RQC2_SCHPO
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 03-AUG-2022, entry version 103.
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}.
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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; 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; 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
