SLH1_YEAST
ID SLH1_YEAST Reviewed; 1967 AA.
AC P53327; D6VV48;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=RQC trigger complex helicase SLH1 {ECO:0000303|PubMed:28757607};
DE EC=3.6.4.13 {ECO:0000305|PubMed:28757607, ECO:0000305|PubMed:32203490};
DE AltName: Full=Antiviral helicase SLH1;
DE AltName: Full=SKI2-like helicase 1;
GN Name=SLH1 {ECO:0000303|PubMed:10922069};
GN Synonyms=RQT2 {ECO:0000303|PubMed:28757607};
GN OrderedLocusNames=YGR271W {ECO:0000312|SGD:S000003503}; ORFNames=G9365;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9133744;
RX DOI=10.1002/(sici)1097-0061(19970330)13:4<391::aid-yea92>3.0.co;2-q;
RA Martegani E., Vanoni M., Mauri I., Rudoni S., Saliola M., Alberghina L.;
RT "Identification of gene encoding a putative RNA-helicase, homologous to
RT SKI2, in chromosome VII of Saccharomyces cerevisiae.";
RL Yeast 13:391-397(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [3]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 51; 193 AND 438.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP FUNCTION.
RX PubMed=10922069; DOI=10.1073/pnas.97.16.9133;
RA Searfoss A.M., Wickner R.B.;
RT "3' poly(A) is dispensable for translation.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9133-9137(2000).
RN [5]
RP FUNCTION.
RX PubMed=11438647; DOI=10.1128/mcb.21.15.4900-4908.2001;
RA Searfoss A., Dever T.E., Wickner R.;
RT "Linking the 3' poly(A) tail to the subunit joining step of translation
RT initiation: relations of Pab1p, eukaryotic translation initiation factor 5b
RT (Fun12p), and Ski2p-Slh1p.";
RL Mol. Cell. Biol. 21:4900-4908(2001).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION IN THE RQT COMPLEX,
RP INTERACTION WITH CUE3; RQT4 AND HEL2, DISRUPTION PHENOTYPE, AND MUTAGENESIS
RP OF LYS-316.
RX PubMed=28757607; DOI=10.1038/s41467-017-00188-1;
RA Matsuo Y., Ikeuchi K., Saeki Y., Iwasaki S., Schmidt C., Udagawa T.,
RA Sato F., Tsuchiya H., Becker T., Tanaka K., Ingolia N.T., Beckmann R.,
RA Inada T.;
RT "Ubiquitination of stalled ribosome triggers ribosome-associated quality
RT control.";
RL Nat. Commun. 8:159-159(2017).
RN [9]
RP FUNCTION, INTERACTION WITH HEL2, AND DISRUPTION PHENOTYPE.
RX PubMed=28223409; DOI=10.1261/rna.060897.117;
RA Sitron C.S., Park J.H., Brandman O.;
RT "Asc1, Hel2, and Slh1 couple translation arrest to nascent chain
RT degradation.";
RL RNA 23:798-810(2017).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION IN THE RQT COMPLEX, AND
RP MUTAGENESIS OF LYS-316.
RX PubMed=32203490; DOI=10.1038/s41594-020-0393-9;
RA Matsuo Y., Tesina P., Nakajima S., Mizuno M., Endo A., Buschauer R.,
RA Cheng J., Shounai O., Ikeuchi K., Saeki Y., Becker T., Beckmann R.,
RA Inada T.;
RT "RQT complex dissociates ribosomes collided on endogenous RQC substrate
RT SDD1.";
RL Nat. Struct. Mol. Biol. 27:323-332(2020).
CC -!- FUNCTION: Involved in activation of the ribosome quality control (RQC)
CC pathway, a pathway that degrades nascent peptide chains during
CC problematic translation (PubMed:28757607, PubMed:28223409,
CC PubMed:32203490). Drives the splitting of stalled ribosomes that are
CC polyubiquitinated in a HEL2-dependent manner, as part of the ribosome
CC quality control trigger (RQT) complex (PubMed:28757607,
CC PubMed:32203490). Also represses the translation of non-poly(A) mRNAs
CC together with SKI2 (PubMed:10922069). May block translation by
CC inhibiting translation initiation factor 5B (FUN12) action on mRNAs
CC lacking a 3' poly(A) structure (PubMed:11438647). Involved in antiviral
CC defense, preventing L-A dsRNA virus propagation by specifically
CC blocking translation of viral mRNAs (PubMed:10922069).
CC {ECO:0000269|PubMed:10922069, ECO:0000269|PubMed:11438647,
CC ECO:0000269|PubMed:28223409, ECO:0000269|PubMed:28757607,
CC ECO:0000269|PubMed:32203490}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000305|PubMed:28757607, ECO:0000305|PubMed:32203490};
CC -!- SUBUNIT: Component of the RQT (ribosome quality control trigger)
CC complex, composed of SLH1, CUE3, and RQT4 (PubMed:28757607,
CC PubMed:32203490). Interacts with CUE3 (PubMed:28757607). Interacts with
CC RQT4 (PubMed:28757607). Interacts with HEL2 (PubMed:28757607,
CC PubMed:28223409). Associates with translating ribosomes
CC (PubMed:28757607). {ECO:0000269|PubMed:28223409,
CC ECO:0000269|PubMed:28757607, ECO:0000269|PubMed:32203490}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:14562095}.
