ZN692_MOUSE
ID ZN692_MOUSE Reviewed; 531 AA.
AC Q3U381;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Zinc finger protein 692 {ECO:0000305};
DE AltName: Full=AICAR responsive element binding protein {ECO:0000250|UniProtKB:Q9BU19};
GN Name=Znf692 {ECO:0000250|UniProtKB:Q9BU19};
GN Synonyms=AREBP {ECO:0000250|UniProtKB:Q9BU19},
GN Zfp692 {ECO:0000312|MGI:MGI:2144276};
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 STRAIN=NOD;
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).
CC -!- FUNCTION: May act as an transcriptional repressor for PCK1 gene
CC expression, in turn may participate in the hepatic gluconeogenesis
CC regulation through the activated AMPK signaling pathway.
CC {ECO:0000250|UniProtKB:Q9BU19}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BU19}.
CC -!- PTM: Phosphorylation at Ser-469 results in loss of DNA-binding
CC activity. {ECO:0000250|UniProtKB:Q9BU19}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AK154896; BAE32908.1; -; mRNA.
DR CCDS; CCDS36162.1; -.
DR RefSeq; NP_001035776.1; NM_001040686.1.
DR RefSeq; NP_892041.2; NM_182996.3.
DR AlphaFoldDB; Q3U381; -.
DR SMR; Q3U381; -.
DR STRING; 10090.ENSMUSP00000131896; -.
DR iPTMnet; Q3U381; -.
DR PhosphoSitePlus; Q3U381; -.
DR MaxQB; Q3U381; -.
DR PaxDb; Q3U381; -.
DR PRIDE; Q3U381; -.
DR ProteomicsDB; 302094; -.
DR Antibodypedia; 54395; 45 antibodies from 15 providers.
DR Ensembl; ENSMUST00000049353; ENSMUSP00000131896; ENSMUSG00000037243.
DR Ensembl; ENSMUST00000153510; ENSMUSP00000126674; ENSMUSG00000037243.
DR GeneID; 103836; -.
DR KEGG; mmu:103836; -.
DR UCSC; uc007jaw.1; mouse.
DR CTD; 103836; -.
DR MGI; MGI:2144276; Zfp692.
DR VEuPathDB; HostDB:ENSMUSG00000037243; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161175; -.
DR HOGENOM; CLU_045687_1_0_1; -.
DR InParanoid; Q3U381; -.
DR OMA; CHAHSRE; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q3U381; -.
DR TreeFam; TF332664; -.
DR BioGRID-ORCS; 103836; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Zfp692; mouse.
DR PRO; PR:Q3U381; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q3U381; protein.
DR Bgee; ENSMUSG00000037243; Expressed in retinal neural layer and 240 other tissues.
DR Genevisible; Q3U381; MM.
DR GO; GO:0005694; C:chromosome; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0043035; F:chromatin insulator sequence binding; 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:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006111; P:regulation of gluconeogenesis; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 2.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE 2: Evidence at transcript level;
KW DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..531
FT /note="Zinc finger protein 692"
FT /id="PRO_0000234015"
FT ZN_FING 327..352
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 358..382
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 388..410
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 416..438
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 447..470
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 155..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..207
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BU19"
FT MOD_RES 469
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BU19"
SQ SEQUENCE 531 AA; 59010 MW; A1B3E57EF9C15C21 CRC64;
MASPVADASR RRREKRRQLD ARRSKCRIRL GGHMEQWCLL KERLGFSLHS QLAKFLLDRY
TSSGCVLCAA PEPGPRKGLQ YLVLLSHTHS RECGLVPGLR GPGGGEGELV WECSAGHTFS
WEPSLIPAPS DVPKQAPLTH TTERAWCSEA RRKQEAQGLE CEQRERTQET RLSRRVDSPL
EIDPPLGEDQ DVEEEEEEEE EEEELLSDAS PWTYSSSPDD SEPDVPRPPP SPVTHTPKEG
EVSPVPATLP TPCAVLASVG SPDALTSDTE VRLELSRTPQ VPAELHMTES LESPGSQAQS
APNPTWDEDT AQIGLRRIRK AAKRELMPCD FPGCGRIFSN RQYLNHHKKY QHIHQKSFCC
PEPACGKSFN FKKHLKEHVK LHSDTRDYIC EFCARSFRTS SNLVIHRRIH TGEKPLQCEI
CGFTCRQKAS LNWHRRKHAE TAAALRFPCE FCGKRFEKPD SVVAHCSKSH PALLPAQEPP
GSLVSSPSIS APESLQSPEG ASISTTSDSN PASSTSISSP GVPDPRNREK S
