ID ZFP58_MOUSE Reviewed; 489 AA. AC P16372; Q3TS54; Q6P8L3; Q7M6X1; Q8BRV1; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 20-APR-2010, sequence version 2. DT 02-SEP-2026, entry version 182. DE RecName: Full=Zinc finger protein 58; DE Short=Zfp-58; DE AltName: Full=Regulator of sex-limitation candidate 5; DE AltName: Full=Zinc finger protein Mfg-1; GN Name=Zfp58; Synonyms=Mfg-1, Rslcan5, Zfp817; 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]. RC STRAIN=C57BL/6J; RX PubMed=14563677; DOI=10.1101/gad.1135703; RA Krebs C.J., Larkins L.K., Price R., Tullis K.M., Miller R.D., Robins D.M.; RT "Regulator of sex-limitation (Rsl) encodes a pair of KRAB zinc-finger genes RT that control sexually dimorphic liver gene expression."; RL Genes Dev. 17:2664-2674(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Aorta, Egg, Placenta, and Vein; 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 GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 99-239, FUNCTION, TISSUE SPECIFICITY, AND RP DEVELOPMENTAL STAGE. RX PubMed=2512579; DOI=10.1073/pnas.86.23.9417; RA Passananti C., Felsani A., Caruso M., Amati P.; RT "Mouse genes coding for 'zinc-finger'-containing proteins: characterization RT and expression in differentiated cells."; RL Proc. Natl. Acad. Sci. U.S.A. 86:9417-9421(1989). CC -!- FUNCTION: May have a role during differentiation processes. CC {ECO:0000269|PubMed:2512579}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. CC -!- TISSUE SPECIFICITY: Expressed in liver, testis and, at considerably CC lower levels, in brain, spleen and heart. {ECO:0000269|PubMed:2512579}. CC -!- DEVELOPMENTAL STAGE: Expression increases upon differentiation and is CC not related to the cell cycle. {ECO:0000269|PubMed:2512579}. CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein CC family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH61200.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BK001635; DAA01860.1; -; mRNA. DR EMBL; AK041250; BAC30880.1; -; mRNA. DR EMBL; AK162259; BAE36821.1; -; mRNA. DR EMBL; AK167399; BAE39488.1; -; mRNA. DR EMBL; CH466661; EDL10303.1; -; Genomic_DNA. DR EMBL; CH466661; EDL10304.1; -; Genomic_DNA. DR EMBL; BC061200; AAH61200.1; ALT_SEQ; mRNA. DR EMBL; BC139150; AAI39151.1; -; mRNA. DR EMBL; BC139151; AAI39152.1; -; mRNA. DR EMBL; M28513; AAA39531.1; -; mRNA. DR CCDS; CCDS26616.1; -. DR PIR; A39240; A39240. DR RefSeq; NP_001007576.1; NM_001007575.2. DR AlphaFoldDB; P16372; -. DR SMR; P16372; -. DR BioGRID; 232010; 32. DR FunCoup; P16372; 1. DR STRING; 10090.ENSMUSP00000075487; -. DR iPTMnet; P16372; -. DR PhosphoSitePlus; P16372; -. DR PaxDb; 10090-ENSMUSP00000075487; -. DR ProteomicsDB; 299548; -. DR DNASU; 238693; -. DR Ensembl; ENSMUST00000076123.12; ENSMUSP00000075487.6; ENSMUSG00000071291.11. DR Ensembl; ENSMUST00000171518.8; ENSMUSP00000132285.2; ENSMUSG00000071291.11. DR GeneID; 238693; -. DR KEGG; mmu:238693; -. DR UCSC; uc007rax.2; mouse. DR AGR; MGI:99205; -. DR CTD; 238693; -. DR MGI; MGI:99205; Zfp58. DR VEuPathDB; HostDB:ENSMUSG00000071291; -. DR eggNOG; KOG1721; Eukaryota. DR GeneTree; ENSGT00940000153165; -. DR HOGENOM; CLU_476683_0_0_1; -. DR InParanoid; P16372; -. DR OMA; AYNCEEC; -. DR OrthoDB; 6077919at2759; -. DR PhylomeDB; P16372; -. DR Reactome; R-MMU-212436; Generic Transcription Pathway. DR BioGRID-ORCS; 238693; 1 hit in 78 CRISPR screens. DR PRO; PR:P16372; -. DR Proteomes; UP000000589; Chromosome 13. DR RNAct; P16372; protein. DR Bgee; ENSMUSG00000071291; Expressed in animal zygote and 65 other cell types or tissues. DR ExpressionAtlas; P16372; baseline and differential. 