CC -!- DISRUPTION PHENOTYPE: Defective activation of the ribosome quality
CC control (RQC) pathway (PubMed:28757607, PubMed:28223409). Mildly
CC defective ribosome stalling induced by RNA arrest sequences
CC (PubMed:28223409). Sensitive to anisomycin (stalls ribosomes in the
CC rotated state) (PubMed:28757607). {ECO:0000269|PubMed:28223409,
CC ECO:0000269|PubMed:28757607}.
CC -!- MISCELLANEOUS: Present with 486 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC {ECO:0000305}.
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DR EMBL; U35242; AAC49699.1; -; Genomic_DNA.
DR EMBL; Z73056; CAA97301.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08359.2; -; Genomic_DNA.
DR PIR; S64604; S64604.
DR RefSeq; NP_011787.4; NM_001181400.4.
DR AlphaFoldDB; P53327; -.
DR SMR; P53327; -.
DR BioGRID; 33520; 154.
DR ComplexPortal; CPX-6643; RQT ribosome-associated quality control trigger complex.
DR DIP; DIP-5563N; -.
DR IntAct; P53327; 7.
DR MINT; P53327; -.
DR STRING; 4932.YGR271W; -.
DR iPTMnet; P53327; -.
DR MaxQB; P53327; -.
DR PaxDb; P53327; -.
DR PRIDE; P53327; -.
DR EnsemblFungi; YGR271W_mRNA; YGR271W; YGR271W.
DR GeneID; 853187; -.
DR KEGG; sce:YGR271W; -.
DR SGD; S000003503; SLH1.
DR VEuPathDB; FungiDB:YGR271W; -.
DR eggNOG; KOG0952; Eukaryota.
DR GeneTree; ENSGT00940000155377; -.
DR HOGENOM; CLU_000335_1_0_1; -.
DR InParanoid; P53327; -.
DR OMA; GTHHAGM; -.
DR BioCyc; YEAST:G3O-30937-MON; -.
DR PRO; PR:P53327; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53327; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0010494; C:cytoplasmic stress granule; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0004386; F:helicase activity; IMP:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0003724; F:RNA helicase activity; ISS:SGD.
DR GO; GO:0002181; P:cytoplasmic translation; IGI:SGD.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0006417; P:regulation of translation; IMP:SGD.
DR GO; GO:0072344; P:rescue of stalled ribosome; IMP:UniProtKB.
DR GO; GO:0032790; P:ribosome disassembly; IMP:UniProtKB.
DR GO; GO:1990116; P:ribosome-associated ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR Gene3D; 1.10.10.10; -; 2.
DR Gene3D; 2.60.40.150; -; 1.
DR Gene3D; 3.40.50.300; -; 4.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004179; Sec63-dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00270; DEAD; 2.
DR Pfam; PF00271; Helicase_C; 2.
DR Pfam; PF02889; Sec63; 2.
DR SMART; SM00382; AAA; 2.
DR SMART; SM00487; DEXDc; 2.
DR SMART; SM00490; HELICc; 2.
DR SMART; SM00973; Sec63; 2.
DR SUPFAM; SSF46785; SSF46785; 2.
DR SUPFAM; SSF52540; SSF52540; 4.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 2.
DR PROSITE; PS51194; HELICASE_CTER; 2.
PE 1: Evidence at protein level;
KW Antiviral defense; ATP-binding; Cytoplasm; Helicase; Hydrolase;
KW Nucleotide-binding; Reference proteome; Repeat; Translation regulation.
FT CHAIN 1..1967
FT /note="RQC trigger complex helicase SLH1"
FT /id="PRO_0000102085"
FT DOMAIN 297..485
FT /note="Helicase ATP-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 516..735
FT /note="Helicase C-terminal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 795..1100
FT /note="SEC63 1"
FT DOMAIN 1149..1324
FT /note="Helicase ATP-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1355..1550
FT /note="Helicase C-terminal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 1626..1776
FT /note="SEC63 2"
FT MOTIF 427..430
FT /note="DEVH box"
FT MOTIF 1266..1269
FT /note="DEAH box"
FT BINDING 310..317
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 1162..1169
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MUTAGEN 316
FT /note="K->R: Abolishes splitting of stalled ribosomes.
FT Defective activation of the ribosome quality control (RQC)
FT pathway. Does not affect the association of the RQT complex
FT with ribosomes."
