ZC12B_HUMAN
ID ZC12B_HUMAN Reviewed; 836 AA.
AC Q5HYM0; B2RTQ3; E9PAJ6; Q5H9C0;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 3.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Probable ribonuclease ZC3H12B;
DE EC=3.1.-.-;
DE AltName: Full=MCP-induced protein 2;
DE AltName: Full=Zinc finger CCCH domain-containing protein 12B;
GN Name=ZC3H12B; Synonyms=CXorf32, MCPIP2;
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 GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 10-836 (ISOFORM 2).
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP IDENTIFICATION.
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).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5HYM0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5HYM0-2; Sequence=VSP_039896;
CC -!- SIMILARITY: Belongs to the ZC3H12 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI40768.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI71781.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAI46044.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL050306; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z83841; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC140767; AAI40768.1; ALT_INIT; mRNA.
DR EMBL; BC171781; AAI71781.1; ALT_INIT; mRNA.
DR EMBL; BX647241; CAI46044.1; ALT_INIT; mRNA.
DR CCDS; CCDS48131.2; -. [Q5HYM0-1]
DR RefSeq; NP_001010888.3; NM_001010888.3. [Q5HYM0-1]
DR RefSeq; XP_011529241.1; XM_011530939.2. [Q5HYM0-1]
DR RefSeq; XP_016884967.1; XM_017029478.1. [Q5HYM0-1]
DR RefSeq; XP_016884968.1; XM_017029479.1. [Q5HYM0-1]
DR RefSeq; XP_016884969.1; XM_017029480.1. [Q5HYM0-1]
DR RefSeq; XP_016884970.1; XM_017029481.1. [Q5HYM0-1]
DR RefSeq; XP_016884971.1; XM_017029482.1. [Q5HYM0-1]
DR RefSeq; XP_016884972.1; XM_017029483.1. [Q5HYM0-1]
DR RefSeq; XP_016884973.1; XM_017029484.1. [Q5HYM0-1]
DR PDB; 6SJD; X-ray; 3.29 A; A/B=185-362.
DR PDBsum; 6SJD; -.
DR AlphaFoldDB; Q5HYM0; -.
DR SMR; Q5HYM0; -.
DR BioGRID; 131074; 3.
DR IntAct; Q5HYM0; 1.
DR STRING; 9606.ENSP00000340839; -.
DR iPTMnet; Q5HYM0; -.
DR PhosphoSitePlus; Q5HYM0; -.
DR BioMuta; ZC3H12B; -.
DR MassIVE; Q5HYM0; -.
DR PaxDb; Q5HYM0; -.
DR PeptideAtlas; Q5HYM0; -.
DR PRIDE; Q5HYM0; -.
DR ProteomicsDB; 19028; -.
DR ProteomicsDB; 62954; -. [Q5HYM0-1]
DR ProteomicsDB; 62955; -. [Q5HYM0-2]
DR Antibodypedia; 414; 90 antibodies from 21 providers.
DR DNASU; 340554; -.
DR Ensembl; ENST00000338957.4; ENSP00000340839.4; ENSG00000102053.12. [Q5HYM0-1]
DR GeneID; 340554; -.
DR KEGG; hsa:340554; -.
DR MANE-Select; ENST00000338957.5; ENSP00000340839.4; NM_001010888.4; NP_001010888.3.
DR UCSC; uc010nko.3; human. [Q5HYM0-1]
DR CTD; 340554; -.
DR DisGeNET; 340554; -.
DR GeneCards; ZC3H12B; -.
DR HGNC; HGNC:17407; ZC3H12B.
DR HPA; ENSG00000102053; Low tissue specificity.
DR MIM; 300889; gene.
DR neXtProt; NX_Q5HYM0; -.
DR OpenTargets; ENSG00000102053; -.
DR VEuPathDB; HostDB:ENSG00000102053; -.
DR eggNOG; KOG3777; Eukaryota.
DR GeneTree; ENSGT00940000159316; -.
DR HOGENOM; CLU_013020_1_0_1; -.
DR InParanoid; Q5HYM0; -.
DR OMA; QGMYSRN; -.
DR OrthoDB; 771251at2759; -.
DR PhylomeDB; Q5HYM0; -.
DR TreeFam; TF315783; -.
DR PathwayCommons; Q5HYM0; -.
DR SignaLink; Q5HYM0; -.
DR BioGRID-ORCS; 340554; 12 hits in 695 CRISPR screens.
DR ChiTaRS; ZC3H12B; human.
DR GenomeRNAi; 340554; -.
