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 25-MAY-2022, entry version 102. 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; Schizosaccharomycetaceae; OC 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., Collins M., RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., RA 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 fission RT yeast Schizosaccharomyces pombe."; RL Nat. Biotechnol. 24:841-847(2006). RN [3] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-478, AND IDENTIFICATION BY RP 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., Loew D., RA 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: As part of the ribosome quality control complex (RQC), a CC ribosome-associated complex, mediates the extraction of incompletely CC synthesized nascent chains from stalled ribosomes as well as their CC ubiquitin-mediated proteasomal degradation. Thereby, frees ribosomes CC from the stalled translation complex and prevents the accumulation of CC nascent polypeptide chains that are potentially toxic for the cell. CC Mtr1/rqc2 is responsible for selective recognition of stalled 60S CC subunits by recognizing an exposed, nascent chain-conjugated tRNA CC moiety. Mtr1/rqc2 is important for the stable association of the E3 CC ubiquitin-protein ligase rkr1/ltn1 to the complex. Mtr1/rqc2 recruits CC alanine- and threonine-charged tRNA to the A site and directs the CC elongation of stalled nascent chains independently of mRNA or 40S CC subunits, leading to non-templated C-terminal Ala and Thr extensions CC (CAT tails). CAT tails induce a heat shock response. CC {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, as CC well as cdc48 and its ubiquitin-binding cofactors associated with the CC 60S ribosomal subunit. RQC2 binds to the 40S-binding surface of tRNAs. CC {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 AlphaFoldDB; Q9USN8; -. DR SMR; Q9USN8; -. DR BioGRID; 275330; 5. DR STRING; 4896.SPCC132.01c.1; -. DR iPTMnet; Q9USN8; -. DR MaxQB; Q9USN8; -. DR PaxDb; Q9USN8; -. DR EnsemblFungi; SPCC132.01c.1; SPCC132.01c.1:pep; SPCC132.01c. DR GeneID; 2538747; -. DR KEGG; spo:SPCC132.01c; -. DR PomBase; SPCC132.01c; mtr1. DR VEuPathDB; FungiDB:SPCC132.01c; -. DR eggNOG; KOG2030; Eukaryota. DR HOGENOM; CLU_003612_1_1_1; -. DR InParanoid; Q9USN8; -. DR OMA; MGAWWVN; -. 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:0043023; F:ribosomal large subunit binding; IBA:GO_Central. DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central. DR GO; GO:0140708; P:CAT tailing; ISS:UniProtKB. DR GO; GO:0072344; P:rescue of stalled ribosome; IBA:GO_Central. DR GO; GO:1990116; P:ribosome-associated ubiquitin-dependent protein catabolic process; IBA:GO_Central. DR InterPro; IPR021846; NFACT-C. DR InterPro; IPR008532; NFACT_RNA-bd. DR Pfam; PF11923; NFACT-C; 1. DR Pfam; PF05670; NFACT-R_1; 1. PE 1: Evidence at protein level; KW Coiled coil; Cytoplasm; Phosphoprotein; Reference proteome. FT CHAIN 1..1021 FT /note="Ribosome quality control complex subunit 2" FT /id="PRO_0000116820" FT REGION 457..484 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 746..801 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 832..905 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 348..388 FT /evidence="ECO:0000255" FT COILED 507..546 FT /evidence="ECO:0000255" FT COILED 698..727 FT /evidence="ECO:0000255" FT COMPBIAS 465..480 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 746..762 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 763..800 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 839..859 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 877..905 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 478 FT /note="Phosphoserine" FT /evidence="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 //