ZFP2_MOUSE
ID ZFP2_MOUSE Reviewed; 459 AA.
AC P08043; Q3V280; Q8R012;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Zinc finger protein ZFP2;
DE Short=Zfp-2;
DE AltName: Full=Protein mKR2;
GN Name=Zfp2; Synonyms=Fnp-2, Mkr2, Zfp-2;
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] (ISOFORM 2).
RX PubMed=3409867; DOI=10.1002/j.1460-2075.1988.tb02950.x;
RA Chowdhury K., Dressler G., Dreier G., Deutsch U., Gruss P.;
RT "The primary structure of the murine multifinger gene mKr2 and its specific
RT expression in developing and adult neurons.";
RL EMBO J. 7:1345-1353(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=ILS, and ISS;
RX PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT "High-throughput sequence identification of gene coding variants within
RT alcohol-related QTLs.";
RL Mamm. Genome 12:657-663(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo, Spinal cord, and Vagina;
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 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Pituitary;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 75-459 (ISOFORM 2).
RX PubMed=3815523; DOI=10.1016/0092-8674(87)90074-2;
RA Chowdhury K., Deutsch U., Gruss P.;
RT "A multigene family encoding several 'finger' structures is present and
RT differentially active in mammalian genomes.";
RL Cell 48:771-778(1987).
CC -!- FUNCTION: Probable transcription factor involved in neuronal
CC differentiation and/or phenotypic maintenance.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P08043-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P08043-2; Sequence=VSP_026332;
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE20918.1; Type=Frameshift; 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; Y00850; CAA68768.1; -; mRNA.
DR EMBL; AF483520; AAL90794.1; -; mRNA.
DR EMBL; AF483521; AAL90795.1; -; mRNA.
DR EMBL; AK036776; BAC29572.1; -; mRNA.
DR EMBL; AK131978; BAE20918.1; ALT_FRAME; mRNA.
DR EMBL; AK141471; BAE24694.1; -; mRNA.
DR EMBL; AL627215; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC089506; AAH89506.1; -; mRNA.
DR EMBL; M15709; AAA37640.1; -; Genomic_DNA.
DR CCDS; CCDS36148.1; -. [P08043-1]
DR PIR; S00549; S00549.
DR RefSeq; NP_001038162.1; NM_001044697.2. [P08043-1]
DR RefSeq; NP_001038163.1; NM_001044698.2. [P08043-1]
DR RefSeq; NP_001038165.1; NM_001044700.2. [P08043-1]
DR RefSeq; NP_001281252.1; NM_001294323.1. [P08043-1]
DR RefSeq; NP_848542.1; NM_178447.3. [P08043-1]
DR RefSeq; XP_017169995.1; XM_017314506.1. [P08043-1]
DR AlphaFoldDB; P08043; -.
DR SMR; P08043; -.
DR BioGRID; 204647; 1.
DR STRING; 10090.ENSMUSP00000112079; -.
DR iPTMnet; P08043; -.
DR PhosphoSitePlus; P08043; -.
DR PaxDb; P08043; -.
DR PRIDE; P08043; -.
DR ProteomicsDB; 275355; -. [P08043-1]
DR ProteomicsDB; 275356; -. [P08043-2]
DR Antibodypedia; 29457; 47 antibodies from 17 providers.
DR DNASU; 22678; -.
DR Ensembl; ENSMUST00000109128; ENSMUSP00000104756; ENSMUSG00000049321. [P08043-1]
DR Ensembl; ENSMUST00000109129; ENSMUSP00000104757; ENSMUSG00000049321. [P08043-1]
DR Ensembl; ENSMUST00000116378; ENSMUSP00000112079; ENSMUSG00000049321. [P08043-1]
DR GeneID; 22678; -.
DR KEGG; mmu:22678; -.
DR UCSC; uc007isy.2; mouse. [P08043-1]
DR CTD; 80108; -.
DR MGI; MGI:99167; Zfp2.
DR VEuPathDB; HostDB:ENSMUSG00000049321; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162743; -.
DR HOGENOM; CLU_002678_44_0_1; -.
DR InParanoid; P08043; -.
DR OMA; TERRVCG; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; P08043; -.
DR TreeFam; TF350858; -.
DR BioGRID-ORCS; 22678; 2 hits in 71 CRISPR screens.
DR PRO; PR:P08043; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P08043; protein.
DR Bgee; ENSMUSG00000049321; Expressed in inferior glossopharyngeal IX ganglion and 232 other tissues.
DR Genevisible; P08043; MM.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0000977; F:RNA polymerase II transcription 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 InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 13.
DR SMART; SM00355; ZnF_C2H2; 13.
DR SUPFAM; SSF57667; SSF57667; 7.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 13.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 13.
PE 2: Evidence at transcript level;
KW Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..459
FT /note="Zinc finger protein ZFP2"
FT /id="PRO_0000047282"
FT ZN_FING 100..122
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 128..150
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 156..178
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 184..206
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 212..234
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 240..262
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 268..290
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 296..318
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 324..346
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 352..374
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 380..402
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 408..430
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 436..458
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT VAR_SEQ 217..328
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:3409867"
FT /id="VSP_026332"
FT CONFLICT 136
FT /note="H -> Q (in Ref. 3; BAE20918)"
FT /evidence="ECO:0000305"
FT CONFLICT 399
FT /note="Q -> R (in Ref. 1; CAA68768 and 6; AAA37640)"
FT /evidence="ECO:0000305"
FT CONFLICT 436
FT /note="Y -> N (in Ref. 3; BAE20918)"
FT /evidence="ECO:0000305"
FT CONFLICT 444
FT /note="S -> P (in Ref. 1; CAA68768 and 6; AAA37640)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 459 AA; 52534 MW; 1211EBD2828F9284 CRC64;
MDREDLWHSA LGAVWDPTCW LKGQQERYLG QVTVAQKEIY NEKSVCGGNT TENSSTEGSM
LNTPQSIPVT PCNWNSYRKD SKQNSELMKT SRMFVQKKVY GCDECGKTFR QSSSLLKHQR
IHTGEKPYTC NVCDKHFIER SSLTVHQRTH TGEKPYKCHE CGKAFSQSMN LTVHQRTHTG
EKPYQCKECG KAFRKNSSLI QHERIHTGEK PYKCHDCGKA FTQSMNLTVH QRTHTGEKPY
ECNQCGKAFS QSMHLIVHQR SHTGEKPYEC SECGKAFSKS STLTLHQRNH TGEKPYKCNK
CGKSFSQSTY LIEHQRLHSG VKPFECNQCG KAFSKNSSLT QHRRIHTGEK PYECMICGKH
FTGRSSLTVH QVIHTGEKPY ECTECGKAFS QSAYLIEHQR IHTGEKPYEC DQCGKAFIKN
SSLIVHQRIH TGEKPYQCNE CGKSFSRSTN LTRHQRTHT