DR Pharos; Q5HYM0; Tbio.
DR PRO; PR:Q5HYM0; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q5HYM0; protein.
DR Bgee; ENSG00000102053; Expressed in prefrontal cortex and 119 other tissues.
DR Genevisible; Q5HYM0; 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 3D-structure; Alternative splicing; Endonuclease; Hydrolase; Magnesium;
KW Metal-binding; Nuclease; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..836
FT /note="Probable ribonuclease ZC3H12B"
FT /id="PRO_0000254045"
FT DOMAIN 190..345
FT /note="RNase NYN"
FT /evidence="ECO:0000255"
FT ZN_FING 355..380
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 94..168
FT /note="SSILQDGKLDLEKEYQAKMEFALKLGYAEEQIQSVLNKLGPESLINDVLAEL
FT VRLGNKGDSEGQINLSLLVPRGP -> NHLLMMYWQSLSDLGTKVIQKG (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_039896"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:6SJD"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:6SJD"
FT HELIX 197..204
FT /evidence="ECO:0007829|PDB:6SJD"
FT TURN 206..208
FT /evidence="ECO:0007829|PDB:6SJD"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:6SJD"
FT HELIX 212..224
FT /evidence="ECO:0007829|PDB:6SJD"
FT STRAND 230..235
FT /evidence="ECO:0007829|PDB:6SJD"
FT HELIX 236..239
FT /evidence="ECO:0007829|PDB:6SJD"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:6SJD"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:6SJD"
FT HELIX 253..258
FT /evidence="ECO:0007829|PDB:6SJD"
FT TURN 259..261
FT /evidence="ECO:0007829|PDB:6SJD"
FT STRAND 263..266
FT /evidence="ECO:0007829|PDB:6SJD"
FT STRAND 269..276
FT /evidence="ECO:0007829|PDB:6SJD"
FT HELIX 281..291
FT /evidence="ECO:0007829|PDB:6SJD"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:6SJD"
FT HELIX 302..307
FT /evidence="ECO:0007829|PDB:6SJD"
FT HELIX 309..318
FT /evidence="ECO:0007829|PDB:6SJD"
FT STRAND 333..336
FT /evidence="ECO:0007829|PDB:6SJD"
FT HELIX 343..346
FT /evidence="ECO:0007829|PDB:6SJD"
FT STRAND 347..350
FT /evidence="ECO:0007829|PDB:6SJD"
SQ SEQUENCE 836 AA; 94205 MW; C7B2D9A790579442 CRC64;
MTATAEVETP KMEKSASKEE KQQPKQDSTE QGNADSEEWM SSESDPEQIS LKSSDNSKSC
QPRDGQLKKK EMHSKPHRQL CRSPCLDRPS FSQSSILQDG KLDLEKEYQA KMEFALKLGY
AEEQIQSVLN KLGPESLIND VLAELVRLGN KGDSEGQINL SLLVPRGPSS REIASPELSL
EDEIDNSDNL RPVVIDGSNV AMSHGNKEEF SCRGIQLAVD WFLDKGHKDI TVFVPAWRKE
QSRPDAPITD QDILRKLEKE KILVFTPSRR VQGRRVVCYD DRFIVKLAFD SDGIIVSNDN
YRDLQVEKPE WKKFIEERLL MYSFVNDKFM PPDDPLGRHG PSLENFLRKR PIVPEHKKQP
CPYGKKCTYG HKCKYYHPER ANQPQRSVAD ELRISAKLST VKTMSEGTLA KCGTGMSSAK
GEITSEVKRV APKRQSDPSI RSVAMEPEEW LSIARKPEAS SVPSLVTALS VPTIPPPKSH
AVGALNTRSA SSPVPGSSHF PHQKASLEHM ASMQYPPILV TNSHGTPISY AEQYPKFESM
GDHGYYSMLG DFSKLNINSM HNREYYMAEV DRGVYARNPN LCSDSRVSHT RNDNYSSYNN
VYLAVADTHP EGNLKLHRSA SQNRLQPFPH GYHEALTRVQ SYGPEDSKQG PHKQSVPHLA
LHAQHPSTGT RSSCPADYPM PPNIHPGATP QPGRALVMTR MDSISDSRLY ESNPVRQRRP
PLCREQHASW DPLPCTTDSY GYHSYPLSNS LMQPCYEPVM VRSVPEKMEQ LWRNPWVGMC
NDSREHMIPE HQYQTYKNLC NIFPSNIVLA VMEKNPHTAD AQQLAALIVA KLRAAR
