ZNF2_BOVIN
ID ZNF2_BOVIN Reviewed; 425 AA.
AC Q29RZ4;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Zinc finger protein 2 {ECO:0000250|UniProtKB:Q9BSG1};
GN Name=ZNF2 {ECO:0000250|UniProtKB:Q9BSG1};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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; BC113303; AAI13304.1; -; mRNA.
DR RefSeq; NP_001039911.1; NM_001046446.2.
DR RefSeq; XP_010808051.1; XM_010809749.2.
DR AlphaFoldDB; Q29RZ4; -.
DR SMR; Q29RZ4; -.
DR STRING; 9913.ENSBTAP00000002533; -.
DR PaxDb; Q29RZ4; -.
DR GeneID; 539022; -.
DR KEGG; bta:539022; -.
DR CTD; 7549; -.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; Q29RZ4; -.
DR OrthoDB; 1318335at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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 InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 7.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 9.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 5.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
PE 2: Evidence at transcript level;
KW DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..425
FT /note="Zinc finger protein 2"
FT /id="PRO_0000274048"
FT DOMAIN 14..85
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 173..195
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 201..223
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 229..251
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 257..279
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 285..307
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 313..335
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 341..363
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 369..391
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 397..419
FT /note="C2H2-type 9; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 97..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 425 AA; 48223 MW; E7220404A4E1FB91 CRC64;
MAAVSPTRCQ DPVTFEDVAV VFTDEEWRRL VPTQRDLYKE VMLENYKSIV SLGLPVPGPD
VIFQLKRGDE PWLVEFHGFE GKEGAENVSL DWETKPEIQG ASEEEKSEGS LKENLGRKGP
PSPKVEVYVL DGRLGTEKES PTVEACKKPP SLEESLRHRA TPPKKFLTKE RDQECSNCGK
TFFDHSSLIR HQRTHTGEKP YDCPECGKAF SHRSSLSRHL MSHTGESPYE CNACGKAFFD
RSSLTVHQRI HTGEKPFKCS ECGKAFFDRS SLTRHQRIHT GESPYECNQC GKAFSQKSIL
TRHQLIHTGR KPYECNECGK AFYGVSSLNR HQKAHAGEPR YQCSECGKAF FDRSSLTQHQ
KIHTGDKPYE CSECGKAFSQ RCRLTRHQRV HTGEKPFECS VCGKVFSSKS SVIQHQRRYA
KQGID