ID   NRIF1_RAT               Reviewed;         822 AA.
AC   Q4V8E9;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Neurotrophin receptor-interacting factor 1;
DE   AltName: Full=Zinc finger protein 110;
GN   Name=Nrif1; Synonyms=Zfp110;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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).
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:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nucleolus
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; BC097420; AAH97420.1; -; mRNA.
DR   RefSeq; NP_001019946.1; NM_001024775.1.
DR   RefSeq; XP_006228174.1; XM_006228112.3.
DR   AlphaFoldDB; Q4V8E9; -.
DR   SMR; Q4V8E9; -.
DR   BioGRID; 258978; 2.
DR   STRING; 10116.ENSRNOP00000026298; -.
DR   iPTMnet; Q4V8E9; -.
DR   PhosphoSitePlus; Q4V8E9; -.
DR   PaxDb; Q4V8E9; -.
DR   PRIDE; Q4V8E9; -.
DR   GeneID; 308362; -.
DR   KEGG; rno:308362; -.
DR   UCSC; RGD:1306339; rat.
DR   CTD; 65020; -.
DR   RGD; 1306339; Zfp110.
DR   VEuPathDB; HostDB:ENSRNOG00000031328; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   HOGENOM; CLU_002678_49_6_1; -.
DR   InParanoid; Q4V8E9; -.
DR   OMA; VEDATWI; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; Q4V8E9; -.
DR   TreeFam; TF338018; -.
DR   Reactome; R-RNO-212436; Generic Transcription Pathway.
DR   PRO; PR:Q4V8E9; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000031328; Expressed in liver and 20 other tissues.
DR   Genevisible; Q4V8E9; RN.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0003682; F:chromatin binding; ISO:RGD.
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; ISO:RGD.
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; ISO:RGD.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR   GO; GO:0097191; P:extrinsic apoptotic signaling pathway; ISO:RGD.
DR   GO; GO:0051402; P:neuron apoptotic process; ISO:RGD.
DR   GO; GO:1900112; P:regulation of histone H3-K9 trimethylation; ISO:RGD.
DR   GO; GO:0046328; P:regulation of JNK cascade; ISO:RGD.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:1990009; P:retinal cell apoptotic process; ISO:RGD.
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   2: Evidence at transcript level;
KW   Apoptosis; Cytoplasm; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW   Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..822
FT                   /note="Neurotrophin receptor-interacting factor 1"
FT                   /id="PRO_0000406968"
FT   DOMAIN          14..85
FT                   /note="KRAB 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT   DOMAIN          160..242
FT                   /note="SCAN box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT   DOMAIN          278..358
FT                   /note="KRAB 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT   ZN_FING         678..700
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         706..728
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         734..756
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         762..784
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         790..812
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          376..481
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          499..550
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        393..407
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        452..477
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        530..550
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"
SQ   SEQUENCE   822 AA;  93628 MW;  39E804A3EEE30FE4 CRC64;
     MASTLPTTWP HESVKFEDVS LTFTKEEWAQ LDLQQKCLYR EIMMENYNNM ISVEHHFSKP
     NVISQLEEAE DCWPMEREIR QDILPECSGP SLDPGMNSFP AESPLMKIKV VEVLTLNKDV
     AGPRNALIQS LYPESRENLN PGNLKPAKPS KRLTDTEALR QKFRHFQYEE SAGPQKAVSR
     LRKLCHQWLQ PNIRSKKQII ELLVFEQFLS ALPEKFRVWL ESQHPEDCRA AVALLENMTS
     VTKDDAQLVC SSEATDQLKE KRKDVATLPV TVPPEEPVTF QDVAVGFSQE EWRLLGPVQR
     TEYHDVMLET LGNLVSVGWE PTLENRAISP DSPIPVVKPI HDPNPKDLSR NGIQSTVFEI
     ISQDRVQEIH TIESNQAGLL QEKSHPQKKL SESSKSQEGT NLHKSQGSLD EVPPRKHVKV
     KQKGTRKGKD RKNTISMTRG LRIRNQQKDS VEWQGRGDSN PMTHGYSIKN QRGSEQGTAG
     ARRDPITLTV SAQFYQKATG SEEGRFRDNS NAIVPDTPTK IHQKSPEWHK VGRSNNSMSS
     VQNDQMGSGA GRGRDNTILT HALPVKIHQK GYEEGKVQGN RNSLRHVKAH QKGSKGERVR
     ELSTSEKHVP YIKNHLKTSE REKGRENNDS IKYGPYIKTC YRGSEVRKLR RANNCTKAIS
     RHAQQIFFIK IHKGSQVCRC SECGKMFRNS RYFSVHKKIH TGERPYMCMA CGKAFVQSSS
     LTQHLRIHSG ERPFECSECG RTFNDRSAIS QHLRTHTGAK PYHCQHCGKA FRQSSHLTRH
     ERTHTGERPY VCSNCGKAFT QSSHLIGHQK THRIKFKKQP KL