ID RQC2_SCHPO Reviewed; 1021 AA. AC Q9USN8; O94551; DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 29-MAR-2004, sequence version 2. DT 28-FEB-2018, entry version 86. DE RecName: Full=Ribosome quality control complex subunit 2 {ECO:0000250|UniProtKB:Q12532}; DE AltName: Full=Microtubule regulator protein 1 {ECO:0000303|PubMed:24928430}; GN Name=mtr1 {ECO:0000303|PubMed:24928430}; GN ORFNames=SPCC132.01c {ECO:0000312|PomBase:SPCC132.01c}, SPCC1322.17c; OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; OC Schizosaccharomycetes; Schizosaccharomycetales; OC Schizosaccharomycetaceae; Schizosaccharomyces. OX NCBI_TaxID=284812; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=972 / ATCC 24843; RX PubMed=11859360; DOI=10.1038/nature724; RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., RA Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., RA Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., RA James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., RA Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., RA Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., RA Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., RA Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., RA Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., RA Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., RA Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., RA Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., RA Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., RA Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., RA Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., RA Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., RA Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., RA Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.; RT "The genome sequence of Schizosaccharomyces pombe."; RL Nature 415:871-880(2002). RN [2] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=16823372; DOI=10.1038/nbt1222; RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., RA Yoshida M.; RT "ORFeome cloning and global analysis of protein localization in the RT fission yeast Schizosaccharomyces pombe."; RL Nat. Biotechnol. 24:841-847(2006). RN [3] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-478, AND IDENTIFICATION RP BY MASS SPECTROMETRY. RX PubMed=18257517; DOI=10.1021/pr7006335; RA Wilson-Grady J.T., Villen J., Gygi S.P.; RT "Phosphoproteome analysis of fission yeast."; RL J. Proteome Res. 7:1088-1097(2008). RN [4] RP SUBCELLULAR LOCATION. RX PubMed=24928430; DOI=10.1242/bio.20148607; RA Carlier-Grynkorn F., Ji L., Fraisier V., Lombard B., Dingli F., RA Loew D., Paoletti A., Ronot X., Tran P.T.; RT "Fission yeast mtr1p regulates interphase microtubule cortical dwell- RT time."; RL Biol. Open 3:591-596(2014). CC -!- FUNCTION: Component of the ribosome quality control complex (RQC), CC a ribosome-associated complex that mediates ubiquitination and CC extraction of incompletely synthesized nascent chains for CC proteasomal degradation. Mtr1/rqc2 is responsible for selective CC recognition of stalled 60S subunits by recognizing an exposed, CC nascent chain-conjugated tRNA moiety. Mtr1/rqc2 is important for CC the stable association of rkr1/ltn1 to the complex. Mtr1/rqc2 CC recruits alanine- and threonine-charged tRNA to the A site and CC directs the elongation of stalled nascent chains independently of CC mRNA or 40S subunits, leading to non-templated C-terminal Ala and CC Thr extensions (CAT tails). CAT tails induce a heat shock CC response. {ECO:0000250|UniProtKB:Q12532}. CC -!