ID SRRT_MOUSE Reviewed; 875 AA. AC Q99MR6; Q3UD04; Q5D042; Q8VEE6; Q99MR4; Q99MR5; Q99MR7; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 27-MAY-2015, entry version 98. DE RecName: Full=Serrate RNA effector molecule homolog; DE AltName: Full=Arsenite-resistance protein 2; GN Name=Srrt; Synonyms=Ars2, Asr2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS RP A; B; C AND D). RC STRAIN=129/Sv; RX PubMed=11239002; DOI=10.1093/nar/29.6.1352; RA Wilson M.D., Riemer C., Martindale D.W., Schnupf P., Boright A.P., RA Cheung T.L., Hardy D.M., Schwartz S., Scherer S.W., Tsui L.-C., RA Miller W., Koop B.F.; RT "Comparative analysis of the gene-dense ACHE/TFR2 region on human RT chromosome 7q22 with the orthologous region on mouse chromosome 5."; RL Nucleic Acids Res. 29:1352-1365(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D). RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Kidney, and Mammary tumor; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 477-875 (ISOFORM C). RC STRAIN=C57BL/6J; TISSUE=Bone marrow; 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 [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-543, 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 SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE. RX PubMed=18086880; DOI=10.1128/MCB.01565-07; RA Wilson M.D., Wang D., Wagner R., Breyssens H., Gertsenstein M., RA Lobe C., Lu X., Nagy A., Burke R.D., Koop B.F., Howard P.L.; RT "ARS2 is a conserved eukaryotic gene essential for early mammalian RT development."; RL Mol. Cell. Biol. 28:1503-1514(2008). RN [6] RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, RP INTERACTION WITH NCBP1 AND DROSHA, AND DISRUPTION PHENOTYPE. RX PubMed=19632182; DOI=10.1016/j.cell.2009.04.046; RA Gruber J.J., Zatechka D.S., Sabin L.R., Yong J., Lum J.J., Kong M., RA Zong W.-X., Zhang Z., Lau C.-K., Rawlings J., Cherry S., Ihle J.N., RA Dreyfuss G., Thompson C.B.; RT "Ars2 links the nuclear cap-binding complex to RNA interference and RT cell proliferation."; RL Cell 138:328-339(2009). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-543, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200; RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; RT "Large scale localization of protein phosphorylation by use of RT electron capture dissociation mass spectrometry."; RL Mol. Cell. Proteomics 8:904-912(2009). RN [8] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=22198669; DOI=10.1038/nature10712; RA Andreu-Agullo C., Maurin T., Thompson C.B., Lai E.C.; RT "Ars2 maintains neural stem-cell identity through direct RT transcriptional activation of Sox2."; RL Nature 481:195-198(2012). CC -!- FUNCTION: Acts as a mediator between the cap-binding complex (CBC) CC and the primary microRNAs (miRNAs) processing machinery during CC cell proliferation. Contributes to the stability and delivery of CC capped primary miRNA transcripts to the primary miRNA processing CC complex containing DGCR8 and DROSHA, thereby playing a role in CC RNA-mediated gene silencing (RNAi) by miRNAs. Binds capped RNAs CC (m7GpppG-capped RNA); however interaction is probably mediated via CC its interaction with NCBP1/CBP80 component of the CBC complex. CC Involved in cell cycle progression at S phase. Does not directly CC confer arsenite resistance but rather modulates arsenic CC sensitivity. Independently of its activity on miRNAs, necessary CC and sufficient to promote neural stem cell self-renewal. Does so CC by directly binding SOX2 promoter and positively regulating its CC transcription. {ECO:0000269|PubMed:19632182, CC ECO:0000269|PubMed:22198669}. CC -!