ZIK1_MOUSE
ID ZIK1_MOUSE Reviewed; 463 AA.
AC Q80YP6; P70405;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Zinc finger protein interacting with ribonucleoprotein K;
GN Name=Zik1;
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], TISSUE SPECIFICITY, INTERACTION WITH HNRPK, AND
RP FUNCTION.
RC TISSUE=B-cell;
RX PubMed=8910362; DOI=10.1074/jbc.271.44.27701;
RA Denisenko O.N., O'Neill B., Ostrowski J., Van Seuningen I., Bomsztyk K.;
RT "Zik1, a transcriptional repressor that interacts with the heterogeneous
RT nuclear ribonucleoprotein particle K protein.";
RL J. Biol. Chem. 271:27701-27706(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Rathke gland;
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].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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).
CC -!- FUNCTION: May be a transcriptional repressor.
CC {ECO:0000269|PubMed:8910362}.
CC -!- SUBUNIT: Interacts with HNRPK. {ECO:0000269|PubMed:8910362}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in ovary and liver, and at lower levels
CC in brain and muscle. {ECO:0000269|PubMed:8910362}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; U69133; AAC52877.1; -; mRNA.
DR EMBL; AK146692; BAE27363.1; -; mRNA.
DR EMBL; AK159077; BAE34796.1; -; mRNA.
DR EMBL; BC050942; AAH50942.1; -; mRNA.
DR EMBL; BC067196; AAH67196.1; -; mRNA.
DR CCDS; CCDS20792.1; -.
DR RefSeq; NP_033603.2; NM_009577.3.
DR AlphaFoldDB; Q80YP6; -.
DR SMR; Q80YP6; -.
DR STRING; 10090.ENSMUSP00000032551; -.
DR iPTMnet; Q80YP6; -.
DR PhosphoSitePlus; Q80YP6; -.
DR MaxQB; Q80YP6; -.
DR PaxDb; Q80YP6; -.
DR PRIDE; Q80YP6; -.
DR ProteomicsDB; 299561; -.
DR Antibodypedia; 33273; 102 antibodies from 19 providers.
DR DNASU; 22775; -.
DR Ensembl; ENSMUST00000032551; ENSMUSP00000032551; ENSMUSG00000030393.
DR GeneID; 22775; -.
DR KEGG; mmu:22775; -.
DR UCSC; uc009fdf.1; mouse.
DR CTD; 284307; -.
DR MGI; MGI:108070; Zik1.
DR VEuPathDB; HostDB:ENSMUSG00000030393; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162907; -.
DR HOGENOM; CLU_002678_44_3_1; -.
DR InParanoid; Q80YP6; -.
DR OMA; WDVEKDL; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q80YP6; -.
DR TreeFam; TF339848; -.
DR Reactome; R-MMU-212436; Generic Transcription Pathway.
DR BioGRID-ORCS; 22775; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Zik1; mouse.
DR PRO; PR:Q80YP6; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q80YP6; protein.
DR Bgee; ENSMUSG00000030393; Expressed in otic placode and 222 other tissues.
DR Genevisible; Q80YP6; MM.
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: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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd07765; KRAB_A-box; 1.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 8.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 9.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 5.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
PE 1: Evidence at protein level;
KW DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..463
FT /note="Zinc finger protein interacting with
FT ribonucleoprotein K"
FT /id="PRO_0000286794"
FT DOMAIN 14..89
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 215..237
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 243..265
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 271..293
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 299..321
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 327..349
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 355..377
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 383..405
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 411..433
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 439..461
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 106..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 211
FT /note="G -> E (in Ref. 1; AAC52877)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 463 AA; 52727 MW; 019059C0D27F5365 CRC64;
MTAEMDMALM QGCVTFQDVA ICFSHEEWRL LDETQRLLYL SVMLQNFALI NSQGCGHKTE
DEERRVSTRA SKGLRSETTP KTNLCEKCVP ILQDILCLPG LPGQKHSTEA SSKVDQHQDH
NSTGKPLEKN ADRSSYLFYL SAKSFPSWDV EKDLPDILSL LKSQVCPKTK KYRKSTEGRK
ETSHESDKSE ECQSLSSQKQ TLAHHPKTSN GKKLYECSKC GKTFRGKYSL DQHQRVHTGE
RPWECRDCGK FFSQTSHLND HRRIHTGERP YECSECGKLF RQNSSLVDHQ KTHTGARPYE
CSQCGKSFSQ KATLVKHKRV HTGERPYKCS ECGNSFSQSA ILNQHRRIHT GVKPYECREC
GKSFSQKATL IKHQRVHTGE RPYKCSECGK SFSQSSILIQ HRRIHTGARP YECSQCGKSF
SQKSGLIQHQ VVHTGERPYE CDTCGNSFSQ CSSLIHHQKC HNA
