ZN467_MOUSE
ID ZN467_MOUSE Reviewed; 594 AA.
AC Q8JZL0; Q9JJ98;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Zinc finger protein 467;
DE AltName: Full=Endothelial cell-derived zinc finger protein;
DE Short=EZI;
GN Name=Znf467; Synonyms=Ezi, Zfp467; ORFNames=MNCb-3350;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION
RP WITH STAT3.
RX PubMed=12426389; DOI=10.1093/emboj/cdf596;
RA Nakayama K., Kim K.-W., Miyajima A.;
RT "A novel nuclear zinc finger protein EZI enhances nuclear retention and
RT transactivation of STAT3.";
RL EMBO J. 21:6174-6184(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT oligo-capping method.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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).
RN [5]
RP FUNCTION, AND INDUCTION.
RX PubMed=21123171; DOI=10.1074/jbc.m110.178251;
RA Quach J.M., Walker E.C., Allan E., Solano M., Yokoyama A., Kato S.,
RA Sims N.A., Gillespie M.T., Martin T.J.;
RT "Zinc finger protein 467 is a novel regulator of osteoblast and adipocyte
RT commitment.";
RL J. Biol. Chem. 286:4186-4198(2011).
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.
CC {ECO:0000269|PubMed:12426389, ECO:0000269|PubMed:21123171}.
CC -!- SUBUNIT: Interacts with STAT3. Enhances STAT3 activity by keeping it in
CC the nucleus. {ECO:0000269|PubMed:12426389}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12426389}.
CC -!- INDUCTION: Down-regulated by CTF1, PTH and OSM.
CC {ECO:0000269|PubMed:21123171}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA95099.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB076746; BAC00997.1; -; mRNA.
DR EMBL; AB041616; BAA95099.1; ALT_FRAME; mRNA.
DR EMBL; AK033146; BAC28171.1; -; mRNA.
DR EMBL; BC029859; AAH29859.1; -; mRNA.
DR CCDS; CCDS51764.1; -.
DR RefSeq; NP_001078884.1; NM_001085415.1.
DR RefSeq; NP_001078885.1; NM_001085416.1.
DR RefSeq; NP_065614.2; NM_020589.2.
DR AlphaFoldDB; Q8JZL0; -.
DR SMR; Q8JZL0; -.
DR BioGRID; 213109; 4.
DR IntAct; Q8JZL0; 1.
DR STRING; 10090.ENSMUSP00000110208; -.
DR iPTMnet; Q8JZL0; -.
DR PhosphoSitePlus; Q8JZL0; -.
DR MaxQB; Q8JZL0; -.
DR PaxDb; Q8JZL0; -.
DR PRIDE; Q8JZL0; -.
DR ProteomicsDB; 275079; -.
DR Antibodypedia; 51657; 13 antibodies from 8 providers.
DR DNASU; 68910; -.
DR Ensembl; ENSMUST00000114560; ENSMUSP00000110207; ENSMUSG00000068551.
DR Ensembl; ENSMUST00000114561; ENSMUSP00000110208; ENSMUSG00000068551.
DR GeneID; 68910; -.
DR KEGG; mmu:68910; -.
DR UCSC; uc009buf.1; mouse.
DR CTD; 68910; -.
DR MGI; MGI:1916160; Zfp467.
DR VEuPathDB; HostDB:ENSMUSG00000068551; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162497; -.
DR HOGENOM; CLU_002678_73_2_1; -.
DR InParanoid; Q8JZL0; -.
DR OMA; CSGDEWM; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q8JZL0; -.
DR TreeFam; TF326846; -.
DR BioGRID-ORCS; 68910; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q8JZL0; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8JZL0; protein.
DR Bgee; ENSMUSG00000068551; Expressed in pigmented layer of retina and 246 other tissues.
DR ExpressionAtlas; Q8JZL0; baseline and differential.
DR Genevisible; Q8JZL0; MM.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
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; IBA:GO_Central.
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; IDA:MGI.
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; 8.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 12.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 12.
PE 1: Evidence at protein 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_0000247518"
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..183
FT /note="Interaction with STAT3"
FT /evidence="ECO:0000269|PubMed:12426389"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..351
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 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"
FT CONFLICT 511
FT /note="S -> G (in Ref. 2; BAA95099)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 594 AA; 65633 MW; E11EA6416C4A5C6C CRC64;
MRETLEALNS LGFSVGQPEM APQSEPRDGF SNAQEKMSSR GESTLHSCSG HETPGQKEGI
HTEQAEAPCM GSQASTPQKA EPAGSVPGEE WMIRKVKVED EDQEAEEEVE WPQHLSFLPS
PFPTPDLGQL AVTYKLEPGT PGALGGIALS GWAPIPEKPY GCEECERRFR DQLTLRLHQR
LHRGEGPCAC PDCGRSFTQR AHMLLHQRSH RGERPFPCSE CDKRFSKKAH LTRHLRTHTG
ERPYPCAECG KRFSQKIHLG SHQKTHTGER PFPCTECEKR FRKKTHLIRH QRIHTGERPY
QCTQCTRSFT HKQHLVRHQR VHDAASRTRS SPDIPVAPHS PTASLTPSPP GPKPFACSHC
GQSFGWKKNL ATHQSLHLTE GRPFGCDECA LGTNVDPAAE PSACTPHAPD CGPGSGPAAP
QRTTSSERSF FCPDCGRGFA HGQHLARHRR VHTGERPFAC AQCGRRFGSR PNLVAHSRAH
SGARPFACAQ CGRRFSRKSH LGRHQAVHTG SRPHACAVCA RCFSSKTNLV RHQAIHTGSR
PFSCPQCAKS FSRKTHLVRH QRIHGDAALP APASNLSAPA WSNPSEVVPP PIFF