FT /evidence="ECO:0000269|PubMed:28757607,
FT ECO:0000269|PubMed:32203490"
FT CONFLICT 27
FT /note="F -> L (in Ref. 1; AAC49699)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="Q -> P (in Ref. 1; AAC49699 and 2; CAA97301)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="K -> E (in Ref. 1; AAC49699 and 2; CAA97301)"
FT /evidence="ECO:0000305"
FT CONFLICT 438
FT /note="S -> P (in Ref. 1; AAC49699 and 2; CAA97301)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1967 AA; 224850 MW; 249DF515AEE511A1 CRC64;
MSTEYSADSS KSFMIAMQSM IDTSQTFNLD RSKISLPDFD DELKKVQKDE QNQRTELTVL
SQDRNDWDDI FEEFKDISFA QLQSIIDSYK TKNAVAVYKK IGKLINEAET TLSSNVLLET
VLQMVYKHQK QELEKELLDF LGTGNIDLVS LLLQHRRMIV ATPIETTILL IKNAVNSTPE
FLTQQDIRNQ VLKSAEDAKN RKLNPATKII KYPHVFRKYE AGSTTAMAFA GQKFTLPVGT
TRMSYNTHEE IIIPAADQAS NKNYLYTKLL KISDLDHFCK TVFPYETLNQ IQSLVYPVAY
KTNENMLICA PTGAGKTDIA LLTIINTIKQ FSVVNGENEI DIQYDDFKVI YVAPLKALAA
EIVDKFSKKL APFNIQVREL TGDMQLTKAE ILATQVIVTT PEKWDVVTRK ANGDNDLVSK
VKLLIIDEVH LLHEDRGSVI ETLVARTLRQ VESSQSMIRI IGLSATLPNF MDVADFLGVN
RQIGMFYFDQ SFRPKPLEQQ LLGCRGKAGS RQSKENIDKV AYDKLSEMIQ RGYQVMVFVH
SRKETVKSAR NFIKLAESNH EVDLFAPDPI EKDKYSRSLV KNRDKDMKEI FQFGFGIHHA
GMARSDRNLT EKMFKDGAIK VLCCTATLAW GVNLPADCVI IKGTQVYDSK KGGFIDLGIS
DVIQIFGRGG RPGFGSANGT GILCTSNDRL DHYVSLITQQ HPIESRFGSK LVDNLNAEIS
LGSVTNVDEA IEWLGYTYMF VRMRKNPFTY GIDWEEIAND PQLYERRRKM IVVAARRLHA
LQMIVFDEVS MHFIAKDLGR VSSDFYLLNE SVEIFNQMCD PRATEADVLS MISMSSEFDG
IKFREEESKE LKRLSDESVE CQIGSQLDTP QGKANVLLQA YISQTRIFDS ALSSDSNYVA
QNSVRICRAL FLIGVNRRWG KFSNVMLNIC KSIEKRLWAF DHPLCQFDLP ENIIRRIRDT
KPSMEHLLEL EADELGELVH NKKAGSRLYK ILSRFPKINI EAEIFPITTN VMRIHIALGP
DFVWDSRIHG DAQFFWVFVE ESDKSQILHF EKFILNRRQL NNQHEMDFMI PLSDPLPPQV
VVKVVSDTWI GCESTHAISF QHLIRPFNET LQTKLLKLRP LPTSALQNPL IESIYPFKYF
NPMQTMTFYT LYNTNENAFV GSPTGSGKTI VAELAIWHAF KTFPGKKIVY IAPMKALVRE
RVDDWRKKIT PVTGDKVVEL TGDSLPDPKD VHDATIVITT PEKFDGISRN WQTRKFVQDV
SLIIMDEIHL LASDRGPILE MIVSRMNYIS SQTKQPVRLL GMSTAVSNAY DMAGWLGVKD
HGLYNFPSSV RPVPLKMYID GFPDNLAFCP LMKTMNKPVF MAIKQHSPDK PALIFVASRR
QTRLTALDLI HLCGMEDNPR RFLNIDDEEE LQYYLSQVTD DTLKLSLQFG IGLHHAGLVQ
KDRSISHQLF QKNKIQILIA TSTLAWGVNL PAHLVIIKGT QFFDAKIEGY RDMDLTDILQ
MMGRAGRPAY DTTGTAIVYT KESKKMFYKH FLNVGFPVES SLHKVLDDHL GAEITSGSIT
NKQEALDFLS WTFLFRRAHH NPTYYGIEDD TSTAGVSEHL SSLIDSTLEN LRESQCVLLH
GDDIVATPFL SISSYYYISH LTIRQLLKQI HDHATFQEVL RWLSLAVEYN ELPVRGGEII
MNEEMSQQSR YSVESTFTDE FELPMWDPHV KTFLLLQAHL SRVDLPIADY IQDTVSVLDQ
SLRILQAYID VASELGYFHT VLTMIKMMQC IKQGYWYEDD PVSVLPGLQL RRIKDYTFSE
QGFIEMTPQQ KKKKLLTLEE IGRFGYKKLL NVFDQLTFGM TESEDTKKRF VSVCQRLPVL
EGMKFEEQEN NEVLTFYSKH LSSKHNNGFE VYCDKFPKIQ KELWFLIGHK GDELLMIKRC
QPKQMNKEVI IHCDLFIPEE IRGEELQFSL INDALGLRYD MVHKLIS
