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 02-MAR-2010, entry version 59. 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. 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 MEDLINE=21138439; 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 SER-74, AND MASS RP SPECTROMETRY. RX PubMed=18973353; DOI=10.1021/pr800599n; RA Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., RA Faessler R., Mann M.; RT "Solid tumor proteome and phosphoproteome analysis by high resolution RT mass spectrometry."; RL J. Proteome Res. 7:5314-5326(2008). 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-543, AND MASS RP SPECTROMETRY. 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 [7] RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, RP INTERACTION WITH NCBP1 AND RNASEN, 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). 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 RNASEN, 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. CC -!- SUBUNIT: Interacts with CASP8AP2/FLASH, NCBP1/CBP80 and RNASEN. 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: Ubiquitously 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. CC -!- INDUCTION: Upon cell proliferation. 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. CC -!- SIMILARITY: Belongs to the ARS2 family. 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 IPI; IPI00224644; -. DR IPI; IPI00224645; -. DR IPI; IPI00266463; -. DR IPI; IPI00761620; -. DR RefSeq; NP_001103379.1; -. DR RefSeq; NP_001103380.1; -. DR RefSeq; NP_113582.1; -. DR UniGene; Mm.387734; -. DR STRING; Q99MR6; -. DR PhosphoSite; Q99MR6; -. DR PRIDE; Q99MR6; -. DR Ensembl; ENSMUST00000040873; ENSMUSP00000043123; ENSMUSG00000037364; Mus musculus. DR GeneID; 83701; -. DR KEGG; mmu:83701; -. DR UCSC; uc009acb.1; mouse. DR UCSC; uc009acc.1; mouse. DR CTD; 83701; -. DR MGI; MGI:1933527; Ars2. DR HOGENOM; HBG717208; -. DR InParanoid; Q99MR6; -. DR OMA; ICWNLNN; -. DR OrthoDB; EOG92Z79D; -. DR NextBio; 350735; -. DR ArrayExpress; Q99MR6; -. DR Bgee; Q99MR6; -. DR CleanEx; MM_ARS2; -. DR Genevestigator; Q99MR6; -. DR GermOnline; ENSMUSG00000037364; Mus musculus. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0008283; P:cell proliferation; IMP:UniProtKB. DR GO; GO:0031053; P:primary microRNA processing; IMP:UniProtKB. DR InterPro; IPR021933; DUF3546. DR Pfam; PF12066; DUF3546; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein; KW RNA-mediated gene silencing. FT CHAIN 1 875 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 8 8 Phosphotyrosine (By similarity). FT MOD_RES 67 67 Phosphoserine (By similarity). FT MOD_RES 74 74 Phosphoserine. FT MOD_RES 136 136 Phosphoserine (By similarity). FT MOD_RES 492 492 Phosphoserine (By similarity). FT MOD_RES 539 539 Phosphoserine (By similarity). FT MOD_RES 543 543 Phosphothreonine. FT MOD_RES 623 623 Phosphotyrosine (By similarity). FT MOD_RES 624 624 Phosphotyrosine (By similarity). FT VAR_SEQ 775 779 ILPPG -> S (in isoform B and isoform C). FT /FTId=VSP_000325. FT VAR_SEQ 809 815 Missing (in isoform C and isoform D). FT /FTId=VSP_000326. FT CONFLICT 567 567 E -> G (in Ref. 3; BAE29458). 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 //