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:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:UniProtKB-ARBA. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR CDD; cd07765; KRAB_A-box; 1. DR FunFam; 3.30.160.60:FF:001956; ZFP37 zinc finger protein; 1. DR FunFam; 3.30.160.60:FF:000380; zinc finger protein 2 isoform X2; 1. DR FunFam; 3.30.160.60:FF:002005; Zinc finger protein 200; 1. DR FunFam; 3.30.160.60:FF:002343; Zinc finger protein 33A; 3. DR FunFam; 3.30.160.60:FF:000690; Zinc finger protein 354C; 2. DR FunFam; 3.30.160.60:FF:002254; Zinc finger protein 540; 1. DR FunFam; 3.30.160.60:FF:001437; Zinc finger protein 594; 1. DR FunFam; 3.30.160.60:FF:001630; Zinc finger protein 888; 1. DR FunFam; 3.30.160.60:FF:001671; Zinc finger protein 94; 1. DR Gene3D; 6.10.140.140; -; 1. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 15. DR InterPro; IPR001909; KRAB. DR InterPro; IPR036051; KRAB_dom_sf. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR24376; ZINC FINGER PROTEIN; 1. DR PANTHER; PTHR24376:SF253; ZINC FINGER PROTEIN 748; 1. DR Pfam; PF01352; KRAB; 1. DR Pfam; PF00096; zf-C2H2; 11. DR Pfam; PF13465; zf-H2C2_2; 1. DR SMART; SM00349; KRAB; 1. DR SMART; SM00355; ZnF_C2H2; 14. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 8. DR SUPFAM; SSF109640; KRAB domain (Kruppel-associated box); 1. DR PROSITE; PS50805; KRAB; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 14. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 15. 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..489 FT /note="Zinc finger protein 58" FT /id="PRO_0000047302" FT DOMAIN 2..73 FT /note="KRAB" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119" FT ZN_FING 78..100 FT /note="C2H2-type 1; degenerate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 106..128 FT /note="C2H2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 134..156 FT /note="C2H2-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 162..184 FT /note="C2H2-type 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 190..212 FT /note="C2H2-type 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 218..240 FT /note="C2H2-type 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 246..268 FT /note="C2H2-type 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 274..296 FT /note="C2H2-type 8" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 302..324 FT /note="C2H2-type 9" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 330..352 FT /note="C2H2-type 10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 358..380 FT /note="C2H2-type 11" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 386..408 FT /note="C2H2-type 12" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 410..432 FT /note="C2H2-type 13" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 438..460 FT /note="C2H2-type 14" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 466..488 FT /note="C2H2-type 15" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT CONFLICT 190 FT /note="Y -> YKCEECGKAFSTSSNLSEHKRIHTGEKPI (in Ref. 5; FT AAA39531)" FT /evidence="ECO:0000305" SQ SEQUENCE 489 AA; 57232 MW; 32A9FFF460AEE061 CRC64; MLSFWDVAID FSPEERECLE PDQWDLYRDV MLENYSHLDF LGLALSKPFL VTFLEQRQGP WDVKRQAAAA VHPGKTVNKC KDFSKAFFCK SLLTQHQRIR TGEKAFKCEE CGKAFNNRSN LSEHKRIHTG EKPYKCEECG KAFRIRSKLS THQRVHTGEK PYKCEECGKA FNSHSNLSEH KRIHTGEKPY KCEECGKAFS TRSTYYRHQK NHTGKKPYKC EECAKEFSYP SLLKVHQRIH SAEKSYKCEE CGKPFYCPLL LKKHQIIHSA EKPYKCAECG KAFHYPSLLK RHQRIHAGKK PCKCKDCDRA FYSSAFLKRH QRIHSEENSY KCGECGKRFC SFPHLQYHQR FHSGEKPYKC EQCGKTFSTL SYLPWHKLRH SGEKSYKCEK CGKMFYSTLD LKKHQKIHEY KCGECHYGFP NYAALTAHQR VHTGEKPHVC EQCGKDFSRI DSLNQHQLVH TGEKPYKCEK CGKCFYRSSS LKRHQGIHS //