ZN830_MOUSE
ID ZN830_MOUSE Reviewed; 363 AA.
AC Q8R1N0; Q3TR52; Q9CWV9; Q9CYI6;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Zinc finger protein 830 {ECO:0000250|UniProtKB:Q96NB3};
DE AltName: Full=Coiled-coil domain-containing protein 16 {ECO:0000250|UniProtKB:Q96NB3};
DE AltName: Full=Ovus mutant candidate gene 1 protein {ECO:0000305|PubMed:15988037};
GN Name=Znf830 {ECO:0000250|UniProtKB:Q96NB3};
GN Synonyms=Ccdc16 {ECO:0000250|UniProtKB:Q96NB3},
GN Omcg1 {ECO:0000303|PubMed:15988037}, Zfp830 {ECO:0000312|MGI:MGI:1914233};
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney, Liver, Skin, and Thymus;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-342, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=15988037; DOI=10.1128/mcb.25.14.6289-6302.2005;
RA Artus J., Vandormael-Pournin S., Froedin M., Nacerddine K., Babinet C.,
RA Cohen-Tannoudji M.;
RT "Impaired mitotic progression and preimplantation lethality in mice lacking
RT OMCG1, a new evolutionarily conserved nuclear protein.";
RL Mol. Cell. Biol. 25:6289-6302(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-342, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-342 AND SER-353, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-342, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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).
RN [9]
RP FUNCTION, PHOSPHORYLATION AT SER-353, AND SUBCELLULAR LOCATION.
RX PubMed=21191184; DOI=10.4161/cc.10.1.14379;
RA Houlard M., Artus J., Leguillier T., Vandormael-Pournin S.,
RA Cohen-Tannoudji M.;
RT "DNA-RNA hybrids contribute to the replication dependent genomic
RT instability induced by Omcg1 deficiency.";
RL Cell Cycle 10:108-117(2011).
RN [10]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=23213458; DOI=10.1242/bio.20121248;
RA Leguillier T., Vandormael-Pournin S., Artus J., Houlard M., Picard C.,
RA Bernex F., Robine S., Cohen-Tannoudji M.;
RT "Omcg1 is critically required for mitosis in rapidly dividing mouse
RT intestinal progenitors and embryonic stem cells.";
RL Biol. Open 1:648-657(2012).
RN [11]
RP DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=25168238; DOI=10.1038/cdd.2014.122;
RA Vandormael-Pournin S., Guigon C.J., Ishaq M., Coudouel N., Ave P.,
RA Huerre M., Magre S., Cohen-Tannoudji J., Cohen-Tannoudji M.;
RT "Oocyte-specific inactivation of Omcg1 leads to DNA damage and c-Abl/TAp63-
RT dependent oocyte death associated with dramatic remodeling of ovarian
RT somatic cells.";
RL Cell Death Differ. 22:108-117(2015).
CC -!- FUNCTION: May play a role in pre-mRNA splicing as component of the
CC spliceosome (By similarity). Acts as an important regulator of the cell
CC cycle that participates in the maintenance of genome integrity
CC (PubMed:21191184, PubMed:23213458, PubMed:25168238, PubMed:15988037).
CC During cell cycle progression in embryonic fibroblast, prevents
CC replication fork collapse, double-strand break formation and cell cycle
CC checkpoint activation (PubMed:21191184). Controls mitotic cell cycle
CC progression and cell survival in rapidly proliferating intestinal
CC epithelium and embryonic stem cells (PubMed:23213458). During the
CC embryo preimplantation, controls different aspects of M phase
CC (PubMed:15988037). During early oocyte growth, plays a role in oocyte
CC survival by preventing chromosomal breaks formation, activation of TP63
CC and reduction of transcription (PubMed:25168238).
CC {ECO:0000250|UniProtKB:Q96NB3, ECO:0000269|PubMed:15988037,
CC ECO:0000269|PubMed:21191184, ECO:0000269|PubMed:23213458,
CC ECO:0000269|PubMed:25168238}.
