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 08-NOV-2023, entry version 108.
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}.
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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; 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: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 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; NUCLEAR EXPORT MEDIATOR FACTOR NEMF; 1.
DR Pfam; PF11923; NFACT-C; 1.
DR Pfam; PF05670; NFACT-R_1; 1.
DR Pfam; PF05833; NFACT_N; 2.
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
//