ZN394_RAT
ID ZN394_RAT Reviewed; 536 AA.
AC Q9Z2K3;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Zinc finger protein 394;
DE AltName: Full=RLZF-Y;
DE AltName: Full=Zinc finger protein 94;
DE Short=Zfp-94;
DE AltName: Full=Zinc finger protein Y1;
GN Name=Znf394; Synonyms=Rlzfy, Zfp394, Zfp94, Zfp99;
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 [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Lung;
RX PubMed=9804994; DOI=10.1016/s0167-4781(98)00167-5;
RA Dovat S., Gilbert K.A., Petrovic-Dovat L., Rannels D.E.;
RT "Isolation, cloning, and characterization of a novel rat lung zinc finger
RT gene, RLZF-Y.";
RL Biochim. Biophys. Acta 1442:380-388(1998).
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AF052042; AAC78780.1; -; mRNA.
DR RefSeq; NP_663776.1; NM_145724.1.
DR AlphaFoldDB; Q9Z2K3; -.
DR SMR; Q9Z2K3; -.
DR STRING; 10116.ENSRNOP00000001302; -.
DR PaxDb; Q9Z2K3; -.
DR PRIDE; Q9Z2K3; -.
DR GeneID; 252860; -.
DR KEGG; rno:252860; -.
DR CTD; 252860; -.
DR RGD; 628654; Zfp394.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; Q9Z2K3; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9Z2K3; -.
DR Reactome; R-RNO-212436; Generic Transcription Pathway.
DR PRO; PR:Q9Z2K3; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd07765; KRAB_A-box; 1.
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; 1.
DR Pfam; PF02023; SCAN; 1.
DR Pfam; PF00096; zf-C2H2; 6.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 7.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS50804; SCAN_BOX; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE 2: Evidence at transcript level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..536
FT /note="Zinc finger protein 394"
FT /id="PRO_0000047560"
FT DOMAIN 44..126
FT /note="SCAN box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT DOMAIN 135..196
FT /note="KRAB"
FT ZN_FING 328..350
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 356..378
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 384..406
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 412..433
FT /note="C2H2-type 4; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 439..461
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 467..489
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 495..517
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 18..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 20
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q53GI3"
FT CROSSLNK 207
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q53GI3"
FT CROSSLNK 260
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q53GI3"
FT CROSSLNK 413
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q53GI3"
SQ SEQUENCE 536 AA; 60987 MW; 9359894B2565ACD4 CRC64;
MAAGSGVAPP PLGVGLCAVK VEEDSPGSQE PSGSGDWQNP ETSRKQFRQL RYQEVAGPEE
ALSRLWELCR RWLRPELRSK EQIMELLVLE QFLTILPREL QAYVRDHCPE SGEEAAALAR
TLQRALDGAS LQSFATFKDV AESLTWEEWE QLAAARKGFC RESTKDPGST VGPGLETKAV
TTDVILKQEM SKEAESQAWL QEVSQGKVPV FTKCGDTWED WEERLPKAAE LLPLQSSPEE
QGRTAIPHLL GVSKDESDSK DNEFENSGSL VLGQHIQTAE GLVTNGECGE DHKQGLHAKC
HTVKPHSSVD NALGLLESQR HFQEGRPYKC DNCEKRFRQR SDLFKHQRTH TGEKPYQCQE
CGKSFSQSAA LVKHQRTHTG EKPYACPECG ECFRQSSHLS RHQRTHGSEK YCKCEECGEI
FHISSLFKHQ RLHKGERPHK CEVCEKSFKQ RSDLFKHQRI HTGEKPYMCF VCERRFSQSA
TLIKHQRTHT GEKPYKCFQC GERFRQSTHL VRHQRIHHNS VSGLRVEKQH GNLLSW