CC -!- SUBUNIT: Component of the XAB2 complex, a multimeric protein complex
CC composed of XAB2, PRPF19, AQR, ZNF830, ISY1, and PPIE; this complex
CC binds preferentially to RNA. Interacts with XAB2. Identified in a
CC pentameric intron-binding (IB) complex composed of AQR, XAB2, ISY1,
CC ZNF830 and PPIE that is incorporated into the spliceosome as a
CC preassembled complex. The IB complex does not contain PRPF19.
CC {ECO:0000250|UniProtKB:Q96NB3}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15988037}. Chromosome
CC {ECO:0000269|PubMed:15988037}. Nucleus speckle
CC {ECO:0000269|PubMed:21191184}. Note=Excluded from nucleolus. In
CC metaphase II oocytes and in mitotic blastomeres, it is detected in
CC cytoplasm, suggesting that it is not associated with chromosomes during
CC mitosis. {ECO:0000269|PubMed:15988037}.
CC -!- TISSUE SPECIFICITY: Widely expressed at low level. Expressed in oocytes
CC from primordial to antral follicles. Also detected in somatic cells of
CC the ovary, namely, in granulosa cells from the pre-antral follicle
CC stage onward (PubMed:25168238). {ECO:0000269|PubMed:15988037,
CC ECO:0000269|PubMed:25168238}.
CC -!- DEVELOPMENTAL STAGE: Expressed in preimplantation embryos.
CC {ECO:0000269|PubMed:15988037}.
CC -!- PTM: Phosphorylated in response to DNA damage by the cell cycle
CC checkpoint kinases ATR/ATM. {ECO:0000269|PubMed:21191184}.
CC -!- DISRUPTION PHENOTYPE: Mice die by the end of preimplantation
CC development and exhibit a dramatic reduction in the total cell number,
CC a high mitotic index, and the presence of abnormal mitotic figures.
CC Mice appear unwell with significant loss of body weight and rapidly
CC decline afterwards and die. Mice reveal major alterations of their
CC digestive tract including a distended and filled stomach and an
CC intestine lacking spontaneous peristaltism. The small intestine
CC exhibits a thinner wall, less abundant and stunted villi and highly
CC disorganized crypts. Large portion of the gut are almost devoid of
CC normal epithelial structure (PubMed:23213458). Conditional inactivation
CC of Omcg1 in oocytes leads to sterility and early folliculogenesis
CC arrest (PubMed:25168238). {ECO:0000269|PubMed:15988037,
CC ECO:0000269|PubMed:23213458, ECO:0000269|PubMed:25168238}.
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DR EMBL; AK050043; BAC34045.1; -; mRNA.
DR EMBL; AK010353; BAB26873.1; -; mRNA.
DR EMBL; AK017640; BAB30851.1; -; mRNA.
DR EMBL; AK132497; BAE21204.1; -; mRNA.
DR EMBL; AK148058; BAE28318.1; -; mRNA.
DR EMBL; AK163064; BAE37178.1; -; mRNA.
DR EMBL; AK167656; BAE39707.1; -; mRNA.
DR EMBL; AK168417; BAE40331.1; -; mRNA.
DR EMBL; AL645594; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC024340; AAH24340.1; -; mRNA.
DR CCDS; CCDS25146.1; -.
DR RefSeq; NP_080160.2; NM_025884.4.
DR AlphaFoldDB; Q8R1N0; -.
DR SMR; Q8R1N0; -.
DR BioGRID; 211854; 2.
DR STRING; 10090.ENSMUSP00000056154; -.
DR iPTMnet; Q8R1N0; -.
DR PhosphoSitePlus; Q8R1N0; -.
DR EPD; Q8R1N0; -.
DR jPOST; Q8R1N0; -.
DR MaxQB; Q8R1N0; -.
DR PaxDb; Q8R1N0; -.
DR PeptideAtlas; Q8R1N0; -.
DR PRIDE; Q8R1N0; -.
DR ProteomicsDB; 275037; -.
