ID   ZC3HF_BOVIN             Reviewed;         426 AA.
AC   Q1RMM1;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Zinc finger CCCH domain-containing protein 15;
GN   Name=ZC3H15;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Protects DRG1 from proteolytic degradation. {ECO:0000250}.
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC       Note=The DRG1-DFRP2/ZC3H15 complex associates with polysomes.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ZC3H15/TMA46 family. {ECO:0000305}.
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DR   EMBL; BC114825; AAI14826.1; -; mRNA.
DR   RefSeq; NP_001039859.1; NM_001046394.2.
DR   AlphaFoldDB; Q1RMM1; -.
DR   SMR; Q1RMM1; -.
DR   STRING; 9913.ENSBTAP00000029007; -.
DR   PaxDb; Q1RMM1; -.
DR   PeptideAtlas; Q1RMM1; -.
DR   PRIDE; Q1RMM1; -.
DR   Ensembl; ENSBTAT00000029007; ENSBTAP00000029007; ENSBTAG00000021762.
DR   GeneID; 535102; -.
DR   KEGG; bta:535102; -.
DR   CTD; 55854; -.
DR   VEuPathDB; HostDB:ENSBTAG00000021762; -.
DR   VGNC; VGNC:37103; ZC3H15.
DR   eggNOG; KOG1763; Eukaryota.
DR   GeneTree; ENSGT00390000015818; -.
DR   HOGENOM; CLU_042870_3_0_1; -.
DR   InParanoid; Q1RMM1; -.
DR   OMA; DGPMEEG; -.
DR   OrthoDB; 1358374at2759; -.
DR   TreeFam; TF300892; -.
DR   Proteomes; UP000009136; Chromosome 2.
DR   Bgee; ENSBTAG00000021762; Expressed in surface of tongue and 104 other tissues.
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:0002181; P:cytoplasmic translation; IBA:GO_Central.
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   2: Evidence at transcript 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_0000324641"
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          299..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          358..411
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        358..381
FT                   /note="Basic and 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         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;  48527 MW;  63A3CBCE16E1631A CRC64;
     MPPKKQAQAG GSKKAEQKKK EKIIEDKTFG LKNKKGAKQQ KFIKAVTHQV KFGQQNPRQV
     AQSEAEKKLK KDDKKKELQE LNELFKPVVA AQKISKGADP KSVVCAFFKQ GQCTKGDKCK
     FSHDLTLERK CEKRSVYIDA RDEELEKDTM DNWDEKKLEE VVNKKHGEAE KKKPKTQIVC
     KHFLEAIENN KYGWFWVCPG GGDICMYRHA LPPGFVLKKD KKKEEKEDEI SLEDLIERER
     SALGPNVTKI TLESFLAWKK RKRQEKIDKL EQDIERRKAD FKAGKALVIS GREVFEFRPE
     LVDDDDEEAD DTRYTQGTGG DEVDDSVSVN DIDLSLYIPR DVDETGITVA SLERFSTYTS
     EKDENKLSEA SGGRAENGER SDLEEDNEGE GQENGAIDAV PVDENLFTGE DLDELEEELN
     TLDLEE