ZN367_MOUSE
ID ZN367_MOUSE Reviewed; 340 AA.
AC Q0VDT2; B1B191; B1B192; Q8BH90; Q8BI44; Q8BI88;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Zinc finger protein 367;
DE AltName: Full=C2H2 zinc finger protein ZFF29;
GN Name=Znf367; Synonyms=Zff29, Zfp367;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Lung, Testis, 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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP PROTEIN SEQUENCE OF 244-252, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Fetal liver;
RX PubMed=15344908; DOI=10.1042/bj20040394;
RA Asano H., Murate T., Naoe T., Saito H., Stamatoyannopoulos G.;
RT "Molecular cloning and characterization of ZFF29: a protein containing a
RT unique Cys2His2 zinc-finger motif.";
RL Biochem. J. 384:647-653(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
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: Transcriptional activator. Isoform 1 may be involved in
CC transcriptional activation of erythroid genes (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Zff29B;
CC IsoId=Q0VDT2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q0VDT2-2; Sequence=VSP_024866;
CC -!- TISSUE SPECIFICITY: Expressed in bone marrow and ovary.
CC {ECO:0000269|PubMed:15344908}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in fetal erythroid tissue. Lower
CC expression in yolk sac. {ECO:0000269|PubMed:15344908}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC39364.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK033288; BAC28224.1; -; mRNA.
DR EMBL; AK041331; BAC30909.1; -; mRNA.
DR EMBL; AK041361; BAC30919.1; -; mRNA.
DR EMBL; AK085094; BAC39364.1; ALT_INIT; mRNA.
DR EMBL; AC158990; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT009717; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC119531; AAI19532.1; -; mRNA.
DR EMBL; BC119532; AAI19533.1; -; mRNA.
DR CCDS; CCDS26596.1; -. [Q0VDT2-1]
DR RefSeq; NP_780703.1; NM_175494.4. [Q0VDT2-1]
DR AlphaFoldDB; Q0VDT2; -.
DR SMR; Q0VDT2; -.
DR STRING; 10090.ENSMUSP00000050854; -.
DR iPTMnet; Q0VDT2; -.
DR PhosphoSitePlus; Q0VDT2; -.
DR EPD; Q0VDT2; -.
DR PaxDb; Q0VDT2; -.
DR PRIDE; Q0VDT2; -.
DR ProteomicsDB; 299576; -. [Q0VDT2-1]
DR ProteomicsDB; 299577; -. [Q0VDT2-2]
DR Antibodypedia; 14186; 99 antibodies from 17 providers.
DR DNASU; 238673; -.
DR Ensembl; ENSMUST00000059817; ENSMUSP00000050854; ENSMUSG00000044934. [Q0VDT2-1]
DR Ensembl; ENSMUST00000117241; ENSMUSP00000113331; ENSMUSG00000044934. [Q0VDT2-2]
DR GeneID; 238673; -.
DR KEGG; mmu:238673; -.
DR UCSC; uc007qyj.1; mouse. [Q0VDT2-1]
DR CTD; 238673; -.
DR MGI; MGI:2442266; Zfp367.
DR VEuPathDB; HostDB:ENSMUSG00000044934; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00670000098074; -.
DR HOGENOM; CLU_068261_0_0_1; -.
DR InParanoid; Q0VDT2; -.
DR OMA; NKHPHVI; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q0VDT2; -.
DR TreeFam; TF321334; -.
DR BioGRID-ORCS; 238673; 6 hits in 77 CRISPR screens.
DR ChiTaRS; Zfp367; mouse.
DR PRO; PR:Q0VDT2; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q0VDT2; protein.
DR Bgee; ENSMUSG00000044934; Expressed in spermatocyte and 219 other tissues.
DR Genevisible; Q0VDT2; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:MGI.
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; ISO:MGI.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 1.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Coiled coil; Direct protein sequencing;
KW DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..340
FT /note="Zinc finger protein 367"
FT /id="PRO_0000285298"
FT ZN_FING 157..179
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 185..209
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 101..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 299..332
FT /evidence="ECO:0000255"
FT COMPBIAS 121..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 268..340
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024866"
FT CONFLICT 5
FT /note="A -> V (in Ref. 3; AAI19533/AAI19532)"
FT /evidence="ECO:0000305"
FT CONFLICT 16
FT /note="V -> I (in Ref. 3; AAI19533/AAI19532)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 340 AA; 37453 MW; 3F64E33395B7064C CRC64;
MIRGAPAPMA EPPPVVFCHD SPKRVLVSVI RTTPATPPCS SVGEPEPPPP LVPTSPGFSD
FMVYPWRWGE NAHNVTLSPG AAGGVVSAGL PVAAELPTLR GAPQSSASVA AVSGGEDEEE
ASSPDSGHLK DGIRRGRPRA DTVRDLINEG EHSSSRIRCN ICNRVFPREK SLQAHKRTHT
GERPYLCDYP DCGKAFVQSG QLKTHQRLHT GEKPFVCSEN GCLSRFTHAN RHCPKHPYAR
LKREEPTDAL SKHQSPDNKA AAEWLAKYWE MREQRTPTLK GKLVQKADQE QQDPLEYLQS
DEEDDEKSGA QRRLQEQRER LHGALALIEL ANLTGAPLRQ
