41280.1; -; mRNA.
DR EMBL; BC036565; AAH36565.1; -; mRNA.
DR EMBL; AK084309; BAC39159.1; -; mRNA.
DR AlphaFoldDB; Q921B4; -.
DR SMR; Q921B4; -.
DR STRING; 10090.ENSMUSP00000119114; -.
DR iPTMnet; Q921B4; -.
DR PhosphoSitePlus; Q921B4; -.
DR PaxDb; Q921B4; -.
DR PRIDE; Q921B4; -.
DR MGI; MGI:2176229; Zfp369.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; Q921B4; -.
DR PhylomeDB; Q921B4; -.
DR PRO; PR:Q921B4; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q921B4; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISO:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005166; F:neurotrophin p75 receptor binding; IPI:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0051726; P:regulation of cell cycle; IDA:MGI.
DR GO; GO:1900112; P:regulation of histone H3-K9 trimethylation; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd07765; KRAB_A-box; 2.
DR CDD; cd07936; SCAN; 1.
DR Gene3D; 1.10.4020.10; -; 1.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR003309; SCAN_dom.
DR InterPro; IPR038269; SCAN_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 2.
DR Pfam; PF02023; SCAN; 1.
DR Pfam; PF00096; zf-C2H2; 4.
DR SMART; SM00349; KRAB; 2.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF109640; SSF109640; 2.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS50805; KRAB; 2.
DR PROSITE; PS50804; SCAN_BOX; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Cytoplasm; DNA-binding; Isopeptide bond;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..824
FT /note="Neurotrophin receptor-interacting factor 2"
FT /id="PRO_0000406967"
FT DOMAIN 14..85
FT /note="KRAB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT DOMAIN 161..243
FT /note="SCAN box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT DOMAIN 279..359
FT /note="KRAB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 680..702
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 708..730
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 736..758
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 764..786
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 792..814
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 137..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 15
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q923B3"
FT VAR_SEQ 319..361
FT /note="GWEPTLGNRELTPDSPIPVVKPIHDPNPKDLSRNRTQSTLFES -> ALGQV
FT HVEDGGAGPNRNGSQPLVRRSSFIPLPAGTRPSAILWS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040912"
FT VAR_SEQ 362..824
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040913"
FT CONFLICT 42
FT /note="I -> V (in Ref. 3; BAC39159)"
FT /evidence="ECO:0000305"
FT CONFLICT 491
FT /note="T -> A (in Ref. 3; BAC39159)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 824 AA; 93244 MW; 2BC3BAF6FAF233DB CRC64;
MASTLPTTWP HESVKFEDVS LRFTEEEWAL LDRQQKCLYR EIMMENLNNM ISVEHHFSKA
NVMPQLEEVE DCWPMQREIP QDTLPECSGH SLDPEMNSFP AESPLMKIKV VEVLTLNKDM
AGPRNALIQS LYPESGEDLN PGNLKPAQQP SKHLTDTEAS RQKFRHFQYE ESAGPQKSVS
QLRKLCHQWL QPSTRSKKQI LELLVLEQFL NALPEKLRVW VESQHPEDCK AVVALLENMT
SVSKDDAWLA CSSEATDELK EKRKDVATLP VTVPPEAPVT FQDVAVDFSQ EEWQLLGPMQ
RTKYHDVMLE TLGNLVSVGW EPTLGNRELT PDSPIPVVKP IHDPNPKDLS RNRTQSTLFE
SISPDEVQGR HTIESNPVGL LQEKGHPQQK LSESSKSQNQ TCIDKSQCSL NEVLPRNHVK
VKQKGTGKGK GRTNTISMTG GLRIRNQQKD SVEWRDRSGS TPVTHGSSIK NQQLGSEQGK
TQTSRDPITL TVPAEFYQEA TGSEEGRFRN SSNAMAADAP PKIHQKGPEW HKAGKSNNSM
LQGSSAQNHQ MGSRAGRARD NSILTHVKIH QKGYKEGKIQ GNNNYLKHVK PHRKGSKEER
LRELSTCQKH VPYVKQHLKT SGRGKGRKIN ASIKCGPYIK TYYRGSDVGR LRRANNCRKA
ISRHAQQISF IKIHKGSQVC QCSECGKMFR NARYFSVHKK IHTGERPYMC MSCGKAFVQS
SSLTQHLRIH SGERPFECSE CGRTFSDRSA ASQHLRTHTG AKPYQCQHCG KAFRQSSHLT
RHVRIHTGER PYVCTKCGKA FTQSSNLIGH QKTHRKKFKK QPKL
