SKI3_YEAST
ID SKI3_YEAST Reviewed; 1432 AA.
AC P17883; Q06585;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Superkiller protein 3;
GN Name=SKI3; OrderedLocusNames=YPR189W; ORFNames=P9677.7;
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], AND SUBCELLULAR LOCATION.
RX PubMed=2660461; DOI=10.1002/yea.320050304;
RA Rhee S.-K., Icho T., Wickner R.B.;
RT "Structure and nuclear localization signal of the SKI3 antiviral protein of
RT Saccharomyces cerevisiae.";
RL Yeast 5:149-158(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [3]
RP GENOME REANNOTATION.
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=363683; DOI=10.1128/jb.136.3.1002-1007.1978;
RA Toh-e A., Guerry P., Wickner R.B.;
RT "Chromosomal superkiller mutants of Saccharomyces cerevisiae.";
RL J. Bacteriol. 136:1002-1007(1978).
RN [5]
RP FUNCTION.
RX PubMed=6371496; DOI=10.1128/mcb.4.4.761-770.1984;
RA Ridley S.P., Sommer S.S., Wickner R.B.;
RT "Superkiller mutations in Saccharomyces cerevisiae suppress exclusion of M2
RT double-stranded RNA by L-A-HN and confer cold sensitivity in the presence
RT of M and L-A-HN.";
RL Mol. Cell. Biol. 4:761-770(1984).
RN [6]
RP DOMAINS TPR REPEATS.
RX PubMed=2404612; DOI=10.1016/0092-8674(90)90745-z;
RA Sikorski R.S., Boguski M.S., Goebl M., Hieter P.A.;
RT "A repeating amino acid motif in CDC23 defines a family of proteins and a
RT new relationship among genes required for mitosis and RNA synthesis.";
RL Cell 60:307-317(1990).
RN [7]
RP FUNCTION.
RX PubMed=7739552; DOI=10.1128/mcb.15.5.2719;
RA Johnson A.W., Kolodner R.D.;
RT "Synthetic lethality of sep1 (xrn1) ski2 and sep1 (xrn1) ski3 mutants of
RT Saccharomyces cerevisiae is independent of killer virus and suggests a
RT general role for these genes in translation control.";
RL Mol. Cell. Biol. 15:2719-2727(1995).
RN [8]
RP FUNCTION.
RX PubMed=7739557; DOI=10.1128/mcb.15.5.2763;
RA Masison D.C., Blanc A., Ribas J.C., Carroll K., Sonenberg N., Wickner R.B.;
RT "Decoying the cap- mRNA degradation system by a double-stranded RNA virus
RT and poly(A)- mRNA surveillance by a yeast antiviral system.";
RL Mol. Cell. Biol. 15:2763-2771(1995).
RN [9]
RP FUNCTION.
RX PubMed=9482746; DOI=10.1093/emboj/17.5.1497;
RA Anderson J.S.J., Parker R.P.;
RT "The 3' to 5' degradation of yeast mRNAs is a general mechanism for mRNA
RT turnover that requires the SKI2 DEVH box protein and 3' to 5' exonucleases
RT of the exosome complex.";
RL EMBO J. 17:1497-1506(1998).
RN [10]
RP FUNCTION, IDENTIFICATION IN THE SKI COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=10744028; DOI=10.1017/s1355838200991787;
RA Brown J.T., Bai X., Johnson A.W.;
RT "The yeast antiviral proteins Ski2p, Ski3p, and Ski8p exist as a complex in
RT vivo.";
RL RNA 6:449-457(2000).
RN [11]
RP INTERACTION WITH SKI7, AND FUNCTION OF THE SKI COMPLEX.
RX PubMed=11532933; DOI=10.1093/emboj/20.17.4684;
RA Araki Y., Takahashi S., Kobayashi T., Kajiho H., Hoshino S., Katada T.;
RT "Ski7p G protein interacts with the exosome and the Ski complex for 3'-to-
RT 5' mRNA decay in yeast.";
RL EMBO J. 20:4684-4693(2001).
RN [12]
RP FUNCTION OF THE SKI COMPLEX.
RX PubMed=11720286;
RA Brown J.T., Johnson A.W.;
RT "A cis-acting element known to block 3' mRNA degradation enhances
RT expression of polyA-minus mRNA in wild-type yeast cells and phenocopies a
RT ski mutant.";
RL RNA 7:1566-1577(2001).
RN [13]
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 [14]
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 [15]
RP FUNCTION.
RX PubMed=14671320; DOI=10.1073/pnas.2536857100;
RA Kushner D.B., Lindenbach B.D., Grdzelishvili V.Z., Noueiry A.O., Paul S.M.,
RA Ahlquist P.;
RT "Systematic, genome-wide identification of host genes affecting replication
RT of a positive-strand RNA virus.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:15764-15769(2003).
