ZGPAT_MOUSE
ID ZGPAT_MOUSE Reviewed; 511 AA.
AC Q8VDM1; A2AU20; A2AU21; Q3TW85; Q69Z90; Q8BWW2;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Zinc finger CCCH-type with G patch domain-containing protein;
GN Name=Zgpat; Synonyms=Kiaa1847;
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 [LARGE SCALE MRNA].
RC TISSUE=Fetal brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Heart, Spinal cord, and Thymus;
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].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; SER-276; THR-280 AND
RP SER-353, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Pancreas, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Transcription repressor that specifically binds the 5'-
CC GGAG[GA]A[GA]A-3' consensus sequence. Represses transcription by
CC recruiting the chromatin multiprotein complex NuRD to target promoters.
CC Negatively regulates expression of EGFR, a gene involved in cell
CC proliferation, survival and migration. Its ability to repress genes of
CC the EGFR pathway suggest it may act as a tumor suppressor (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CHD4/Mi-2; the interaction is direct.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32554.1; Type=Miscellaneous discrepancy; Note=The sequence differs from that shown because it seems to be derived from a pre-mRNA.; Evidence={ECO:0000305};
CC Sequence=CAM26425.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AK173276; BAD32554.1; ALT_SEQ; Transcribed_RNA.
DR EMBL; AK041491; BAC30962.1; -; mRNA.
DR EMBL; AK049764; BAC33909.1; -; mRNA.
DR EMBL; AK052236; BAC34894.1; -; mRNA.
DR EMBL; AK159801; BAE35381.1; -; mRNA.
DR EMBL; AL928965; CAM26424.1; -; Genomic_DNA.
DR EMBL; AL928965; CAM26425.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH466626; EDL07412.1; -; Genomic_DNA.
DR EMBL; BC021513; AAH21513.1; -; mRNA.
DR EMBL; BC027218; AAH27218.1; -; mRNA.
DR CCDS; CCDS17210.1; -.
DR RefSeq; NP_001041613.1; NM_001048148.1.
DR RefSeq; NP_659143.1; NM_144894.3.
DR AlphaFoldDB; Q8VDM1; -.
DR SMR; Q8VDM1; -.
DR BioGRID; 230809; 1.
DR STRING; 10090.ENSMUSP00000029105; -.
DR iPTMnet; Q8VDM1; -.
DR PhosphoSitePlus; Q8VDM1; -.
DR SwissPalm; Q8VDM1; -.
DR EPD; Q8VDM1; -.
DR MaxQB; Q8VDM1; -.
DR PaxDb; Q8VDM1; -.
DR PeptideAtlas; Q8VDM1; -.
DR PRIDE; Q8VDM1; -.
DR ProteomicsDB; 275367; -.
DR Antibodypedia; 29857; 120 antibodies from 25 providers.
DR DNASU; 229007; -.
DR Ensembl; ENSMUST00000029105; ENSMUSP00000029105; ENSMUSG00000027582.
DR Ensembl; ENSMUST00000108807; ENSMUSP00000104435; ENSMUSG00000027582.
DR Ensembl; ENSMUST00000116366; ENSMUSP00000112067; ENSMUSG00000027582.
DR GeneID; 229007; -.
DR KEGG; mmu:229007; -.
DR UCSC; uc008omb.1; mouse.
DR CTD; 84619; -.
DR MGI; MGI:2449939; Zgpat.
DR VEuPathDB; HostDB:ENSMUSG00000027582; -.
DR eggNOG; KOG2185; Eukaryota.
DR GeneTree; ENSGT00390000000732; -.
DR HOGENOM; CLU_040504_1_0_1; -.
DR InParanoid; Q8VDM1; -.
DR OMA; QYTRGIG; -.
DR OrthoDB; 1238995at2759; -.
DR PhylomeDB; Q8VDM1; -.
DR TreeFam; TF105970; -.
DR BioGRID-ORCS; 229007; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Zgpat; mouse.
DR PRO; PR:Q8VDM1; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8VDM1; protein.
DR Bgee; ENSMUSG00000027582; Expressed in bronchus and 80 other tissues.
DR ExpressionAtlas; Q8VDM1; baseline and differential.
DR Genevisible; Q8VDM1; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
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:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0007175; P:negative regulation of epidermal growth factor-activated receptor activity; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd04508; TUDOR; 1.
DR InterPro; IPR000467; G_patch_dom.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR043560; ZGPAT.
DR InterPro; IPR041367; Znf-CCCH_4.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR46297; PTHR46297; 1.
DR Pfam; PF01585; G-patch; 1.
DR Pfam; PF18044; zf-CCCH_4; 1.
DR SMART; SM00443; G_patch; 1.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF90229; SSF90229; 1.
DR PROSITE; PS50174; G_PATCH; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 1: Evidence at protein level;
KW Acetylation; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Zinc; Zinc-finger.
FT CHAIN 1..511
FT /note="Zinc finger CCCH-type with G patch domain-containing
FT protein"
FT /id="PRO_0000213895"
FT DOMAIN 313..359
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT ZN_FING 174..200
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 92..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..511
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q8N5A5"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 280
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 236
FT /note="R -> Q (in Ref. 2; BAC33909)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="I -> T (in Ref. 2; BAE35381)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 511 AA; 56411 MW; 13B7C46AB107F918 CRC64;
MDEDNLETAL QTYRAQLQQV ELALGAGLDA SEQADLRQLQ GDLKELIELT EASLLSVRKS
KLLSTVDQES PAQEDAEYLA FQKAIAEEVE APGAPCNDSE TAPGSEVQPG STSSALEEEE
EDPDLEELSG AKVNAPYYSA WGTLEYHNAM VVGAEEAEDG SACVRVLYLY PTHKSLKPCP
FFLEGKCRFK ENCRFSHGQV VSVDELRPFQ DPDLSLLQTG SACLAKHQDG LWHPARITDV
DNGYYTVKFD SLLLKEAVVE GDSILPPLRT EATESSDSDT GDASDSSYAR VVEPSTVDTG
TCSSAFAGWE VHTRGIGSKL LVKMGYEFGK GLGRHAEGRV EPIHAVVLPR GKSLDQCAEI
LQKKTKRGQA GSNRPPKCRR SGSRPEGRPP PRNVFDFLNE KLQSQVPGTP DAGVDTPERR
NKDMYHASKS AKQALSLQLF QTEEKIERTQ RDIRGIQEAL TRNTGRHNMT TAHLQEKLEG
AQRQLGQLRA QEADLQRKQR KADTHRKMTE F
