ZC3HF_MOUSE
ID ZC3HF_MOUSE Reviewed; 426 AA.
AC Q3TIV5; Q3TWQ0; Q3U855; Q8K2B6; Q8K346; Q9CVM4; Q9DAP2;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Zinc finger CCCH domain-containing protein 15;
DE AltName: Full=DRG family-regulatory protein 1;
DE AltName: Full=Epo-immediate response gene protein FM22;
GN Name=Zc3h15; Synonyms=Dfrp1;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Pancreas, Placenta, and Testis;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and Czech II;
RC TISSUE=Mammary tumor, and Olfactory epithelium;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-337 (ISOFORM 2), TISSUE SPECIFICITY, AND
RP INDUCTION BY EPO.
RX PubMed=10880228; DOI=10.1006/cyto.2000.0686;
RA Gregory R.C. Jr., Lord K.A., Panek L.B., Gaines P., Dillon S.B.,
RA Wojchowski D.M.;
RT "Subtraction cloning and initial characterization of novel EPO-immediate
RT response genes.";
RL Cytokine 12:845-857(2000).
RN [5]
RP INTERACTION WITH DRG1, AND FUNCTION.
RX PubMed=15676025; DOI=10.1111/j.1365-2443.2005.00825.x;
RA Ishikawa K., Azuma S., Ikawa S., Semba K., Inoue J.;
RT "Identification of DRG family regulatory proteins (DFRPs): specific
RT regulation of DRG1 and DRG2.";
RL Genes Cells 10:139-150(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen, and
RC Testis;
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: Protects DRG1 from proteolytic degradation (PubMed:15676025).
CC Stimulates DRG1 GTPase activity likely by increasing the affinity for
CC the potassium ions (By similarity). {ECO:0000250|UniProtKB:Q8WU90,
CC ECO:0000269|PubMed:15676025}.
CC -!- SUBUNIT: Interacts with DRG1; the interaction forms a polysomal DRG1-
CC DFRP1/ZC3H15 complex which provides protein stability to DRG1 possibly
CC by blocking poly-ubiquitination (PubMed:15676025). Associates with
CC microtubules (By similarity). {ECO:0000250|UniProtKB:Q8WU90,
CC ECO:0000269|PubMed:15676025}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus
CC {ECO:0000250|UniProtKB:Q8WU90}. Note=The DRG1-DFRP2/ZC3H15 complex
CC associates with polysomes. {ECO:0000250|UniProtKB:Q8WU90}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q3TIV5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3TIV5-2; Sequence=VSP_032341;
CC Name=3;
CC IsoId=Q3TIV5-3; Sequence=VSP_032342, VSP_032343;
CC -!- INDUCTION: By erythropoietin. {ECO:0000269|PubMed:10880228}.
CC -!- SIMILARITY: Belongs to the ZC3H15/TMA46 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE31164.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK005661; BAB24173.1; -; mRNA.
DR EMBL; AK007452; BAB25047.1; -; mRNA.
DR EMBL; AK152374; BAE31164.1; ALT_FRAME; mRNA.
DR EMBL; AK159596; BAE35216.1; -; mRNA.
DR EMBL; AK167696; BAE39741.1; -; mRNA.
DR EMBL; AL772301; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX294652; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC028787; AAH28787.1; -; mRNA.
DR EMBL; BC031845; AAH31845.1; -; mRNA.
DR EMBL; BC058229; AAH58229.1; -; mRNA.
DR EMBL; AF221851; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS16180.1; -. [Q3TIV5-1]
DR RefSeq; NP_081210.2; NM_026934.3. [Q3TIV5-1]
DR AlphaFoldDB; Q3TIV5; -.
DR SMR; Q3TIV5; -.
DR BioGRID; 213217; 8.
DR IntAct; Q3TIV5; 1.
DR MINT; Q3TIV5; -.
DR STRING; 10090.ENSMUSP00000080301; -.
DR iPTMnet; Q3TIV5; -.
DR PhosphoSitePlus; Q3TIV5; -.
DR EPD; Q3TIV5; -.
DR jPOST; Q3TIV5; -.
DR MaxQB; Q3TIV5; -.
