ZN252_CANLF
ID ZN252_CANLF Reviewed; 873 AA.
AC Q9XSR1;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Zinc finger protein 252;
GN Name=ZNF252; ORFNames=BC3;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND SUBCELLULAR LOCATION.
RC TISSUE=Thyroid;
RX PubMed=10964405; DOI=10.1006/abio.2000.4674;
RA Pichon B., Mercan D., Pouillon V., Christophe-Hobertus C., Christophe D.;
RT "A method for the large-scale cloning of nuclear proteins and nuclear
RT targeting sequences on a functional basis.";
RL Anal. Biochem. 284:231-239(2000).
CC -!- FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10964405}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AJ388557; CAB46856.1; -; mRNA.
DR RefSeq; NP_001002954.1; NM_001002954.1.
DR AlphaFoldDB; Q9XSR1; -.
DR SMR; Q9XSR1; -.
DR PaxDb; Q9XSR1; -.
DR PRIDE; Q9XSR1; -.
DR GeneID; 403421; -.
DR KEGG; cfa:403421; -.
DR CTD; 705244; -.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; Q9XSR1; -.
DR OrthoDB; 1318335at2759; -.
DR Proteomes; UP000002254; 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; 16.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 21.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 12.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 18.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 20.
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..873
FT /note="Zinc finger protein 252"
FT /id="PRO_0000348064"
FT DOMAIN 15..86
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 265..287
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 291..315
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 321..343
FT /note="C2H2-type 3; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 372..394
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 400..422
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 428..450
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 456..478
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 484..506
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 512..534
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 540..562
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 568..590
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 596..618
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 624..646
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 652..674
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 680..702
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 708..730
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 736..758
FT /note="C2H2-type 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 764..786
FT /note="C2H2-type 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 792..814
FT /note="C2H2-type 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 820..842
FT /note="C2H2-type 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 145..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 873 AA; 99448 MW; FC08B032F878DC47 CRC64;
MAVKQLLPAG SQVLVSFEDV AVLLSREEWG RLGPAQRGLY SDVMLETYRN LISLGLQGSK
PDVISRLEKG EEPWAPYSAK IEESWIRSHE SESFQSLMEK KGLTPKQEIS KAMGFRRAKS
EYVRNVSKES EFEEMNKTKG KLKNYRKKSA EEELKKSFSQ KNSSRPVTLT HVKSPVSGKG
QKSSSLEVDY TVDASPVRFH RASTGGSLHQ NVPCVNDFQQ SQDLINLQCL HLGERACQTD
LFMKAPRQSS VLSENQRVNN PEKSFECTEC RRLFSPSKAL SQHQRSHTGE IPCESGGCGR
TSHHCSVLSQ HQEVHHGGES HTCAECGKAF KAHSYFIQQH NTHTGERPYE CSECAHLSYS
QHLQIHSGQK PHECSQCGKA FSHSSNLFHH QRIHSGEKPY ECKECGKAFG RHSHLLQHKR
IHSGEKPYDC TECGKAFSAR LSLIQHQRTH TGEKPYECNE CGKSFSLNRT LIVHQRIHTG
EKPYRCNECG KSFSQRAQVI QHKRIHTGEK PYVCNECGKS FSARLSLIQH QRIHTGEKPY
GCSECGKTFS QKGHLIQHQR IHTGEKPYEC NECGKAFSQS FNLIHHQRTH NGEKPYECNE
CDKAFSVLSS LVQHQRVHNG EKPYECHKCG KAFSQGSHLI QHQRSHTGEK PYECNECGKT
FGQISTLIKH ERTHNGEKPY ECGDCGKAFS QSAHLVRHRR IHTGENPYEC SDCGKAFNVR
SSLVQHHRIH TGEKPYECEK CGKAFSQHSQ FIQHQRIHTG EKPYICNECE KAFSARLSLI
QHKRIHTGEK PYKCTECGKS FRQSSHLIRH QRVHSGERPY MCNECGKTFS QRITLTSHEK
THTREQAYKC VKREDLLTAQ SASIQHHKVH NGE
