ID   ZC3HF_RAT               Reviewed;         426 AA.
AC   Q6U6G5;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Zinc finger CCCH domain-containing protein 15;
DE   AltName: Full=p48ZnF;
GN   Name=Zc3h15;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP   INDUCTION BY NGF.
RC   TISSUE=Brain;
RX   PubMed=15150441; DOI=10.1038/emm.2004.19;
RA   Heese K., Nagai Y., Sawada T.;
RT   "Nerve growth factor (NGF) induces mRNA expression of the new transcription
RT   factor protein p48ZnF.";
RL   Exp. Mol. Med. 36:130-134(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Protects DRG1 from proteolytic degradation. Stimulates DRG1
CC       GTPase activity likely by increasing the affinity for the potassium
CC       ions. {ECO:0000250|UniProtKB:Q8WU90}.
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. Associates with microtubules.
CC       {ECO:0000250|UniProtKB:Q8WU90}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15150441}. Nucleus
CC       {ECO:0000269|PubMed:15150441}. Note=The DRG1-DFRP2/ZC3H15 complex
CC       associates with polysomes. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC       {ECO:0000269|PubMed:15150441}.
CC   -!- INDUCTION: By NGF in neuronal cells. {ECO:0000269|PubMed:15150441}.
CC   -!- SIMILARITY: Belongs to the ZC3H15/TMA46 family. {ECO:0000305}.
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DR   EMBL; BC088438; AAH88438.1; -; mRNA.
DR   EMBL; AY377983; AAR24540.1; -; mRNA.
DR   RefSeq; NP_001010963.1; NM_001010963.1.
DR   AlphaFoldDB; Q6U6G5; -.
DR   SMR; Q6U6G5; -.
DR   STRING; 10116.ENSRNOP00000007276; -.
DR   iPTMnet; Q6U6G5; -.
DR   PhosphoSitePlus; Q6U6G5; -.
DR   jPOST; Q6U6G5; -.
DR   PaxDb; Q6U6G5; -.
DR   PRIDE; Q6U6G5; -.
DR   Ensembl; ENSRNOT00000007276; ENSRNOP00000007276; ENSRNOG00000005256.
DR   GeneID; 362154; -.
DR   KEGG; rno:362154; -.
DR   UCSC; RGD:1359234; rat.
DR   CTD; 55854; -.
DR   RGD; 1359234; Zc3h15.
DR   eggNOG; KOG1763; Eukaryota.
DR   GeneTree; ENSGT00390000015818; -.
DR   HOGENOM; CLU_042870_3_0_1; -.
DR   InParanoid; Q6U6G5; -.
DR   OMA; DGPMEEG; -.
DR   OrthoDB; 1358374at2759; -.
DR   PhylomeDB; Q6U6G5; -.
DR   TreeFam; TF300892; -.
DR   PRO; PR:Q6U6G5; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   Bgee; ENSRNOG00000005256; Expressed in testis and 19 other tissues.
DR   Genevisible; Q6U6G5; RN.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; ISO:RGD.
DR   GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; ISO:RGD.
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   Coiled coil; Cytoplasm; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Zinc; Zinc-finger.
FT   CHAIN           1..426
FT                   /note="Zinc finger CCCH domain-containing protein 15"
FT                   /id="PRO_0000324644"
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:0000250"
FT   REGION          302..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          359..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:0007744|PubMed:22673903"
FT   MOD_RES         351
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WU90"
FT   MOD_RES         360
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WU90"
FT   MOD_RES         381
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WU90"
SQ   SEQUENCE   426 AA;  48299 MW;  E094B6DEAF90B28A 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 DEVDDSVGVN DIDLSLYVPR DVEETGITVA SLERFSTYAS
     DKDENKLSEA SGGLAENGER SDLDEDSGGG GQENGSIDAV PVDENLFTGE DLDELEEELN
     TLDLEE