ZC3H3_MOUSE
ID ZC3H3_MOUSE Reviewed; 950 AA.
AC Q8CHP0; Q80X78;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Zinc finger CCCH domain-containing protein 3;
DE AltName: Full=Smad-interacting CPSF-like factor {ECO:0000303|PubMed:16115198};
GN Name=Zc3h3;
GN Synonyms=Kiaa0150, Smicl {ECO:0000303|PubMed:16115198}, Zc3hdc3, Zfp623;
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 [MRNA].
RC STRAIN=FVB/N;
RA Van Veldhoven P.P.;
RT "Cloning of mouse KIAA0150 gene product.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Salivary gland;
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 FUNCTION, INTERACTION WITH SMAD1; SMAD3; SMAD4; CPSF2 AND CPSF3, AND
RP SUBCELLULAR LOCATION.
RX PubMed=16115198; DOI=10.1111/j.1365-2443.2005.00887.x;
RA Collart C., Remacle J.E., Barabino S., van Grunsven L.A., Nelles L.,
RA Schellens A., Van de Putte T., Pype S., Huylebroeck D., Verschueren K.;
RT "Smicl is a novel Smad interacting protein and cleavage and polyadenylation
RT specificity factor associated protein.";
RL Genes Cells 10:897-906(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-851; SER-855 AND SER-934, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, Spleen, and Testis;
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: Required for the export of polyadenylated mRNAs from the
CC nucleus (By similarity). Enhances ACVR1B-induced SMAD-dependent
CC transcription. Binds to single-stranded DNA but not to double-stranded
CC DNA in vitro. Involved in RNA cleavage (PubMed:16115198).
CC {ECO:0000250|UniProtKB:Q8IXZ2, ECO:0000269|PubMed:16115198}.
CC -!- SUBUNIT: Interacts with SMAD1, SMAD3, SMAD4, CPSF2 and CPSF3.
CC {ECO:0000269|PubMed:16115198}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16115198}.
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DR EMBL; AJ516034; CAD56773.1; -; mRNA.
DR EMBL; BC049953; AAH49953.1; -; mRNA.
DR EMBL; BC060682; AAH60682.1; -; mRNA.
DR CCDS; CCDS27550.1; -.
DR RefSeq; NP_742119.1; NM_172121.1.
DR AlphaFoldDB; Q8CHP0; -.
DR STRING; 10090.ENSMUSP00000098106; -.
DR iPTMnet; Q8CHP0; -.
DR PhosphoSitePlus; Q8CHP0; -.
DR EPD; Q8CHP0; -.
DR jPOST; Q8CHP0; -.
DR MaxQB; Q8CHP0; -.
DR PaxDb; Q8CHP0; -.
DR PRIDE; Q8CHP0; -.
DR ProteomicsDB; 275268; -.
DR Antibodypedia; 14596; 102 antibodies from 20 providers.
DR DNASU; 223642; -.
DR Ensembl; ENSMUST00000100538; ENSMUSP00000098106; ENSMUSG00000075600.
DR GeneID; 223642; -.
DR KEGG; mmu:223642; -.
DR UCSC; uc007whf.1; mouse.
DR CTD; 23144; -.
DR MGI; MGI:2663721; Zc3h3.
DR VEuPathDB; HostDB:ENSMUSG00000075600; -.
DR eggNOG; KOG1492; Eukaryota.
DR GeneTree; ENSGT00940000161068; -.
DR HOGENOM; CLU_014207_0_0_1; -.
DR InParanoid; Q8CHP0; -.
DR OMA; TPNKGLM; -.
DR OrthoDB; 400525at2759; -.
DR PhylomeDB; Q8CHP0; -.
DR TreeFam; TF324375; -.
DR BioGRID-ORCS; 223642; 15 hits in 74 CRISPR screens.
DR ChiTaRS; Zc3h3; mouse.
DR PRO; PR:Q8CHP0; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8CHP0; protein.
