ZN704_MOUSE
ID ZN704_MOUSE Reviewed; 566 AA.
AC Q9ERQ3; Q7TQL8; Q8BJW9;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Zinc finger protein 704 {ECO:0000312|MGI:MGI:2180715};
DE AltName: Full=Glucocorticoid-induced gene 1 protein {ECO:0000303|PubMed:17693064};
GN Name=Znf704 {ECO:0000250|UniProtKB:Q6ZNC4};
GN Synonyms=Gig1 {ECO:0000303|PubMed:17693064},
GN Zfp704 {ECO:0000312|MGI:MGI:2180715};
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, DEVELOPMENTAL
RP STAGE, DISRUPTION PHENOTYPE, MOTIF, AND MUTAGENESIS OF 537-LYS--LYS-541 AND
RP 555-CYS--LYS-559.
RC STRAIN=BALB/cJ;
RX PubMed=17693064; DOI=10.1016/j.mod.2007.07.002;
RA Yamamoto M., Watt C.D., Schmidt R.J., Kuscuoglu U., Miesfeld R.L.,
RA Goldhamer D.J.;
RT "Cloning and characterization of a novel MyoD enhancer-binding factor.";
RL Mech. Dev. 124:715-728(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 301-566.
RC TISSUE=Pancreas;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 363-566.
RC STRAIN=C57BL/6J; TISSUE=Muellerian duct;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378 AND SER-381, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, and Lung;
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 factor which binds to RE2 sequence elements in
CC the MYOD1 enhancer. {ECO:0000269|PubMed:17693064}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17693064}.
CC -!- DEVELOPMENTAL STAGE: Expressed from embryonic stage 9.5 dpc to 14.5
CC dpc. Detected in tissues from all three germ layers, with particularly
CC strong expression in mesodermal derivatives. Strongly expressed in
CC somites and also detected in limb bud mesenchyme, apical epidermal
CC ridge (AER), otic vesicle, and nephrogenic mesenchyme. Expression in
CC somites follows an anterior-to-posterior gradient of activation and
CC localizes to somite myotomes. In limbs, first detected at stage 10.5
CC dpc, probably in a subset of muscle precursor cells. Expression in
CC developing muscles continues during stage 14.5 dpc. Found in a subset
CC of tendon precursors, particularly in the distal region of the limb.
CC Also detected in ectoderm at the digit tips. Other notable sites of
CC expression at stage 11.5 dpc include skin epithelium in the posterior
CC embryo, thyroid rudiment, ventral neural tube, roof plate, floor plate,
CC dorsal aorta, sympathetic chain ganglia, endolymphatic duct, otic
CC vesicle epithelium and vascular wall. {ECO:0000269|PubMed:17693064}.
CC -!- DOMAIN: The CR1 and CR2 motifs mediate sequence-specific DNA binding,
CC and are important for binding to the MYOD1 enhancer.
CC {ECO:0000269|PubMed:17693064}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:17693064}.
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DR EMBL; AF292939; AAG34027.1; -; mRNA.
DR EMBL; BC052936; AAH52936.1; -; mRNA.
DR EMBL; AK078492; BAC37306.1; -; mRNA.
DR CCDS; CCDS17234.1; -.
DR RefSeq; NP_573481.1; NM_133218.2.
DR AlphaFoldDB; Q9ERQ3; -.
DR SMR; Q9ERQ3; -.
DR BioGRID; 228416; 2.
DR STRING; 10090.ENSMUSP00000041242; -.
DR iPTMnet; Q9ERQ3; -.
DR PhosphoSitePlus; Q9ERQ3; -.
DR PaxDb; Q9ERQ3; -.
DR PRIDE; Q9ERQ3; -.
DR ProteomicsDB; 275031; -.
DR Antibodypedia; 12438; 53 antibodies from 12 providers.
DR DNASU; 170753; -.
DR Ensembl; ENSMUST00000041124; ENSMUSP00000041242; ENSMUSG00000040209.
DR GeneID; 170753; -.
DR KEGG; mmu:170753; -.
DR UCSC; uc012cng.1; mouse.
DR CTD; 170753; -.
DR MGI; MGI:2180715; Zfp704.
DR VEuPathDB; HostDB:ENSMUSG00000040209; -.
DR eggNOG; ENOG502QW7P; Eukaryota.
DR GeneTree; ENSGT00940000156172; -.
DR InParanoid; Q9ERQ3; -.
DR OMA; RINSVVF; -.
DR OrthoDB; 915379at2759; -.
DR PhylomeDB; Q9ERQ3; -.
DR TreeFam; TF326610; -.
DR Reactome; R-MMU-212436; Generic Transcription Pathway.
DR BioGRID-ORCS; 170753; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Zfp704; mouse.
DR PRO; PR:Q9ERQ3; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9ERQ3; protein.
DR Bgee; ENSMUSG00000040209; Expressed in rostral migratory stream and 242 other tissues.
DR ExpressionAtlas; Q9ERQ3; baseline and differential.
DR Genevisible; Q9ERQ3; MM.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; 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:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..566
FT /note="Zinc finger protein 704"
FT /id="PRO_0000288825"
FT ZN_FING 346..371
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..566
FT /note="Sufficient for binding to RE2 sequence motifs"
FT /evidence="ECO:0000269|PubMed:17693064"
FT REGION 497..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 537..541
FT /note="CR1"
FT /evidence="ECO:0000269|PubMed:17693064"
FT MOTIF 555..559
FT /note="CR2"
FT /evidence="ECO:0000269|PubMed:17693064"
FT COMPBIAS 27..56
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..129
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MUTAGEN 537..541
FT /note="KKCRK->VALAL: Fails to bind to RE2 sequence motifs."
FT /evidence="ECO:0000269|PubMed:17693064"
FT MUTAGEN 555..559
FT /note="CRWKK->VALAL: Fails to bind to RE2 sequence motifs."
FT /evidence="ECO:0000269|PubMed:17693064"
SQ SEQUENCE 566 AA; 61150 MW; 25DCE20EC0180E64 CRC64;
MQARRLAKRP SLGSRRGGAA PAPAPEAAAL GLPPPGPSPA AAPGSWRPPL PPPRGTGPSR
AAAASSPVLL LLGEEDEDEE GAGRRRRTRG RVTEKPRGVA EEEDDDEEED EEVVVEVVDG
DEDDEDAEER FVPLGPGRAL PKGPARGAVK VGSFKREMTF TFQSEDFRRD SSKKPSHHLF
PLAMEEDVRT ADTKKTSRVL DQEKETRSVC LLEQKRKVVS SNIDVPPARK SSEELDMDKV
TAAMVLTSLS TSPLVRSPPV RPNEGLSGSW KEGAPSSSSS SGYWSWSAPS DQSNPSTPSP
PLSADSFKPF RSPAPPDDGI DEADASNLLF DEPIPRKRKN SMKVMFKCLW KSCGKVLNTA
AGIQKHIRAV HLGRVGESDC SDGEEDFYYT EIKLNTDATA EGLNTVAPVS PSQSLASAPA
FPIPDSSRTE TPCAKTDTKL VTPLSRSAPT TLYLVHTDHA YQATPPVTIP GSAKFTPNGS
SFSISWQSPP VTFTGVPVSP PHHPTAGSGE QRQHAHTALS SPPRGTVTLR KPRGEGKKCR
KVYGMENRDM WCTACRWKKA CQRFID
