ID A0A1S3WWD7_ERIEU Unreviewed; 455 AA.
AC A0A1S3WWD7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Zinc finger protein 446 isoform X1 {ECO:0000313|RefSeq:XP_016050622.1};
GN Name=ZNF446 {ECO:0000313|RefSeq:XP_016050622.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_016050622.1};
RN [1] {ECO:0000313|RefSeq:XP_016050622.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PROSITE-ProRule:PRU00187}.
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DR RefSeq; XP_016050622.1; XM_016195136.1.
DR AlphaFoldDB; A0A1S3WWD7; -.
DR GeneID; 103128012; -.
DR CTD; 55663; -.
DR InParanoid; A0A1S3WWD7; -.
DR OrthoDB; 4640674at2759; -.
DR Proteomes; UP000079721; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd07765; KRAB_A-box; 1.
DR CDD; cd07936; SCAN; 1.
DR Gene3D; 6.10.140.140; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 3.
DR Gene3D; 1.10.4020.10; DNA breaking-rejoining enzymes; 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 PANTHER; PTHR45935; PROTEIN ZBED8-RELATED; 1.
DR PANTHER; PTHR45935:SF27; SCAN BOX DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF02023; SCAN; 1.
DR Pfam; PF00096; zf-C2H2; 1.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 2.
DR SUPFAM; SSF109640; KRAB domain (Kruppel-associated box); 1.
DR SUPFAM; SSF47353; Retrovirus capsid dimerization domain-like; 1.
DR PROSITE; PS50804; SCAN_BOX; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|PROSITE-ProRule:PRU00187};
KW Reference proteome {ECO:0000313|Proteomes:UP000079721};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00042}.
FT DOMAIN 34..115
FT /note="SCAN box"
FT /evidence="ECO:0000259|PROSITE:PS50804"
FT DOMAIN 346..373
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 400..427
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 428..455
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 134..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 455 AA; 48754 MW; 3BD52F180588F2D7 CRC64;
MLSPLGRQNQ PSVGPGAVPV AVPVPVPEDP DVARLCFRTF CYQEAAGPRE ALARLRELCR
RWLRPELRSK EQMLELLVLE QFLGALPPEI QAWAREQRPG SPEEAAALVE GLRQDPEPLL
GWITARVLRR EALPAAQKSE GSSGSPLAAG AEGLQDTQPG CTVKEEPDAA KGQEPAFSNP
DPPAAAPSPA GQPGQPGHQE AASSTSQPPE MPHTVGTPGV SQPRPPQGPH PHPACRKEAE
GAGRLHQEEW MLLNRSQKEL HWDVMLEKYG SVVSLAGLPA PQTDTAAESH HGVLLTGPQG
AGSVHPGVQG QGPGAVLPSS SESQPQGDPP GVQTGVGPLP QRKPPYTCEQ CGLSFDWKSV
FVIHHRSHTS GQSPKTVSGR PQKPGAPRHP RHALAGARSY TCEDCGHSFS WKSQLVIHRK
GHASRQRHVC GDCGRGFDWK SQLVIHRKGH QPEAP
//
