ZC12C_MOUSE
ID ZC12C_MOUSE Reviewed; 884 AA.
AC Q5DTV4;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Probable ribonuclease ZC3H12C;
DE EC=3.1.-.-;
DE AltName: Full=Zinc finger CCCH domain-containing protein 12C;
GN Name=Zc3h12c; Synonyms=Kiaa1726;
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 272-884.
RC TISSUE=Brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP IDENTIFICATION, AND INDUCTION.
RX PubMed=18178554; DOI=10.1074/jbc.m707861200;
RA Liang J., Wang J., Azfer A., Song W., Tromp G., Kolattukudy P.E., Fu M.;
RT "A novel CCCH-zinc finger protein family regulates proinflammatory
RT activation of macrophages.";
RL J. Biol. Chem. 283:6337-6346(2008).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
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: May function as RNase and regulate the levels of target RNA
CC species. {ECO:0000305}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC -!- INDUCTION: By bacterial lipopolysaccharides (LPS) in macrophage cell
CC line RAW 264.7. {ECO:0000269|PubMed:18178554}.
CC -!- SIMILARITY: Belongs to the ZC3H12 family. {ECO:0000305}.
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DR EMBL; CT009732; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK220416; BAD90462.1; -; mRNA.
DR RefSeq; NP_001156393.1; NM_001162921.1.
DR RefSeq; XP_006510396.1; XM_006510333.2.
DR PDB; 7NDH; X-ray; 1.94 A; A/B=241-409.
DR PDB; 7NDI; X-ray; 2.88 A; A/B/C/D=242-406.
DR PDB; 7NDJ; X-ray; 1.65 A; A/B=243-434.
DR PDB; 7NDK; X-ray; 2.34 A; A/B/C/D=242-405.
DR PDBsum; 7NDH; -.
DR PDBsum; 7NDI; -.
DR PDBsum; 7NDJ; -.
DR PDBsum; 7NDK; -.
DR AlphaFoldDB; Q5DTV4; -.
DR SMR; Q5DTV4; -.
DR BioGRID; 232696; 5.
DR STRING; 10090.ENSMUSP00000127603; -.
DR iPTMnet; Q5DTV4; -.
DR PhosphoSitePlus; Q5DTV4; -.
DR MaxQB; Q5DTV4; -.
DR PaxDb; Q5DTV4; -.
DR PRIDE; Q5DTV4; -.
DR ProteomicsDB; 275130; -.
DR Antibodypedia; 45577; 57 antibodies from 22 providers.
DR Ensembl; ENSMUST00000213645; ENSMUSP00000150821; ENSMUSG00000035164.
DR GeneID; 244871; -.
DR KEGG; mmu:244871; -.
DR CTD; 85463; -.
DR MGI; MGI:3026959; Zc3h12c.
DR VEuPathDB; HostDB:ENSMUSG00000035164; -.
DR eggNOG; KOG3777; Eukaryota.
DR GeneTree; ENSGT00940000158397; -.
DR InParanoid; Q5DTV4; -.
DR OMA; RSPDCRY; -.
DR OrthoDB; 771251at2759; -.
DR PhylomeDB; Q5DTV4; -.
DR BioGRID-ORCS; 244871; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Zc3h12c; mouse.
DR PRO; PR:Q5DTV4; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q5DTV4; protein.
DR Bgee; ENSMUSG00000035164; Expressed in optic fissure and 232 other tissues.
DR ExpressionAtlas; Q5DTV4; baseline and differential.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004521; F:endoribonuclease activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IBA:GO_Central.
DR InterPro; IPR040546; Rege-1_UBA-like.
DR InterPro; IPR040757; Regnase_1/ZC3H12_C.
DR InterPro; IPR021869; RNase_Zc3h12_NYN.
DR InterPro; IPR000571; Znf_CCCH.
DR Pfam; PF18561; Regnase_1_C; 1.
DR Pfam; PF11977; RNase_Zc3h12a; 1.