- SUBUNIT: Component of the ribosome quality control complex (RQC), CC composed of the E3 ubiquitin ligase rkr1/ltn1, rqc1 and mtr1/rqc2, CC as well as cdc48 and its ubiquitin-binding cofactors. RQC forms a CC stable complex with 60S ribosomal subunits. RQC2 binds to the 40S- CC binding surface of tRNAs. {ECO:0000250|UniProtKB:Q12532}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372, CC ECO:0000269|PubMed:24928430}. CC -!- SIMILARITY: Belongs to the NEMF family. {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; CU329672; CAA22870.1; -; Genomic_DNA. DR PIR; T40928; T40928. DR RefSeq; NP_588145.2; NM_001023135.2. DR BioGrid; 275330; 3. DR STRING; 4896.SPCC132.01c.1; -. DR iPTMnet; Q9USN8; -. DR MaxQB; Q9USN8; -. DR PaxDb; Q9USN8; -. DR PRIDE; Q9USN8; -. DR EnsemblFungi; SPCC132.01c.1; SPCC132.01c.1:pep; SPCC132.01c. DR GeneID; 2538747; -. DR KEGG; spo:SPCC132.01c; -. DR EuPathDB; FungiDB:SPCC132.01c; -. DR PomBase; SPCC132.01c; mtr1. DR InParanoid; Q9USN8; -. DR OMA; FEWPKNV; -. DR OrthoDB; EOG092C0NXU; -. DR PhylomeDB; Q9USN8; -. DR PRO; PR:Q9USN8; -. DR Proteomes; UP000002485; Chromosome III. DR GO; GO:0005829; C:cytosol; HDA:PomBase. DR GO; GO:1990112; C:RQC complex; ISO:PomBase. DR GO; GO:1990116; P:ribosome-associated ubiquitin-dependent protein catabolic process; ISO:PomBase. DR InterPro; IPR021846; DUF3441. DR InterPro; IPR008532; DUF814. DR Pfam; PF11923; DUF3441; 1. DR Pfam; PF05670; DUF814; 1. PE 1: Evidence at protein level; KW Coiled coil; Complete proteome; Cytoplasm; Phosphoprotein; KW Reference proteome. FT CHAIN 1 1021 Ribosome quality control complex subunit FT 2. FT /FTId=PRO_0000116820. FT COILED 348 388 {ECO:0000255}. FT COILED 507 546 {ECO:0000255}. FT COILED 698 727 {ECO:0000255}. FT MOD_RES 478 478 Phosphoserine. FT {ECO:0000269|PubMed:18257517}. SQ SEQUENCE 1021 AA; 114240 MW; 5308EEA9AEC52178 CRC64; MKQRFSALDI AAIAAELREQ VVGCRLNNFY DLNARTFLLK FGKQDAKYSI VIESGFRAHL TKFDRENAPL SGFVTKLRKH IKSRRLTGVS QLGTDRVLVF TFGGGANDQD PDWTYYLVCE FFAAGNVLLL DGHYKILSLL RVVTFDKDQV YAVGQKYNLD KNNLVNDNKS QSTIPHMTAE RLNILLDEIS TAYASPTSIN EPLPDQQLSS STKPIKVPKP VSLRKALTIR LGEYGNALIE HCLRRSKLDP LFPACQLCAD ETKKNDLLAA FQEADSILAA VNKPPVKGYI FSLEQALTNA ADPQHPEECT TLYEDFHPFQ PLQLVQANRK CMEFPTYNEC VDEFFSSIEA QKLKKRAHDR LATAERRLES AKEDQARKLQ SLQDAQATCA LRAQAIEMNP ELVEAIISYI NSLLNQGMDW LDIEKLIQSQ KRRSPVAAAI QIPLKLIKNA VTVFLPNPES VDNSDESSET SDDDLDDSDD DNKVKEGKVS SKFIAVELDL SLGAFANARK QYELRREALI KETKTAEAAS KALKSTQRKI EQDLKRSTTA DTQRILLGRK TFFFEKFHWF ISSEGYLVLG GRDAQQNELL FQKYCNTGDI FVCADLPKSS IIIVKNKNPH DPIPPNTLQQ AGSLALASSK AWDSKTVISA WWVRIDEVSK LAPTGEILPT GSFAIRAKKN YLPPTVLIMG YGILWQLDEK SSERRKARRL EMEVVETQGK VSELKMEGTS VTSEDNIQDV VSEVSYNEDT NNQSTPDTTG SDIHIVSEKR GKKGSKVITA KKVSAKERRE ARRARRQTAL EESLKAPISI EDATDPQTIL AILKQKKAKK KHAAREMEIS SQIPSNDSSN VQTPTAESEI EEDGVSEPIS AEVIEDQSRN SEAENEKGLS TEQRDEKKHA KVESFQRQEM PRSLFEEIFF AIDSLTPNPQ QQDTVINAVP TFAPYNAMTK FNQKVKVMPG TGKVGKAARE SIAYFMKKLP KSSKEAAYLE NLKDGEIVAP ISVSRLKMVF GSSGNTKKSK K //