DR Bgee; ENSMUSG00000075600; Expressed in islet of Langerhans and 75 other tissues.
DR ExpressionAtlas; Q8CHP0; baseline and differential.
DR Genevisible; Q8CHP0; MM.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IDA:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070412; F:R-SMAD binding; IDA:MGI.
DR GO; GO:0046332; F:SMAD binding; IPI:MGI.
DR GO; GO:0031124; P:mRNA 3'-end processing; IDA:MGI.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0032927; P:positive regulation of activin receptor signaling pathway; IGI:MGI.
DR GO; GO:1900363; P:regulation of mRNA polyadenylation; ISS:UniProtKB.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR Pfam; PF00642; zf-CCCH; 2.
DR SMART; SM00356; ZnF_C3H1; 5.
DR SUPFAM; SSF90229; SSF90229; 1.
DR PROSITE; PS50103; ZF_C3H1; 5.
PE 1: Evidence at protein level;
KW DNA-binding; Metal-binding; mRNA transport; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transport; Zinc; Zinc-finger.
FT CHAIN 1..950
FT /note="Zinc finger CCCH domain-containing protein 3"
FT /id="PRO_0000213897"
FT ZN_FING 662..690
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 694..717
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 718..744
FT /note="C3H1-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 745..772
FT /note="C3H1-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 773..795
FT /note="C3H1-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 32..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 793..950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..841
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..934
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 405
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IXZ2"
FT MOD_RES 851
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 855
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 918
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IXZ2"
FT MOD_RES 920
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IXZ2"
FT MOD_RES 934
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 950 AA; 103224 MW; F21F8307492C21E1 CRC64;
MEEKEQLRRQ IRLLQGLIDD YKTLHGNGPA LGNSSATRWQ PPMFPGGRTF GARYSRPSRR
GFSSHHGPSW RKKYSLVNQP VESSDPASDP AFQTSLRSED SQHPEPQQYV LERQVQLSPD
QNMVIKIKPP SKSGAINASG VQRGSLEGCD DPSWSGQRPQ GSEVEVPGGQ LQPARPGRTK
VGYSVDDPLL VCQKEPGKPR VVKSVGRVSD SSPEHRRTVS ENEVALRVHF PSVLPHHTAV
ALGRKVGPHS TSYSEQFIGD QRANTGHSDQ PASLGPVVAS VRPATARQVR EASLLVSCRT
SKFRKNNYKW VAASEKSPRV ARRALSPRTT LESGNKATLG TVGKTEKPQP KVDPEVRPEK
LATPSKPGLS PSKYKWKASS PSASSSSSFR WQSEAGSKDH TSQLSPVPSR PTSGDRPAGG
PSSLKPLFGE SQLSAYKVKS RTKIIRRRGN TSIPGDKKNS PTTATTSKNH LTQRRRQALR
GKNSPVLRKT PHKGLMQVNR HRLCCLPSSR THLSTKEASS VHMGIPPSNK VIKTRYRIVK
KTPSSSFGAP SFPSSLPSWR ARRIPLSRSL VLNRLRPAIT GGGKAPPGTP RWRNKGYRCI
GGVLYKVSAN KLSKTSSRPS DGNRTLLRTG RLDPATTCSR SLASRAIQRS LAIIRQAKQK
KEKKREYCMY YNRFGRCNRG ECCPYIHDPE KVAVCTRFVR GTCKKTDGSC PFSHHVSKEK
MPVCSYFLKG ICSNSNCPYS HVYVSRKAEV CSDFLKGYCP LGAKCKKKHT LLCPDFARRG
ICPRGSQCQL LHRNQKRHGR RTAAPPIPGP SDGAPRSKAS AGHVLRKPTT TQRSVRQMSS
GLASGAEAPA SPPPSPRVLA STSTLSSKAT AASSPSPSPS TSSPAPSLEQ EEAVSGTGSG
TGSSGLCKLP SFISLHSSPS PGGQTETGPQ APRSPRTKDS GKPLHIKPRL
