ZCH12_MOUSE
ID ZCH12_MOUSE Reviewed; 402 AA.
AC Q9CZA5;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Zinc finger CCHC domain-containing protein 12;
DE AltName: Full=Smad-interacting zinc finger protein 1;
GN Name=Zcchc12; Synonyms=Sizn1;
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], FUNCTION, INTERACTION WITH SMAD1 AND CBP, AND
RP TISSUE SPECIFICITY.
RX PubMed=18160706; DOI=10.1128/mcb.01038-07;
RA Cho G., Lim Y., Zand D., Golden J.A.;
RT "Sizn1 is a novel protein that functions as a transcriptional coactivator
RT of bone morphogenic protein signaling.";
RL Mol. Cell. Biol. 28:1565-1572(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; 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).
CC -!- FUNCTION: Transcriptional coactivator in the bone morphogenetic protein
CC (BMP)-signaling pathway. It positively modulates BMP signaling by
CC interacting with SMAD1 and associating with CBP in the transcription
CC complex. It contributes to the BMP-induced enhancement of cholinergic-
CC neuron-specific gene expression. {ECO:0000269|PubMed:18160706}.
CC -!- SUBUNIT: Interacts with SMAD1 and CREB-binding protein (CBP). Forms a
CC protein-DNA complex through its association with SMAD1.
CC {ECO:0000269|PubMed:18160706}.
CC -!- TISSUE SPECIFICITY: In embryonic brains expression is restricted to the
CC ventral region of the forebrain, including the septum, amygdala, caudal
CC putamen, and in the basal-forebrain cholinergic neurons. In adults,
CC expressed in the brain, and at low levels in the testis.
CC {ECO:0000269|PubMed:18160706}.
CC -!- SIMILARITY: Belongs to the ZCCHC12 family. {ECO:0000305}.
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DR EMBL; AY466375; AAR85891.1; -; mRNA.
DR EMBL; AK012833; BAB28501.1; -; mRNA.
DR EMBL; BC049071; AAH49071.1; -; mRNA.
DR EMBL; BC055714; AAH55714.1; -; mRNA.
DR CCDS; CCDS30058.1; -.
DR RefSeq; NP_082601.1; NM_028325.3.
DR RefSeq; XP_006541458.1; XM_006541395.1.
DR RefSeq; XP_006541460.1; XM_006541397.1.
DR RefSeq; XP_006541461.1; XM_006541398.1.
DR RefSeq; XP_006541462.1; XM_006541399.1.
DR RefSeq; XP_006541463.1; XM_006541400.2.
DR RefSeq; XP_006541464.1; XM_006541401.1.
DR RefSeq; XP_006541466.1; XM_006541403.1.
DR RefSeq; XP_011249276.1; XM_011250974.2.
DR RefSeq; XP_017174118.1; XM_017318629.1.
DR RefSeq; XP_017174119.1; XM_017318630.1.
DR AlphaFoldDB; Q9CZA5; -.
DR STRING; 10090.ENSMUSP00000110913; -.
DR PhosphoSitePlus; Q9CZA5; -.
DR MaxQB; Q9CZA5; -.
DR PaxDb; Q9CZA5; -.
DR PRIDE; Q9CZA5; -.
DR ProteomicsDB; 275131; -.
DR DNASU; 72693; -.
DR Ensembl; ENSMUST00000048067; ENSMUSP00000044550; ENSMUSG00000036699.
DR Ensembl; ENSMUST00000115256; ENSMUSP00000110911; ENSMUSG00000036699.
DR Ensembl; ENSMUST00000115257; ENSMUSP00000110912; ENSMUSG00000036699.
DR Ensembl; ENSMUST00000115258; ENSMUSP00000110913; ENSMUSG00000036699.
DR GeneID; 72693; -.
DR KEGG; mmu:72693; -.
DR UCSC; uc009sxk.2; mouse.
DR CTD; 170261; -.
DR MGI; MGI:1919943; Zcchc12.
DR VEuPathDB; HostDB:ENSMUSG00000036699; -.
DR eggNOG; ENOG502RU0T; Eukaryota.
DR GeneTree; ENSGT01030000234522; -.
DR HOGENOM; CLU_686127_0_0_1; -.
DR InParanoid; Q9CZA5; -.
DR OMA; GPPLMAN; -.
DR OrthoDB; 697027at2759; -.
DR PhylomeDB; Q9CZA5; -.
DR TreeFam; TF335054; -.
DR BioGRID-ORCS; 72693; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Zcchc12; mouse.
DR PRO; PR:Q9CZA5; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9CZA5; protein.
DR Bgee; ENSMUSG00000036699; Expressed in medial preoptic region and 162 other tissues.
DR Genevisible; Q9CZA5; MM.
DR GO; GO:0016607; C:nuclear speck; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0016605; C:PML body; IDA:MGI.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0032183; F:SUMO binding; IDA:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030509; P:BMP signaling pathway; IDA:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR InterPro; IPR026523; PNMA.
DR InterPro; IPR001878; Znf_CCHC.
DR PANTHER; PTHR23095; PTHR23095; 1.
DR Pfam; PF14893; PNMA; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 1: Evidence at protein level;
KW Metal-binding; Reference proteome; Transcription; Transcription regulation;
KW Zinc; Zinc-finger.
FT CHAIN 1..402
FT /note="Zinc finger CCHC domain-containing protein 12"
FT /id="PRO_0000150972"
FT ZN_FING 346..363
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 402 AA; 45107 MW; 3603A26F2CCD5C3D CRC64;
MASILSRLGS SRGQNSPLPP WAHSMLRSLG RSLGPLMASM AERNMRLFSG RAEPAQGEET
FENWLSQVTG VLPDWHMPEE EKVRRLMRTL RGPAREVMRL LQAANPGLDV EDFLRAMKLV
FGESESSVTA HSKFVNTVQE HGEKPSLYVI RLEVQLQNAI QAGVFAEREA NQARLHQLLV
GAEMSTDLRF RLKNLLRVYA NEPERLPNFL ELIRMIREEE EWEETFINPK RPRRAESVME
RALSPMAFQS SPPIMISSID CNVIEIDDSP DDSDEDVILV EPEDPPLPSS SASSFLGRAV
SEDQVLVIES PNIFEIQAPS TSSGAGRKNN RGFGELRRAR KRKHTIHCSH CGEEGHSKET
CDNESDKGQV FENLIITLQE LTHAEERARG APGEPIGLSE PQ
