Entry euk: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   10-MAY-2017, entry version 120.
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},
GN   Zfp830 {ECO:0000312|MGI:MGI:1914233};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the 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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-342, AND IDENTIFICATION
RP   BY 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
RP   PHENOTYPE, 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.,
RA   Babinet C., Cohen-Tannoudji M.;
RT   "Impaired mitotic progression and preimplantation lethality in mice
RT   lacking 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
RP   BY 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,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., 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
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, 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
RT   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-
RT   Abl/TAp63-dependent oocyte death associated with dramatic remodeling
RT   of ovarian somatic cells.";
RL   Cell Death Differ. 22:108-117(2015).
CC   -!- FUNCTION: Acts as an important regulator of the cell cycle that
CC       participates in the maintenance of genome integrity
CC       (PubMed:21191184, PubMed:23213458, PubMed:25168238,
CC       PubMed:15988037). During cell cycle progression in embryonic
CC       fibroblast, prevents replication fork collapse, double-strand
CC       break formation and cell cycle checkpoint activation
CC       (PubMed:21191184). Controls mitotic cell cycle progression and
CC       cell survival in rapidly proliferating intestinal epithelium and
CC       embryonic stem cells (PubMed:23213458). During the embryo
CC       preimplantation, controls different aspects of M phase
CC       (PubMed:15988037). During early oocyte growth, plays a role in
CC       oocyte survival by preventing chromosomal breaks formation,
CC       activation of TP63 and reduction of transcription
CC       (PubMed:25168238). {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
CC       complex composed of XAB2, PRPF19, AQR, ZNF830, ISY1, and PPIE;
CC       this complex binds preferentially to RNA. Interacts with XAB2.
CC       {ECO:0000250|UniProtKB:Q96NB3}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15988037}.
CC       Chromosome {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
CC       during mitosis. {ECO:0000269|PubMed:15988037}.
CC   -!- TISSUE SPECIFICITY: Widely expressed at low level. Expressed in
CC       oocytes from primordial to antral follicles. Also detected in
CC       somatic cells of the ovary, namely, in granulosa cells from the
CC       pre-antral follicle stage onward (PubMed:25168238).
CC       {ECO:0000269|PubMed:15988037, 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
CC       number, a high mitotic index, and the presence of abnormal mitotic
CC       figures. Mice appear unwell with significant loss of body weight
CC       and rapidly decline afterwards and die. Mice reveal major
CC       alterations of their digestive tract including a distended and
CC       filled stomach and an intestine lacking spontaneous peristaltism.
CC       The small intestine exhibits a thinner wall, less abundant and
CC       stunted villi and highly disorganized crypts. Large portion of the
CC       gut are almost devoid of normal epithelial structure
CC       (PubMed:23213458). Conditional inactivation of Omcg1 in oocytes
CC       leads to sterility and early folliculogenesis arrest
CC       (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; CAI25093.1; -; Genomic_DNA.
DR   EMBL; BC024340; AAH24340.1; -; mRNA.
DR   CCDS; CCDS25146.1; -.
DR   RefSeq; NP_080160.2; NM_025884.4.
DR   UniGene; Mm.29622; -.
DR   ProteinModelPortal; Q8R1N0; -.
DR   SMR; Q8R1N0; -.
DR   IntAct; Q8R1N0; 1.
DR   MINT; MINT-4118608; -.
DR   STRING; 10090.ENSMUSP00000056154; -.
DR   iPTMnet; Q8R1N0; -.
DR   PhosphoSitePlus; Q8R1N0; -.
DR   EPD; Q8R1N0; -.
DR   MaxQB; Q8R1N0; -.
DR   PaxDb; Q8R1N0; -.
DR   PeptideAtlas; Q8R1N0; -.
DR   PRIDE; Q8R1N0; -.
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   eggNOG; KOG3032; Eukaryota.
DR   eggNOG; ENOG4111GTR; LUCA.
DR   GeneTree; ENSGT00390000012151; -.
DR   HOGENOM; HOG000246999; -.
DR   HOVERGEN; HBG105347; -.
DR   InParanoid; Q8R1N0; -.
DR   KO; K13104; -.
DR   OMA; VLGKQHR; -.
DR   OrthoDB; EOG091G0MBX; -.
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   PRO; PR:Q8R1N0; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   Bgee; ENSMUSG00000046010; -.
DR   CleanEx; MM_ZFP830; -.
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: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:0044773; P:mitotic DNA damage checkpoint; IMP:MGI.
DR   GO; GO:0033314; P:mitotic DNA replication checkpoint; IMP:UniProtKB.
DR   GO; GO:0007067; P:mitotic nuclear division; IMP:MGI.
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   InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR   InterPro; IPR013087; Znf_C2H2_type.
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   Complete proteome; Developmental protein; Metal-binding; Mitosis;
KW   Nucleus; Phosphoprotein; Reference proteome; Zinc; Zinc-finger.
FT   INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:Q96NB3}.
FT   CHAIN         2    363       Zinc finger protein 830.
FT                                /FTId=PRO_0000076194.
FT   ZN_FING      53     75       C2H2-type.
FT   COILED       16     40       {ECO:0000255}.
FT   COILED      303    331       {ECO:0000255}.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000250|UniProtKB:Q96NB3}.
FT   MOD_RES     216    216       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q96NB3}.
FT   MOD_RES     342    342       Phosphoserine.
FT                                {ECO:0000244|PubMed:15345747,
FT                                ECO:0000244|PubMed:17242355,
FT                                ECO:0000244|PubMed:17525332,
FT                                ECO:0000244|PubMed:21183079}.
FT   MOD_RES     353    353       Phosphoserine.
FT                                {ECO:0000244|PubMed:17525332,
FT                                ECO:0000269|PubMed:21191184}.
FT   CONFLICT     81     82       EL -> DV (in Ref. 1; BAB30851).
FT                                {ECO:0000305}.
FT   CONFLICT    111    111       Q -> L (in Ref. 1; BAB26873).
FT                                {ECO:0000305}.
FT   CONFLICT    305    305       C -> G (in Ref. 1; BAE37178).
FT                                {ECO:0000305}.
FT   CONFLICT    309    309       V -> G (in Ref. 1; BAE37178).
FT                                {ECO:0000305}.
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CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT        48     82       ismart:ZnF_U1 [T]
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
//