- SUBUNIT: Interacts with CASP8AP2 and ERBB4 (By similarity). CC Interacts with NCBP1 and DROSHA. {ECO:0000250, CC ECO:0000269|PubMed:19632182}. CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm. Cytoplasm. CC Note=Predominantly nuclear. Shuttles between the nucleus and the CC cytoplasm in a CRM1-dependent way. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=A; CC IsoId=Q99MR6-1; Sequence=Displayed; CC Name=B; CC IsoId=Q99MR6-2; Sequence=VSP_000325; CC Name=C; CC IsoId=Q99MR6-3; Sequence=VSP_000325, VSP_000326; CC Name=D; CC IsoId=Q99MR6-4; Sequence=VSP_000326; CC -!- TISSUE SPECIFICITY: Widely expressed, with a preference for CC proliferating cells. Highly expressed in hematopoietic tissues and CC reduced or absent expression in parenchymal organs like liver and CC kidney. In the brain, expressed in the subventricular zone by CC niche astrocytes, ependymal cells and neural stem cells. In this CC cerebral context, expressed in slowly dividing cells. CC {ECO:0000269|PubMed:18086880, ECO:0000269|PubMed:19632182, CC ECO:0000269|PubMed:22198669}. CC -!- INDUCTION: Upon cell proliferation. {ECO:0000269|PubMed:19632182}. CC -!- DISRUPTION PHENOTYPE: Death around the time of implantation. CC Deletion in adults leads to proliferative arrest and bone marrow CC hypoplasia whereas parenchymal organs composed of nonproliferating CC cells are unaffected. {ECO:0000269|PubMed:18086880, CC ECO:0000269|PubMed:19632182}. CC -!- SIMILARITY: Belongs to the ARS2 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH19117.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; CC Sequence=BAE29458.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF312033; AAK28817.1; -; Genomic_DNA. DR EMBL; AF312033; AAK28818.1; -; Genomic_DNA. DR EMBL; AF312033; AAK28819.1; -; Genomic_DNA. DR EMBL; AF312033; AAK28820.1; -; Genomic_DNA. DR EMBL; BC019117; AAH19117.1; ALT_INIT; mRNA. DR EMBL; BC066831; AAH66831.1; -; mRNA. DR EMBL; AK150310; BAE29458.1; ALT_INIT; mRNA. DR CCDS; CCDS39331.1; -. [Q99MR6-1] DR RefSeq; NP_001103379.1; NM_001109909.1. [Q99MR6-4] DR RefSeq; NP_001103380.1; NM_001109910.1. [Q99MR6-3] DR RefSeq; NP_113582.1; NM_031405.2. [Q99MR6-1] DR RefSeq; XP_006504692.1; XM_006504629.1. [Q99MR6-2] DR UniGene; Mm.387734; -. DR ProteinModelPortal; Q99MR6; -. DR SMR; Q99MR6; 149-288. DR BioGrid; 219965; 1. DR IntAct; Q99MR6; 2. DR MINT; MINT-1853620; -. DR PhosphoSite; Q99MR6; -. DR MaxQB; Q99MR6; -. DR PaxDb; Q99MR6; -. DR PRIDE; Q99MR6; -. DR Ensembl; ENSMUST00000040873; ENSMUSP00000043123; ENSMUSG00000037364. [Q99MR6-1] DR GeneID; 83701; -. DR KEGG; mmu:83701; -. DR UCSC; uc009acb.2; mouse. [Q99MR6-1] DR UCSC; uc009acc.2; mouse. [Q99MR6-3] DR UCSC; uc012eew.1; mouse. [Q99MR6-4] DR CTD; 51593; -. DR MGI; MGI:1933527; Srrt. DR eggNOG; NOG283007; -. DR GeneTree; ENSGT00390000005492; -. DR InParanoid; Q99MR6; -. DR OMA; DDHGGDP; -. DR OrthoDB; EOG70PBXD; -. DR PhylomeDB; Q99MR6; -. DR TreeFam; TF317609; -. DR ChiTaRS; Srrt; mouse. DR NextBio; 350735; -. DR PRO; PR:Q99MR6; -. DR Proteomes; UP000000589; Chromosome 5. DR Bgee; Q99MR6; -. DR CleanEx; MM_ARS2; -. DR Genevestigator; Q99MR6; -. