ID   OZF_MOUSE               Reviewed;         292 AA.
AC   Q8BQN6; A0JNX3; Q9Z0Q5;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 2.
DT   27-MAR-2024, entry version 160.
DE   RecName: Full=Zinc finger protein OZF;
DE   AltName: Full=Only zinc finger protein;
DE   AltName: Full=Zinc finger protein 146;
GN   Name=Znf146; Synonyms=Ozf, Zfp146;
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], AND TISSUE SPECIFICITY.
RX   PubMed=10449921; DOI=10.1159/000015316;
RA   Blottiere L., Apiou F., Ferbus D., Guenzi C., Dutrillaux B.,
RA   Prosperi M.-T., Goubin G.;
RT   "Cloning, characterization, and chromosome assignment of Zfp146 the mouse
RT   ortholog of human ZNF146, a gene amplified and overexpressed in pancreatic
RT   cancer, and Zfp260 a closely related gene.";
RL   Cytogenet. Cell Genet. 85:297-300(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Corpus striatum;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [4]
RP   DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=12437081; DOI=10.1023/a:1020347123109;
RA   Besnar N., Persuy M.-A., Stinnakre M.-G., Lepourry L., Da Silva J.C.,
RA   Goubin G., Vilotte J.-L.;
RT   "Targeted expression of the only zinc finger gene in transgenic mice is
RT   associated with impaired mammary development.";
RL   Transgenic Res. 11:505-513(2002).
CC   -!- SUBUNIT: Binds DNA. Interacts with SUMO conjugating enzyme UBC9/UBE2I.
CC       Interacts with the telomeric protein TERF2IP (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in heart, brain, liver, lung, skeletal
CC       muscle and kidney, and at much lower level in spleen and testicle.
CC       Expressed in lactating mammary gland. {ECO:0000269|PubMed:10449921,
CC       ECO:0000269|PubMed:12437081}.
CC   -!- DISRUPTION PHENOTYPE: Mice lacking Zfp146 in mammary gland display
CC       impaired mammary gland development. They cannot sustain full growth of
CC       their pups. This phenotype is associated with an impaired mammary gland
CC       development noticeable only after mid-gestation.
CC       {ECO:0000269|PubMed:12437081}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC33129.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AJ224763; CAB38320.1; -; mRNA.
DR   EMBL; AK047696; BAC33129.1; ALT_INIT; mRNA.
DR   EMBL; BC127038; AAI27039.1; -; mRNA.
DR   EMBL; BC127039; AAI27040.1; -; mRNA.
DR   CCDS; CCDS21079.1; -.
DR   RefSeq; NP_036110.1; NM_011980.3.
DR   RefSeq; XP_006540071.1; XM_006540008.2.
DR   RefSeq; XP_006540072.1; XM_006540009.2.
DR   AlphaFoldDB; Q8BQN6; -.
DR   SMR; Q8BQN6; -.
DR   STRING; 10090.ENSMUSP00000058588; -.
DR   iPTMnet; Q8BQN6; -.
DR   PhosphoSitePlus; Q8BQN6; -.
DR   EPD; Q8BQN6; -.
DR   MaxQB; Q8BQN6; -.
DR   PaxDb; 10090-ENSMUSP00000058588; -.
DR   PeptideAtlas; Q8BQN6; -.
DR   ProteomicsDB; 294086; -.
DR   Pumba; Q8BQN6; -.
DR   Antibodypedia; 929; 187 antibodies from 25 providers.
DR   DNASU; 26465; -.
DR   Ensembl; ENSMUST00000062181.9; ENSMUSP00000058588.8; ENSMUSG00000037029.9.
DR   GeneID; 26465; -.
DR   KEGG; mmu:26465; -.
DR   UCSC; uc009gdn.1; mouse.
DR   AGR; MGI:1347092; -.
DR   CTD; 26465; -.
DR   MGI; MGI:1347092; Zfp146.
DR   VEuPathDB; HostDB:ENSMUSG00000037029; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000162671; -.
DR   HOGENOM; CLU_002678_2_1_1; -.
DR   InParanoid; Q8BQN6; -.
DR   OMA; ENQSEMA; -.
DR   OrthoDB; 3823881at2759; -.
DR   PhylomeDB; Q8BQN6; -.
DR   TreeFam; TF337055; -.
DR   BioGRID-ORCS; 26465; 0 hits in 79 CRISPR screens.
DR   PRO; PR:Q8BQN6; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q8BQN6; Protein.
DR   Bgee; ENSMUSG00000037029; Expressed in ventricular zone and 153 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005730; C:nucleolus; ISO:MGI.
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:0000977; F:RNA polymerase II transcription 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   Gene3D; 3.30.160.60; Classic Zinc Finger; 10.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR23232; KRAB DOMAIN C2H2 ZINC FINGER; 1.
DR   PANTHER; PTHR23232:SF135; ZINC FINGER PROTEIN 11; 1.
DR   Pfam; PF00096; zf-C2H2; 10.
DR   SMART; SM00355; ZnF_C2H2; 10.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 5.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 10.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 10.
DR   Genevisible; Q8BQN6; MM.
PE   2: Evidence at transcript level;
KW   DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW   Repeat; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..292
FT                   /note="Zinc finger protein OZF"
FT                   /id="PRO_0000047277"
FT   ZN_FING         16..38
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         44..66
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         72..94
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         100..122
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         128..150
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         156..178
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         184..206
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         212..234
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         240..262
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         268..290
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          212..292
FT                   /note="Interaction with TERF2IP"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        28
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q15072"
FT   CROSSLNK        51
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q15072"
FT   CROSSLNK        56
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q15072"
FT   CROSSLNK        157
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        169
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        173
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q15072"
SQ   SEQUENCE   292 AA;  33093 MW;  A0F985ABBEE7CADD CRC64;
     MSQLSQQRIL SGGSPFACKV CGKLFSHKSN LTEHEHFHSR EKPFECNECG KAFSQKQYVI
     KHQSTHSGEK LFECSDCGKA FSQKENLLTH QKIHTGEKPF ECKDCGKAFI QKSNLIRHQR
     THTGEKPFIC KECGKTFSGK SNLTEHEKIH IGEKPFKCNE CGTAFGQKKY LIKHQNIHTG
     EKPYECNECG KAFSQRTSLI VHVRIHSGDK PYECNVCGKA FSQSSSLTVH VRSHTGEKPY
     GCNECGKAFS QFSTLALHLR IHTGKKPYQC SECGKAFSQK SHHIRHQKIH TH
//