ZN205_BOVIN
ID ZN205_BOVIN Reviewed; 550 AA.
AC Q58DK7;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Zinc finger protein 205;
GN Name=ZNF205;
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].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-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}.
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DR EMBL; BT021590; AAX46437.1; -; mRNA.
DR EMBL; BC123477; AAI23478.1; -; mRNA.
DR RefSeq; NP_001029645.1; NM_001034473.2.
DR RefSeq; XP_005224502.1; XM_005224445.3.
DR AlphaFoldDB; Q58DK7; -.
DR SMR; Q58DK7; -.
DR STRING; 9913.ENSBTAP00000007323; -.
DR PaxDb; Q58DK7; -.
DR PRIDE; Q58DK7; -.
DR Ensembl; ENSBTAT00000074230; ENSBTAP00000067638; ENSBTAG00000005572.
DR GeneID; 514765; -.
DR KEGG; bta:514765; -.
DR CTD; 7755; -.
DR VEuPathDB; HostDB:ENSBTAG00000005572; -.
DR VGNC; VGNC:37224; ZNF205.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161865; -.
DR InParanoid; Q58DK7; -.
DR OMA; EWRGAYT; -.
DR OrthoDB; 1318335at2759; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000005572; Expressed in retina and 102 other tissues.
DR ExpressionAtlas; Q58DK7; baseline and differential.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
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:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
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:0010729; P:positive regulation of hydrogen peroxide biosynthetic process; IEA:Ensembl.
DR GO; GO:1901030; P:positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; IEA:Ensembl.
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; 8.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 8.
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; 8.
PE 2: Evidence at transcript level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..550
FT /note="Zinc finger protein 205"
FT /id="PRO_0000254022"
FT DOMAIN 124..193
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 306..328
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 334..356
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 362..384
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 390..412
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 418..440
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 446..468
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 474..496
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 502..524
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95201"
FT CROSSLNK 216
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O95201"
SQ SEQUENCE 550 AA; 60459 MW; C1B14CA37B485DE9 CRC64;
MSADDGGIRA AQDKERARET PGHGHSCQEM LSESEGTVPL GEAWESPHIK MEPEEPHPEG
VSQETRAEGA RGWVPLSQGT KEKVCFLPGG ALPAPQTPVL SREGRTRDRQ MAAALLTAWS
QMPVTFEDMA LYLSREEWGR LDHTQQSFYR EVLQKRSGLS LGFPFSRPFW ASQVQGKGEA
PGSSRQLGHE EEEKRGVVEV DKEELAASLG ALGDAKSFKS RMGRAQGEAP RCGQRAASGQ
NSGPAKDDVQ PCPVKEAQLE SAPPDTDLPK TQEGHFPEQP REGGTAAPES SEEGLALDSE
AGKKTYKCEQ CGKAFSWHSH LVTHRRTHTG EKPYACTDCG KRFGRSSHLI QHQIIHTGEK
PYTCPSCWKS FSHHSTLIQH QRIHTGEKPY VCDRCAKRFT RRSDLVTHQG THTGAKPHKC
PICGKCFTQS SALVTHQRTH TGVKPYPCPE CGKCFSQRSN LIAHNRTHTG EKPYHCLDCG
KSFSHSSHLT AHQRTHRGVR PYSCPLCGKS FSRRSNLHRH EKIHTAGPKA LAMLMLGAAG
TLAAPPPAPT