DR PaxDb; Q3TIV5; -.
DR PeptideAtlas; Q3TIV5; -.
DR PRIDE; Q3TIV5; -.
DR ProteomicsDB; 302111; -. [Q3TIV5-1]
DR ProteomicsDB; 302112; -. [Q3TIV5-2]
DR ProteomicsDB; 302113; -. [Q3TIV5-3]
DR Antibodypedia; 34002; 129 antibodies from 23 providers.
DR DNASU; 69082; -.
DR Ensembl; ENSMUST00000081591; ENSMUSP00000080301; ENSMUSG00000027091. [Q3TIV5-1]
DR GeneID; 69082; -.
DR KEGG; mmu:69082; -.
DR UCSC; uc008khx.1; mouse. [Q3TIV5-3]
DR UCSC; uc008khy.1; mouse. [Q3TIV5-1]
DR CTD; 55854; -.
DR MGI; MGI:1919747; Zc3h15.
DR VEuPathDB; HostDB:ENSMUSG00000027091; -.
DR eggNOG; KOG1763; Eukaryota.
DR GeneTree; ENSGT00390000015818; -.
DR HOGENOM; CLU_042870_3_0_1; -.
DR InParanoid; Q3TIV5; -.
DR OMA; DGPMEEG; -.
DR OrthoDB; 1358374at2759; -.
DR PhylomeDB; Q3TIV5; -.
DR TreeFam; TF300892; -.
DR BioGRID-ORCS; 69082; 6 hits in 74 CRISPR screens.
DR ChiTaRS; Zc3h15; mouse.
DR PRO; PR:Q3TIV5; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q3TIV5; protein.
DR Bgee; ENSMUSG00000027091; Expressed in rostral migratory stream and 262 other tissues.
DR Genevisible; Q3TIV5; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:MGI.
DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:MGI.
DR InterPro; IPR032378; ZC3H15/TMA46_C.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR Pfam; PF16543; DFRP_C; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR SMART; SM00356; ZnF_C3H1; 2.
DR SUPFAM; SSF90229; SSF90229; 1.
DR PROSITE; PS50103; ZF_C3H1; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..426
FT /note="Zinc finger CCCH domain-containing protein 15"
FT /id="PRO_0000324643"
FT ZN_FING 99..126
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 174..212
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..260
FT /note="Required for interaction with DRG1"
FT /evidence="ECO:0000269|PubMed:15676025"
FT REGION 303..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 61..86
FT /evidence="ECO:0000255"
FT COILED 218..285
FT /evidence="ECO:0000255"
FT COMPBIAS 11..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..426
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WU90"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WU90"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WU90"
FT VAR_SEQ 1..205
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10880228,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_032341"
FT VAR_SEQ 148..151
FT /note="DTMD -> GISS (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_032342"
FT VAR_SEQ 152..426
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_032343"
FT CONFLICT 142
FT /note="D -> E (in Ref. 1; BAE35216)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="L -> P (in Ref. 1; BAE39741)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="D -> G (in Ref. 4; AF221851)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 426 AA; 48327 MW; FB926F87899E9FA9 CRC64;
MPPKKQAQAG GSKKAEQKKK EKIIEDKTFG LKNKKGAKQQ KFIKAVTHQV KFGQQNPRQV
AQSEAEKKLK KDDKKKELQE LNELFKPVVA AQKISKGADP KSVVCAFFKQ GQCTKGDKCK
FSHDLTLERK CEKRSVYIDA RDEELEKDTM DNWDEKKLEE VVNKKHGEAE KKKPKTQIVC
RHFLEAIENN KYGWFWVCPG GGDNCMYRHA LPPGFVLKKD KKKEEKEDEI SLEDLIERER
SALGPNVTKI TLESFLAWKK RKRQEKIDKL EQDMERRKAD FKAGKALVIS GREVFEFRPE
LVNDDDEEAD DTRYIQGTGG DEVDDSMGVN DIDISLYVPR DVEETGITVA SVERFSTYAP
DKDENKLSEA SGGLAENGER SDLDEDSGGG GQENGSIDAV PVDENLFTGE DLDELEEELN
TLDLEE
