ZC12C_HUMAN
ID ZC12C_HUMAN Reviewed; 883 AA.
AC Q9C0D7; B4DI65; B4DR47;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Probable ribonuclease ZC3H12C;
DE EC=3.1.-.-;
DE AltName: Full=MCP-induced protein 3;
DE AltName: Full=Zinc finger CCCH domain-containing protein 12C;
GN Name=ZC3H12C; Synonyms=KIAA1726, MCPIP3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Corpus callosum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 260-883 (ISOFORM 1/2).
RC TISSUE=Brain;
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [4]
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
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 -!- INTERACTION:
CC Q9C0D7; Q9BUZ4: TRAF4; NbExp=3; IntAct=EBI-2857430, EBI-3650647;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9C0D7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C0D7-2; Sequence=VSP_054127;
CC -!- INDUCTION: By cytokines (TNF-alpha and interleukin-1) in acute
CC monocytic leukemia cell line THP-1 cells.
CC {ECO:0000269|PubMed:18178554}.
CC -!- SIMILARITY: Belongs to the ZC3H12 family. {ECO:0000305}.
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DR EMBL; AK295437; BAG58377.1; -; mRNA.
DR EMBL; AK299100; BAG61159.1; -; mRNA.
DR EMBL; AP000901; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP001889; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB051513; BAB21817.1; -; mRNA.
DR CCDS; CCDS44727.1; -. [Q9C0D7-1]
DR RefSeq; NP_203748.1; NM_033390.1. [Q9C0D7-1]
DR RefSeq; XP_016873966.1; XM_017018477.1. [Q9C0D7-2]
DR AlphaFoldDB; Q9C0D7; -.
DR SMR; Q9C0D7; -.
DR BioGRID; 124547; 10.
DR IntAct; Q9C0D7; 4.
DR STRING; 9606.ENSP00000278590; -.
DR GlyGen; Q9C0D7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9C0D7; -.
DR PhosphoSitePlus; Q9C0D7; -.
DR BioMuta; ZC3H12C; -.
DR DMDM; 190485746; -.
DR EPD; Q9C0D7; -.
DR jPOST; Q9C0D7; -.
DR MassIVE; Q9C0D7; -.
DR MaxQB; Q9C0D7; -.
DR PaxDb; Q9C0D7; -.
DR PeptideAtlas; Q9C0D7; -.
DR PRIDE; Q9C0D7; -.
DR ProteomicsDB; 4923; -.
DR ProteomicsDB; 80017; -. [Q9C0D7-1]
DR Antibodypedia; 45577; 57 antibodies from 22 providers.
DR DNASU; 85463; -.
DR Ensembl; ENST00000278590.8; ENSP00000278590.3; ENSG00000149289.11. [Q9C0D7-1]
DR Ensembl; ENST00000528673.5; ENSP00000431821.1; ENSG00000149289.11. [Q9C0D7-2]
DR GeneID; 85463; -.
DR KEGG; hsa:85463; -.
DR MANE-Select; ENST00000278590.8; ENSP00000278590.3; NM_033390.2; NP_203748.1.
DR UCSC; uc009yxw.3; human. [Q9C0D7-1]
DR CTD; 85463; -.
DR DisGeNET; 85463; -.
DR GeneCards; ZC3H12C; -.
DR HGNC; HGNC:29362; ZC3H12C.
DR HPA; ENSG00000149289; Low tissue specificity.
DR MIM; 615001; gene.
DR neXtProt; NX_Q9C0D7; -.
DR OpenTargets; ENSG00000149289; -.
DR PharmGKB; PA128394739; -.
DR VEuPathDB; HostDB:ENSG00000149289; -.
DR eggNOG; KOG3777; Eukaryota.
DR GeneTree; ENSGT00940000158397; -.
DR InParanoid; Q9C0D7; -.
DR OMA; RSPDCRY; -.
DR OrthoDB; 771251at2759; -.
DR PhylomeDB; Q9C0D7; -.
DR TreeFam; TF315783; -.
DR PathwayCommons; Q9C0D7; -.
DR SignaLink; Q9C0D7; -.
DR BioGRID-ORCS; 85463; 7 hits in 1069 CRISPR screens.
DR ChiTaRS; ZC3H12C; human.
DR GenomeRNAi; 85463; -.
DR Pharos; Q9C0D7; Tdark.
DR PRO; PR:Q9C0D7; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9C0D7; protein.
DR Bgee; ENSG00000149289; Expressed in tibialis anterior and 178 other tissues.
DR ExpressionAtlas; Q9C0D7; baseline and differential.
DR Genevisible; Q9C0D7; HS.
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 Alternative splicing; Endonuclease; Hydrolase; Magnesium; Metal-binding;
KW Nuclease; Phosphoprotein; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..883
FT /note="Probable ribonuclease ZC3H12C"
FT /id="PRO_0000337843"
FT DOMAIN 245..400
FT /note="RNase NYN"
FT /evidence="ECO:0000255"
FT ZN_FING 410..435
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 53..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 680..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..701
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..769
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 1..7
FT /note="MPGGGSQ -> MSLYFPAN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054127"
FT CONFLICT 69
FT /note="D -> G (in Ref. 1; BAG58377)"
FT /evidence="ECO:0000305"
FT CONFLICT 574
FT /note="P -> A (in Ref. 1; BAG58377)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 883 AA; 99340 MW; BF369391C5A36854 CRC64;
MPGGGSQEYG VLCIQEYRKN SKVESSTRNN FMGLKDHLGH DLGHLYVEST DPQLSPAVPW
STVENPSMDT VNVGKDEKEA SEENASSGDS EENTNSDHES EQLGSISVEP GLITKTHRQL
CRSPCLEPHI LKRNEILQDF KPEESQTTSK EAKKPPDVVR EYQTKLEFAL KLGYSEEQVQ
LVLNKLGTDA LINDILGELV KLGNKSEADQ TVSTINTITR ETSSLESQRS ESPMQEIVTD
DGENLRPIVI DGSNVAMSHG NKEVFSCRGI KLAVDWFLER GHKDITVFVP AWRKEQSRPD
ALITDQEILR KLEKEKILVF TPSRRVQGRR VVCYDDRFIV KLAFESDGII VSNDNYRDLA
NEKPEWKKFI DERLLMYSFV NDKFMPPDDP LGRHGPSLDN FLRKKPIVPE HKKQPCPYGK
KCTYGHKCKY YHPERGSQPQ RSVADELRAM SRNTAAKTAN EGGLVKSNSV PCSTKADSTS
DVKRGAPKRQ SDPSIRTQVY QDLEEKLPTK NKLETRSVPS LVSIPATSTA KPQSTTSLSN
GLPSGVHFPP QDQRPQGQYP SMMMATKNHG TPMPYEQYPK CDSPVDIGYY SMLNAYSNLS
LSGPRSPERR FSLDTDYRIS SVASDCSSEG SMSCGSSDSY VGYNDRSYVS SPDPQLEENL
KCQHMHPHSR LNPQPFLQNF HDPLTRGQSY SHEEPKFHHK PPLPHLALHL PHSAVGARSS
CPGDYPSPPS SAHSKAPHLG RSLVATRIDS ISDSRLYDSS PSRQRKPYSR QEGLGSWERP
GYGIDAYGYR QTYSLPDNST QPCYEQFTFQ SLPEQQEPAW RIPYCGMPQD PPRYQDNREK
IYINLCNIFP PDLVRIVMKR NPHMTDAQQL AAAILVEKSQ LGY