DR Pfam; PF18039; UBA_6; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW Phosphoprotein; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..884
FT /note="Probable ribonuclease ZC3H12C"
FT /id="PRO_0000337844"
FT DOMAIN 246..401
FT /note="RNase NYN"
FT /evidence="ECO:0000255"
FT ZN_FING 411..436
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 66..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 755..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..513
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..770
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0D7"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:7NDI"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:7NDJ"
FT HELIX 253..259
FT /evidence="ECO:0007829|PDB:7NDJ"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:7NDJ"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:7NDJ"
FT HELIX 268..280
FT /evidence="ECO:0007829|PDB:7NDJ"
FT STRAND 286..291
FT /evidence="ECO:0007829|PDB:7NDJ"
FT HELIX 292..295
FT /evidence="ECO:0007829|PDB:7NDJ"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:7NDI"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:7NDJ"
FT HELIX 308..315
FT /evidence="ECO:0007829|PDB:7NDJ"
FT STRAND 318..322
FT /evidence="ECO:0007829|PDB:7NDJ"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:7NDJ"
FT STRAND 330..333
FT /evidence="ECO:0007829|PDB:7NDJ"
FT HELIX 336..346
FT /evidence="ECO:0007829|PDB:7NDJ"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:7NDJ"
FT HELIX 358..363
FT /evidence="ECO:0007829|PDB:7NDJ"
FT HELIX 365..374
FT /evidence="ECO:0007829|PDB:7NDJ"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:7NDJ"
FT STRAND 384..386
FT /evidence="ECO:0007829|PDB:7NDJ"
FT HELIX 399..402
FT /evidence="ECO:0007829|PDB:7NDJ"
FT STRAND 404..406
FT /evidence="ECO:0007829|PDB:7NDJ"
FT HELIX 412..414
FT /evidence="ECO:0007829|PDB:7NDJ"
FT HELIX 420..422
FT /evidence="ECO:0007829|PDB:7NDJ"
FT HELIX 426..428
FT /evidence="ECO:0007829|PDB:7NDJ"
SQ SEQUENCE 884 AA; 99430 MW; 9AB6E6E5236B4902 CRC64;
MAAEKTLQEY GVLCIQEYRK SSKVESSARN SFMGLKDHLG HDLGHLYMES TDPQMSAAVP
WPMVEKPTMD TVNSGKEGKG VSEENVSSGD SEGSTSSDHE SEQLSSLSVE PCSLTKTHRQ
LCRSPCLEPR LLKHSDILQD FKPEESQTPS KEVKKPPDVV REYQTKLEFA LKLGYSEEQV
QLVLNKLGTD ALINDILGEL VKLGNKSEAD QTVSTINSVM RETSSLESQR SESPMQEVVV
DDGENLRPVV IDGSNVAMSH GNKEVFSCRG IKLAVDWFLE RGHKDITVFV PAWRKEQSRP
DALITDQEIL RKLEKEKILV FTPSRRVQGR RVVCYDDRFI VKLAFESDGI IVSNDNYRDL
ANEKPEWKKF IDERLLMYSF VNDKFMPPDD PLGRHGPSLD NFLRKKPIVP EHKKQPCPYG
KKCTYGHKCK YYHPERGSQP QRSVADELRA MSRNTAAKTT NEGGLVKSNS VPCSTKADST
SDVKRGAPKR QSDPSIRTHV YQDIEEKLPT KNKLETRSVP SLVSIPATST AKPQSTTPLS
NGLPSGVHFP PQDQRPQGQY PPMMMATKNH GTPMPYEQYP KCDSPVDVGY YSMLNAYSNL
SISGPRSPER RFSLDTDYRV NSVASDCSSE GSMSCGSSDS YVGYNDRSYV SSPDPQLEES
LKCQHMHPHS RLNSQPFLQN FHDPLTRVQS YSHEEPKFHP KRPLPHLAMH LQHPAVGARS
SCPGDYPSPP SSAHSKAPHL GRSLVATRID SISDSRLYDS SPSRQRKPYS RQEGLGSWGR
PSYGLEAYGY RQTYSLPDNS TPPCYESITF QSLPEQQEPT WRIPYCGMPH DPPRYQDNRE
KIFINLCNIF PPDLVRLVMK RNPHMTDAQQ LAAAILVEKS QLGY
