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 10-FEB-2021, entry version 98. 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: Component of the ribosome quality control complex (RQC), a CC ribosome-associated complex that mediates ubiquitination and extraction CC of incompletely synthesized nascent chains for proteasomal degradation. 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 rkr1/ltn1 CC to the complex. Mtr1/rqc2 recruits alanine- and threonine-charged tRNA CC to the A site and directs the elongation of stalled nascent chains CC independently of mRNA or 40S subunits, leading to non-templated C- CC terminal Ala and Thr extensions (CAT tails). CAT tails induce a heat CC shock 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, as CC well as cdc48 and its ubiquitin-binding cofactors. RQC forms a stable CC complex with 60S ribosomal subunits. RQC2 binds to the 40S-binding CC 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 SMR; Q9USN8; -. DR BioGRID; 275330; 5. 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 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; CEAGAWC; -. 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:0072344; P:rescue of stalled ribosome; IBA:GO_Central. DR GO; GO:1990116; P:ribosome-associated ubiquitin-dependent protein catabolic process; ISO:PomBase. 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 COILED 348..388 FT /evidence="ECO:0000255" FT COILED 507..546 FT /evidence="ECO:0000255" FT COILED 698..727 FT /evidence="ECO:0000255" 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 //