RN [16]
RP MODELING OF THE SKI COMPLEX 3D-STRUCTURE.
RX PubMed=15044803; DOI=10.1126/science.1092645;
RA Aloy P., Boettcher B., Ceulemans H., Leutwein C., Mellwig C., Fischer S.,
RA Gavin A.-C., Bork P., Superti-Furga G., Serrano L., Russell R.B.;
RT "Structure-based assembly of protein complexes in yeast.";
RL Science 303:2026-2029(2004).
CC -!- FUNCTION: Component of the SKI complex involved in 3'-mRNA degradation
CC pathway. Represses dsRNA virus propagation by specifically blocking
CC translation of viral mRNAs, perhaps recognizing the absence of CAP or
CC poly(A). Essential for cell growth only in the presence of M1 replicon.
CC {ECO:0000269|PubMed:10744028, ECO:0000269|PubMed:11532933,
CC ECO:0000269|PubMed:11720286, ECO:0000269|PubMed:14671320,
CC ECO:0000269|PubMed:363683, ECO:0000269|PubMed:6371496,
CC ECO:0000269|PubMed:7739552, ECO:0000269|PubMed:7739557,
CC ECO:0000269|PubMed:9482746}.
CC -!- SUBUNIT: Component of the SKI complex composed of at least SKI2, SKI3
CC and SKI8. The SKI complex interacts with SKI7, which makes the link
CC between the SKI complex and the exosome in order to perform mRNA
CC degradation. {ECO:0000269|PubMed:10744028,
CC ECO:0000269|PubMed:11532933}.
CC -!- INTERACTION:
CC P17883; P35207: SKI2; NbExp=11; IntAct=EBI-1861, EBI-1851;
CC P17883; Q08491: SKI7; NbExp=2; IntAct=EBI-1861, EBI-1389;
CC P17883; Q02793: SKI8; NbExp=8; IntAct=EBI-1861, EBI-17260;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- MISCELLANEOUS: Present with 11900 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
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DR EMBL; L36940; AAA50573.1; -; Genomic_DNA.
DR EMBL; U25841; AAB64618.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11605.1; -; Genomic_DNA.
DR PIR; S58819; S58819.
DR RefSeq; NP_015515.1; NM_001184286.1.
DR PDB; 4BUJ; X-ray; 3.70 A; B/F=1-1432.
DR PDB; 5MC6; EM; 3.80 A; i=1-1432.
DR PDBsum; 4BUJ; -.
DR PDBsum; 5MC6; -.
DR AlphaFoldDB; P17883; -.
DR SMR; P17883; -.
DR BioGRID; 36361; 265.
DR ComplexPortal; CPX-1040; SKI complex.
DR DIP; DIP-6379N; -.
DR IntAct; P17883; 40.
DR MINT; P17883; -.
DR STRING; 4932.YPR189W; -.
DR iPTMnet; P17883; -.
DR MaxQB; P17883; -.
DR PaxDb; P17883; -.
DR PRIDE; P17883; -.
DR EnsemblFungi; YPR189W_mRNA; YPR189W; YPR189W.
DR GeneID; 856319; -.
DR KEGG; sce:YPR189W; -.
DR SGD; S000006393; SKI3.
DR VEuPathDB; FungiDB:YPR189W; -.
DR eggNOG; KOG1127; Eukaryota.
DR GeneTree; ENSGT00390000016407; -.
DR HOGENOM; CLU_001688_0_0_1; -.
DR InParanoid; P17883; -.
DR OMA; FNLWKAV; -.
DR BioCyc; YEAST:G3O-34312-MON; -.
DR Reactome; R-SCE-429958; mRNA decay by 3' to 5' exoribonuclease.
DR PRO; PR:P17883; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P17883; protein.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0055087; C:Ski complex; IDA:SGD.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0006402; P:mRNA catabolic process; IDA:ComplexPortal.
DR GO; GO:0070478; P:nuclear-transcribed mRNA catabolic process, 3'-5' exonucleolytic nonsense-mediated decay; IMP:SGD.
DR GO; GO:0034427; P:nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5'; IDA:ComplexPortal.
DR GO; GO:0070481; P:nuclear-transcribed mRNA catabolic process, non-stop decay; IMP:SGD.
DR Gene3D; 1.25.40.10; -; 5.
DR InterPro; IPR039226; Ski3/TTC37.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR040962; TPR_22.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR15704; PTHR15704; 1.
DR Pfam; PF18833; TPR_22; 1.
DR Pfam; PF13181; TPR_8; 2.
