ZN467_RAT
ID ZN467_RAT Reviewed; 594 AA.
AC Q5RJR4;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Zinc finger protein 467;
GN Name=Znf467; Synonyms=Zfp467;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Transcription factor that promotes adipocyte differentiation
CC and suppresses osteoblast differentiation in the bone marrow. Enhances
CC the osteoclast-supporting ability of stromal cells. Binds with STAT3
CC the consensus sequence 5'-CTTCTGGGAAGA-3' of the acute phase response
CC element (APRE). Transactivates several promoters including FOS, OSM and
CC PPARG. Recruits a histone deacetylase complex (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with STAT3. Enhances STAT3 activity by keeping it in
CC the nucleus (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; BC086534; AAH86534.1; -; mRNA.
DR RefSeq; NP_001019498.1; NM_001024327.1.
DR RefSeq; XP_006236493.1; XM_006236431.3.
DR RefSeq; XP_006236494.1; XM_006236432.3.
DR RefSeq; XP_006236495.1; XM_006236433.3.
DR RefSeq; XP_006236496.1; XM_006236434.3.
DR AlphaFoldDB; Q5RJR4; -.
DR SMR; Q5RJR4; -.
DR STRING; 10116.ENSRNOP00000010377; -.
DR PaxDb; Q5RJR4; -.
DR Ensembl; ENSRNOT00000010377; ENSRNOP00000010377; ENSRNOG00000007707.
DR GeneID; 500110; -.
DR KEGG; rno:500110; -.
DR UCSC; RGD:1561603; rat.
DR CTD; 68910; -.
DR RGD; 1561603; Zfp467.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162497; -.
DR HOGENOM; CLU_002678_73_2_1; -.
DR InParanoid; Q5RJR4; -.
DR OMA; CSGDEWM; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q5RJR4; -.
DR TreeFam; TF326846; -.
DR PRO; PR:Q5RJR4; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000007707; Expressed in liver and 19 other tissues.
DR ExpressionAtlas; Q5RJR4; baseline and differential.
DR Genevisible; Q5RJR4; RN.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator 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; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 9.
DR SMART; SM00355; ZnF_C2H2; 12.
DR SUPFAM; SSF57667; SSF57667; 7.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 12.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 12.
PE 2: Evidence at transcript level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..594
FT /note="Zinc finger protein 467"
FT /id="PRO_0000247519"
FT ZN_FING 160..182
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 188..210
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 216..238
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 244..266
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 272..294
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 300..322
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 355..377
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 430..452
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 458..480
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 486..508
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 514..536
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 542..564
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..348
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 97
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q7Z7K2"
FT CROSSLNK 368
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q7Z7K2"
SQ SEQUENCE 594 AA; 65753 MW; 9AC61F71F72AEC84 CRC64;
MRETLEALNS LGFSVGQPEM APQSEPRDGF SNPQEKMSSR DESTLHSCSG PETPGQKEGI
HTEQAEAPCM GSQACIPQKA EPASSVPGEE WMIRKVKVED EDQEAEEEVE WPQHLSFLPS
PFPTPDLGQL AVAYKLEPGT PGTLGGIALS GWAPIPEKPY GCEECERRFR DQLTLRLHQR
LHRGEGPCAC PDCGRSFTQR AHMLLHQRSH RGERPFPCSE CDKRFSKKAH LTRHLRTHTG
ERPYPCAECG KRFSQKIHLG SHQKTHTGER PFPCTECEKR FRKKTHLIRH QRIHTGERPY
QCTQCTRSFT HKQHLVRHQR VHDAASRTRS SPDIPATPHP PTASLAPSPT GPKPFACSHC
GQSFGWKKNL ATHQSLHLTE GRPFGCDECA LGTNVDPAAE PSACTPHAPD CGPGSGPVAP
QRTTSSERSF FCPDCGRGFA HGQHLARHRR VHTGERPFAC AQCGRRFGSR PNLVAHSRAH
SGARPFACAQ CGRRFSRKSH LGRHQAVHTG SRPHACAVCA RCFSSKTNLV RHQAIHTGSR
PFSCPQCAKS FSRKTHLVRH QRIHGEAALP ASASNLSAPA WSNPSEVVPP PIFF
