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 29-MAY-2024, entry version 111. 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: Key component of the ribosome quality control complex (RQC), CC a ribosome-associated complex that mediates the extraction of CC incompletely synthesized nascent chains from stalled ribosomes as well CC as their ubiquitin-mediated proteasomal degradation. Thereby, frees 60S CC subunit ribosomes from the stalled translation complex and prevents the CC accumulation of nascent polypeptide chains that are potentially toxic CC for the cell. Within the RQC complex, mtr1/rqc2 specifically binds CC stalled 60S ribosomal subunits by recognizing an exposed, nascent CC chain-conjugated tRNA moiety and promotes the recruitment of rkr1/ltn1 CC to stalled 60S subunits. Following binding to stalled 60S ribosomal CC subunits, mtr1/rqc2 mediates CAT tailing by recruiting alanine- and CC threonine-charged tRNA to the A-site and directing the elongation of CC stalled nascent chains independently of mRNA or 40S subunits, leading CC to non-templated C-terminal Ala and Thr extensions (CAT tails). CAT CC tails promote the rkr1/ltn1-mediated ubiquitination of incompletely CC synthesized nascent polypeptides: CAT tailing facilitates rkr1/ltn1- CC dependent ubiquitination by exposing lysine residues that would CC otherwise remain buried in the ribosomal exit tunnel. Following CC ubiquitination, incompletely synthesized nascent polypeptides are CC recognized by CDC48 and degraded by the proteasome. CAT-tailed proteins CC tend to aggregate and sequester chaperones and can induce proteotoxic CC stress; their rkr1/ltn1-dependent ubiquitination and degradation is CC required to prevent proteotoxic stress. {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; CAA22870.2; -; 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; 284812.Q9USN8; -. DR iPTMnet; Q9USN8; -. DR MaxQB; Q9USN8; -. DR PaxDb; 4896-SPCC132-01c-1; -. 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; MFLEFFA; -. DR PhylomeDB; Q9USN8; -. DR PRO; PR:Q9USN8; -. DR Proteomes; UP000002485; Chromosome III. DR GO; GO:0005737; C:cytoplasm; IDA:PomBase. DR GO; GO:0005829; C:cytosol; HDA:PomBase. DR GO; GO:1990112; C:RQC complex; IBA:GO_Central. 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 Gene3D; 2.30.310.10; ibrinogen binding protein from staphylococcus aureus domain; 1. DR InterPro; IPR021846; NFACT-C. DR InterPro; IPR008532; NFACT_RNA-bd. DR PANTHER; PTHR15239; NUCLEAR EXPORT MEDIATOR FACTOR NEMF; 1. DR PANTHER; PTHR15239:SF6; RIBOSOME QUALITY CONTROL COMPLEX SUBUNIT NEMF; 1. DR Pfam; PF11923; NFACT-C; 1. DR Pfam; PF05670; NFACT-R_1; 1. DR Pfam; PF05833; NFACT_N; 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 //