ZNF2_PONAB
ID ZNF2_PONAB Reviewed; 425 AA.
AC Q5RBY9;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Zinc finger protein 2 {ECO:0000250|UniProtKB:Q9BSG1};
GN Name=ZNF2 {ECO:0000250|UniProtKB:Q9BSG1};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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}.
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DR EMBL; CR858493; CAH90721.1; -; mRNA.
DR RefSeq; NP_001125401.1; NM_001131929.1.
DR AlphaFoldDB; Q5RBY9; -.
DR SMR; Q5RBY9; -.
DR STRING; 9601.ENSPPYP00000013439; -.
DR GeneID; 100172306; -.
DR KEGG; pon:100172306; -.
DR CTD; 7549; -.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; Q5RBY9; -.
DR Proteomes; UP000001595; 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 transcription, DNA-templated; IEA:InterPro.
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_0000274051"
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 125..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 425 AA; 48409 MW; DCF2A9608183AD17 CRC64;
MAAVSPTTRC QESVTFEDVA VVFTDEEWSH LVPTQRDLYK EVMLENYNSI VSLGLPVPQP
DVIFQLKRGD KPWMVDLHGS EEREWPESVS LDWETKPEIH DASNEKSEGS LRECLGRQSP
LCPKFEVHTP DGRMGTEKQS SSGETHKKSL SQDKGLRRGS ALPREILTKE RHQECSDCGK
TFFDHSSLTR HQRTHTGEKP YDCHECGKAF SHRSSLSRHL MSHTGESPYG CSVCAKAFFD
RSSLTVHQRI HTGEKPFQCN ECGKAFFDRS SLTRHQRIHT GESPYECHQC GKAFSQKSIL
TRHQLIHTGR KPYECNECGK AFYGVSSLNR HQKAHAGDPR YQCNECGKAF FDRSSLTQHQ
KIHTGDKPYE CSECGKAFSQ RCRLTRHQRV HTGEKPFECS VCGKVFSSKS SVIQHQRRYA
KQGID