DR SMART; SM00028; TPR; 8.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 7.
DR PROSITE; PS50293; TPR_REGION; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; Cytoplasm; Nucleus; Reference proteome;
KW Repeat; TPR repeat.
FT CHAIN 1..1432
FT /note="Superkiller protein 3"
FT /id="PRO_0000106323"
FT REPEAT 4..37
FT /note="TPR 1"
FT REPEAT 47..80
FT /note="TPR 2"
FT REPEAT 425..458
FT /note="TPR 3"
FT REPEAT 471..507
FT /note="TPR 4"
FT REPEAT 508..541
FT /note="TPR 5"
FT REPEAT 627..661
FT /note="TPR 6"
FT REPEAT 702..735
FT /note="TPR 7"
FT REPEAT 736..769
FT /note="TPR 8"
FT REPEAT 945..985
FT /note="TPR 9"
FT REPEAT 987..1018
FT /note="TPR 10"
FT REPEAT 1226..1259
FT /note="TPR 11"
FT REGION 339..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..385
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 985
FT /note="T -> I (in Ref. 1; AAA50573)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1432 AA; 163726 MW; 18FFF78D7CA5A6E4 CRC64;
MSDIKQLLKE AKQELTNRDY EETIEISEKV LKLDPDNYFA HIFLGKALSS LPASNNVSSN
RNLERATNHY VSAAKLVPDN LLAWKGLFLL FRTTEVVPDI LSYDEYFDLC GQYADALLKQ
EQSQVELIND IKLLKKTHPD CQKAFYQHLK PGSLMAETIG RHLSTPQDAL LNLIKILSNI
ETTEIGKTLS QNRLKLKASD PDYQIKLNSF SWEIIKNSEI DQLYNQLVNI LADDQKRSEI
ENQWLEYRIK VLKSMPLDVK KDFFTKVKEM VEDMVLVNHQ SLLAWQKYFE WTDYEDLDNM
DAPLIIKYFK KFPKDPLAMI LYSWLSSKLS KYDIKSLESA NKPPEGHKKT EKETDIKDVD
ETNEDEVKDR VEDEVKDRVE DEVKDQDEEA KEDEEEDLDD IEIGLLEEEV VTVLTENIVK
CKNNILAHRI LCQYYLLTKE YEAALPYIKN GISLIAYNIK DLGVHLPLTK REFSLDLATV
YTYVDAPKDH NAALKLYDNI LSGDFSNIQA KMGKGIIFIE RKNWKDAMTL LTQVHEQSPN
NLEVLSELSW SKAHMGYMDE ALAGLDTVIK GIKGMDLRSI DFRALNLWRQ AKVYIMKHAS
INDAKQENVK CAFKLLIQSI KILDTFAPGF STLGDIYCHY YKDHLRAFKC YFKAFDLDAG
DYTAAKYITE TYASKPNWQA ASSIASRLIK GEKAKAELRS NNWPFRVVGI AHLEKQEESD
SIEWFQSALR VDPNDVESWV GLGQAYHACG RIEASIKVFD KAIQLRPSHT FAQYFKAISL
CDVGEYLESL DILEKVCQEA ATEESFQIGL VEVLMRCSLD LYSQGFLLKS VSIAKDTIER
IKIIISELKC ENQQVWIYLS QVLRLFIWIE SKVDTLPVES LVSIFENSQF SGSEEIDSVD
NIKIDTLLDS TTDDNVSIAC KFLILASKYS VSDQKFTDIA GTVRASYWYN IGISELTAFI
TLKEPQYRDA AIFAFKKSIQ LQSNTSETWI GLGIATMDIN FRVSQHCFIK ATALEPKATN
TWFNLAMLGL KKKDTEFAQQ VLNKLQSLAP QDSSPWLGMA LILEEQGDII GSSKLFAHSF
ILSNGRSKAA QFMYAKNVLE NHINNGDDER DIETVEKLTT ASIALEQFFK KSPDSQFALQ
CALLTLERLH HYENANELAN RLIGILEKKF EKTQDERELF NFAIIKGQFA RIHLGLGNFE
LSIENADLSQ GIISESSDEK SMKTKISNHI CLGLSYFFLN DFDQTLNQFQ ELLSISKDSK
HLVVLIAKVL YDVGESDTKE IALQELTEYI ATSGADLLVT LTIAAMSILD DKREDLSIIL
EELKALPLSK QIIDKHKDAP YLIEEITKRL YRNDTGKQVW QRSAYFFPNN LKVWERLDKN
IQRRIASNGQ NKVTAEEMSK LYCESKNLRS IQRGMFLCPW NVTAVKALNE CF
