ZC12D_MOUSE
ID ZC12D_MOUSE Reviewed; 533 AA.
AC Q8BIY3; A4FU74;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Probable ribonuclease ZC3H12D;
DE EC=3.1.-.-;
DE AltName: Full=MCP-induced protein 4 {ECO:0000303|PubMed:18178554};
DE AltName: Full=Transformed follicular lymphoma homolog;
DE AltName: Full=Zinc finger CCCH domain-containing protein 12D {ECO:0000250|UniProtKB:Q6ZRW2};
GN Name=Zc3h12d {ECO:0000312|MGI:MGI:3045313};
GN Synonyms=Mcpip4 {ECO:0000303|PubMed:18178554}, Tfl;
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] {ECO:0000312|EMBL:BAC35154.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC35154.1};
RC TISSUE=Mammary gland {ECO:0000312|EMBL:BAC35154.1};
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] {ECO:0000312|EMBL:AAI12399.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 20-527.
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] {ECO:0000305}
RP IDENTIFICATION, AND TISSUE SPECIFICITY.
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 FUNCTION.
RX PubMed=26134560; DOI=10.1074/jbc.m114.635870;
RA Huang S., Liu S., Fu J.J., Tony Wang T., Yao X., Kumar A., Liu G., Fu M.;
RT "Monocyte chemotactic protein-induced protein 1 and 4 form a complex but
RT act independently in regulation of interleukin-6 mRNA degradation.";
RL J. Biol. Chem. 290:20782-20792(2015).
CC -!- FUNCTION: May regulate cell growth likely by suppressing RB1
CC phosphorylation (By similarity). May function as RNase and regulate the
CC levels of target RNA species (Potential). In association with ZC3H12A
CC enhances the degradation of interleukin IL-6 mRNA level in activated
CC macrophages (PubMed:26134560). Serve as a tumor suppressor in certain
CC leukemia cells (By similarity). Overexpression inhibits the G1 to S
CC phase progression through suppression of RB1 phosphorylation (By
CC similarity). {ECO:0000250|UniProtKB:A2A288,
CC ECO:0000269|PubMed:26134560}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC -!- SUBUNIT: Interacts with ZC3H12A. {ECO:0000250|UniProtKB:A2A288}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A2A288}.
CC Cytoplasm, P-body {ECO:0000250|UniProtKB:A2A288}. Note=Colocalizes with
CC ZC3H12A in GW bodies (GWBs). {ECO:0000250|UniProtKB:A2A288}.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in bone marrow derived
CC macrophages. {ECO:0000269|PubMed:18178554}.
CC -!- SIMILARITY: Belongs to the ZC3H12 family.
CC {ECO:0000250|UniProtKB:A6QQJ8}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI12399.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC35154.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK052806; BAC35154.1; ALT_FRAME; mRNA.
DR EMBL; BC112398; AAI12399.1; ALT_FRAME; mRNA.
DR CCDS; CCDS48496.1; -.
DR RefSeq; NP_766373.2; NM_172785.3.
DR AlphaFoldDB; Q8BIY3; -.
DR SMR; Q8BIY3; -.
DR BioGRID; 231859; 1.
DR IntAct; Q8BIY3; 1.
DR STRING; 10090.ENSMUSP00000040217; -.
DR iPTMnet; Q8BIY3; -.
DR PhosphoSitePlus; Q8BIY3; -.
DR EPD; Q8BIY3; -.
DR MaxQB; Q8BIY3; -.
DR PaxDb; Q8BIY3; -.
DR PeptideAtlas; Q8BIY3; -.
DR PRIDE; Q8BIY3; -.
DR ProteomicsDB; 275057; -.
DR DNASU; 237256; -.
DR GeneID; 237256; -.
DR KEGG; mmu:237256; -.
DR CTD; 340152; -.
DR MGI; MGI:3045313; Zc3h12d.
DR eggNOG; KOG3777; Eukaryota.
DR InParanoid; Q8BIY3; -.
DR OrthoDB; 771251at2759; -.
DR PhylomeDB; Q8BIY3; -.
DR BioGRID-ORCS; 237256; 1 hit in 73 CRISPR screens.
DR PRO; PR:Q8BIY3; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8BIY3; protein.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0000932; C:P-body; ISS:UniProtKB.
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:0061158; P:3'-UTR-mediated mRNA destabilization; IDA:UniProtKB.
DR GO; GO:0006402; P:mRNA catabolic process; IMP:MGI.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; IMP:MGI.
DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IBA:GO_Central.
DR GO; GO:0042098; P:T cell proliferation; IMP:MGI.
DR InterPro; IPR040546; Rege-1_UBA-like.
DR InterPro; IPR021869; RNase_Zc3h12_NYN.
DR InterPro; IPR000571; Znf_CCCH.
DR Pfam; PF11977; RNase_Zc3h12a; 1.
DR Pfam; PF18039; UBA_6; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Endonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..533
FT /note="Probable ribonuclease ZC3H12D"
FT /id="PRO_0000348932"
FT DOMAIN 92..246
FT /note="RNase NYN"
FT /evidence="ECO:0000255"
FT ZN_FING 251..282
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 262..368
FT /note="Necessary for interaction with ZC3H12A"
FT /evidence="ECO:0000250|UniProtKB:A2A288"
FT REGION 302..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 125
FT /note="T -> R (in Ref. 2; AAI12399)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 533 AA; 59340 MW; 70A129CC07BF6C64 CRC64;
MEHRSKMEFF QKLGYSQEDV VRVLGKLGDS ALVNDVLQEL IQTGSRPRAQ EDPASGTGVV
LIPRGCCGVQ DSAQQGPGTR PRRGWRRSSP LLRPIVIDGS NVAMSHGNKE AFSCRGIRLA
VDWFTDRGHT YIKVFVPSWR KEPSRSDTPI REQHVLEELE RQAVLVYTPS RKVNGKRVVC
YDDRYIVKVA YEKDGIIVSN DNYRDLQNEN PEWKWFIEQR LLMFSFVNDR FMPPDDPLGR
RGPTLSNFLS KKPRPPEPSW QHCPYGKKCT YGVKCRFYHP ERPHHGQLSV ADELRAKTRA
WLGGGAEEPR TPSARSRPTT ARLLPQEPGE HDLPPAPQPA VLAALNRSFA RLTFSDTAAS
GVVSQSRGPD WMPTGVPTSW APPSLRAGSA ATIGLPGMRS LRTPNNPLSP GDLGSPICPQ
ARLSERHRSR DMHSDLPPQR RPLEDPWALL PSSYCYLNHS VWSESAWGED IFRGPSESAQ
PVANGGGTRP VHCSFFPPDQ DHPVMASGPP LSDMALLTLL QRSQKTGAPL GDP