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; ISO:MGI. DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB. DR GO; GO:0044822; F:poly(A) RNA binding; ISO:MGI. DR GO; GO:0008283; P:cell proliferation; IMP:UniProtKB. DR GO; GO:0097150; P:neuronal stem cell maintenance; IMP:UniProtKB. DR GO; GO:0050769; P:positive regulation of neurogenesis; IMP:CACAO. DR GO; GO:0031053; P:primary miRNA processing; IMP:UniProtKB. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR InterPro; IPR007042; Arsenite-R_2. DR InterPro; IPR021933; DUF3546. DR Pfam; PF04959; ARS2; 1. DR Pfam; PF12066; DUF3546; 1. PE 1: Evidence at protein level; KW Acetylation; Activator; Alternative splicing; Complete proteome; KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; KW RNA-mediated gene silencing; Transcription; Transcription regulation. FT INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q9BXP5}. FT CHAIN 2 875 Serrate RNA effector molecule homolog. FT /FTId=PRO_0000220966. FT COMPBIAS 10 82 Arg-rich. FT COMPBIAS 258 401 Glu-rich. FT COMPBIAS 759 827 Pro-rich. FT MOD_RES 2 2 N-acetylglycine. FT {ECO:0000250|UniProtKB:Q9BXP5}. FT MOD_RES 4 4 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9BXP5}. FT MOD_RES 8 8 Phosphotyrosine. FT {ECO:0000250|UniProtKB:Q9BXP5}. FT MOD_RES 67 67 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9BXP5}. FT MOD_RES 74 74 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9BXP5}. FT MOD_RES 492 492 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9BXP5}. FT MOD_RES 539 539 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9BXP5}. FT MOD_RES 543 543 Phosphothreonine. FT {ECO:0000269|PubMed:15345747, FT ECO:0000269|PubMed:19131326}. FT MOD_RES 569 569 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9BXP5}. FT VAR_SEQ 775 779 ILPPG -> S (in isoform B and isoform C). FT {ECO:0000303|PubMed:16141072}. FT /FTId=VSP_000325. FT VAR_SEQ 809 815 Missing (in isoform C and isoform D). FT {ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:16141072}. FT /FTId=VSP_000326. FT CONFLICT 567 567 E -> G (in Ref. 3; BAE29458). FT {ECO:0000305}. SQ SEQUENCE 875 AA; 100452 MW; 9571445674452886 CRC64; MGDSDDEYDR RRRDKFRRER SDYDRSRERD ERRRGDDWND REWDRGRERR SRGEYRDYDR NRRERFSPPR HELSPPQKRM RRDWDEHSSD PYHSGYDMPY AGGGGGPTYG PPQPWGHPDV HIMQHHVLPI QARLGSIAEI DLGVPPPIMK SFKEFLLSLD DSVDETEAVK RYNDYKLDFR RQQMQDFFLA HKDEEWFRSK YHPDEVGKRR QEARGALQNR LKVFLSLMES GWFDNLLLDI DKADAIVKML DAAVIKMEGG TENDLRILEQ EEEEEQAGKT GEASKKEEAR AGPALGEGER KANDKDEKKE DGKQAENDSS NDDKTKKSEG DGDKEEKKEE AEKEAKKSKK RNRKQSGDDS FDEGSVSESE SESEGGQAEE EKEEAEEALK EKEKPKEEEK EKPKDAAGLE CKPRPLHKTC SLFMRNIAPN ISRAEIISLC KRYPGFMRVA LSEPQPERRF FRRGWVTFDR SVNIKEICWN LQNIRLRECE LSPGVNRDLT RRVRNINGIT QHKQIVRNDI KLAAKLIHTL DDRTQLWASE PGTPPVPTSL PSQNPILKNI TDYLIEEVSA EEEELLGSSG GPPPEEPPKE GNPAEINVER DEKLIKVLDK LLLYLRIVHS LDYYNTCEYP NEDEMPNRCG IIHVRGPMPP NRISHGEVLE WQKTFEEKLT PLLSVRESLS EEEAQKMGRK DPEQEVEKFV TSNTQELGKD KWLCPLSGKK FKGPEFVRKH IFNKHAEKIE EVKKEVAFFN NFLTDAKRPA LPEIKPAQPP GPAQILPPGL TPGLPYPHQT PQGLMPYGQP RPPILGYGAG AVRPAVPTGG PPYPHAPYGA GRGNYDAFRG QGGYPGKPRN RMVRGDPRAI VEYRDLDAPD DVDFF //