DR Antibodypedia; 15518; 111 antibodies from 23 providers.
DR Ensembl; ENSMUST00000056677; ENSMUSP00000056154; ENSMUSG00000046010.
DR GeneID; 66983; -.
DR KEGG; mmu:66983; -.
DR UCSC; uc007kmy.1; mouse.
DR CTD; 66983; -.
DR MGI; MGI:1914233; Zfp830.
DR VEuPathDB; HostDB:ENSMUSG00000046010; -.
DR eggNOG; KOG3032; Eukaryota.
DR GeneTree; ENSGT00390000012151; -.
DR HOGENOM; CLU_058140_1_0_1; -.
DR InParanoid; Q8R1N0; -.
DR OMA; EQIECYK; -.
DR OrthoDB; 1458826at2759; -.
DR PhylomeDB; Q8R1N0; -.
DR TreeFam; TF315895; -.
DR Reactome; R-MMU-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-MMU-6782135; Dual incision in TC-NER.
DR Reactome; R-MMU-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR BioGRID-ORCS; 66983; 19 hits in 73 CRISPR screens.
DR ChiTaRS; Zfp830; mouse.
DR PRO; PR:Q8R1N0; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8R1N0; protein.
DR Bgee; ENSMUSG00000046010; Expressed in ear vesicle and 250 other tissues.
DR Genevisible; Q8R1N0; MM.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0001832; P:blastocyst growth; IMP:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051276; P:chromosome organization; IMP:MGI.
DR GO; GO:0060729; P:intestinal epithelial structure maintenance; IMP:MGI.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:MGI.
DR GO; GO:0044773; P:mitotic DNA damage checkpoint signaling; IMP:MGI.
DR GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; IMP:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0033260; P:nuclear DNA replication; IMP:MGI.
DR GO; GO:0001541; P:ovarian follicle development; IMP:UniProtKB.
DR GO; GO:0001546; P:preantral ovarian follicle growth; IMP:UniProtKB.
DR GO; GO:0048478; P:replication fork protection; IMP:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR040050; ZNF830-like.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR PANTHER; PTHR13278; PTHR13278; 1.
DR SMART; SM00451; ZnF_U1; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cell division; Chromosome; Coiled coil;
KW Developmental protein; Metal-binding; Mitosis; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Spliceosome;
KW Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q96NB3"
FT CHAIN 2..363
FT /note="Zinc finger protein 830"
FT /id="PRO_0000076194"
FT ZN_FING 53..75
FT /note="C2H2-type"
FT REGION 81..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 16..40
FT /evidence="ECO:0000255"
FT COILED 303..331
FT /evidence="ECO:0000255"
FT COMPBIAS 89..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q96NB3"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96NB3"
FT MOD_RES 342
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21191184,
FT ECO:0007744|PubMed:17525332"
FT CONFLICT 81..82
FT /note="EL -> DV (in Ref. 1; BAB30851)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="Q -> L (in Ref. 1; BAB26873)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="C -> G (in Ref. 1; BAE37178)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="V -> G (in Ref. 1; BAE37178)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 363 AA; 40658 MW; 1247580A0D8B6E60 CRC64;
MASSTSTRTP AGKRVVNQEE LRRLMREKQR LSTNRKRIES PFAKYNRLGQ LSCALCNTPV
KSELLWQTHV LGKQHRERVA ELKGAKGATQ GPSTGTVPQA TKRRATDVES QDAKKAKASA
GPQVQPSTSA SSANLDAARA APSKPGLGLL PDYDDEEEEE EEGGGEERRD SSKHLPDAQG
KEHSLASPRE TTSNVLPNDP FNTNPPKAPL VPHSGSIEKA EIHEKVVERR ENTAEALPEG
FFDDPEVDAK VRKVDAPKDQ MDKEWDEFQK AMRQVNTISE AIVAEEDEEG RLDRQIGEID
EQIECYRRVE KLRNRQDEIK NKLKEVLTIK ELQKKEEENV DSDDEGELQD LLSQDWRVKG
ALL
