CLU_YEAST
ID CLU_YEAST Reviewed; 1277 AA.
AC Q03690; D6VZI6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Clustered mitochondria protein 1;
DE AltName: Full=Translation initiation factor 31;
DE AltName: Full=eIF3-associated protein p135;
GN Name=CLU1 {ECO:0000255|HAMAP-Rule:MF_03013};
GN Synonyms=TIF31 {ECO:0000255|HAMAP-Rule:MF_03013};
GN OrderedLocusNames=YMR012W; ORFNames=YM8270.16;
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], PARTIAL PROTEIN SEQUENCE, AND
RP ASSOCIATION WITH THE EIF-3 COMPLEX.
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=10358023; DOI=10.1074/jbc.274.24.16802;
RA Vornlocher H.-P., Hanachi P., Ribeiro S., Hershey J.W.B.;
RT "A 110-kilodalton subunit of translation initiation factor eIF3 and an
RT associated 135-kilodalton protein are encoded by the Saccharomyces
RT cerevisiae TIF32 and TIF31 genes.";
RL J. Biol. Chem. 274:16802-16812(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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, AND DISRUPTION PHENOTYPE.
RX PubMed=9601101; DOI=10.1242/jcs.111.12.1717;
RA Fields S.D., Conrad M.N., Clarke M.;
RT "The S. cerevisiae CLU1 and D. discoideum cluA genes are functional
RT homologues that influence mitochondrial morphology and distribution.";
RL J. Cell Sci. 111:1717-1727(1998).
RN [5]
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 [6]
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND ASSOCIATION WITH THE 80S RIBOSOME.
RX PubMed=16215987; DOI=10.1002/jcb.20658;
RA Jao D.L., Chen K.Y.;
RT "Tandem affinity purification revealed the hypusine-dependent binding of
RT eukaryotic initiation factor 5A to the translating 80S ribosomal complex.";
RL J. Cell. Biochem. 97:583-598(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1247, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [9]
RP INDUCTION.
RX PubMed=19804647; DOI=10.1186/1471-2164-10-461;
RA Rintala E., Toivari M., Pitkanen J.P., Wiebe M.G., Ruohonen L.,
RA Penttila M.;
RT "Low oxygen levels as a trigger for enhancement of respiratory metabolism
RT in Saccharomyces cerevisiae.";
RL BMC Genomics 10:461-461(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1247, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: mRNA-binding protein involved in proper cytoplasmic
CC distribution of mitochondria. {ECO:0000255|HAMAP-Rule:MF_03013,
CC ECO:0000269|PubMed:9601101}.
CC -!- SUBUNIT: May associate with the eukaryotic translation initiation
CC factor 3 (eIF-3) complex. Associates with the 80S ribosome.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03013,
CC ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: Expression is increased in intermediate compared to fully
CC aerobic conditions. {ECO:0000269|PubMed:19804647}.
CC -!- DISRUPTION PHENOTYPE: Causes mitochondria to cluster within cells.
CC {ECO:0000269|PubMed:9601101}.
CC -!- MISCELLANEOUS: Present with 17000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CLU family. {ECO:0000255|HAMAP-
CC Rule:MF_03013}.
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DR EMBL; AF004911; AAB82415.1; -; Genomic_DNA.
DR EMBL; Z48613; CAA88529.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09910.1; -; Genomic_DNA.
DR PIR; S53043; S53043.
DR RefSeq; NP_013725.1; NM_001182508.1.
DR AlphaFoldDB; Q03690; -.
DR SMR; Q03690; -.
DR BioGRID; 35182; 160.
DR DIP; DIP-5924N; -.
DR IntAct; Q03690; 78.
DR MINT; Q03690; -.
DR STRING; 4932.YMR012W; -.
DR iPTMnet; Q03690; -.
DR MaxQB; Q03690; -.
DR PaxDb; Q03690; -.
DR PRIDE; Q03690; -.
DR EnsemblFungi; YMR012W_mRNA; YMR012W; YMR012W.
DR GeneID; 855025; -.
DR KEGG; sce:YMR012W; -.
DR SGD; S000004614; CLU1.
DR VEuPathDB; FungiDB:YMR012W; -.
DR eggNOG; KOG1839; Eukaryota.
DR GeneTree; ENSGT00390000012485; -.
DR HOGENOM; CLU_003256_2_0_1; -.
DR InParanoid; Q03690; -.
DR OMA; VSGFYVN; -.
DR BioCyc; YEAST:G3O-32720-MON; -.
DR PRO; PR:Q03690; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q03690; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0010494; C:cytoplasmic stress granule; HDA:SGD.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0003723; F:RNA binding; IDA:SGD.
DR GO; GO:0048312; P:intracellular distribution of mitochondria; IBA:GO_Central.
DR CDD; cd15466; CLU-central; 1.
DR Gene3D; 1.25.40.10; -; 1.
DR HAMAP; MF_03013; CLU; 1.
DR InterPro; IPR033646; CLU-central.
DR InterPro; IPR025697; CLU_dom.
DR InterPro; IPR028275; CLU_N.
DR InterPro; IPR027523; CLU_prot.
DR InterPro; IPR023231; GSKIP_dom_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR12601; PTHR12601; 1.
DR Pfam; PF13236; CLU; 1.
DR Pfam; PF15044; CLU_N; 1.
DR Pfam; PF12807; eIF3_p135; 1.
DR SUPFAM; SSF103107; SSF103107; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS51823; CLU; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Phosphoprotein; Reference proteome;
KW Repeat; TPR repeat.
FT CHAIN 1..1277
FT /note="Clustered mitochondria protein 1"
FT /id="PRO_0000123557"
FT DOMAIN 339..596
FT /note="Clu"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01167"
FT REPEAT 704..738
FT /note="TPR 1"
FT REPEAT 1020..1053
FT /note="TPR 2"
FT REPEAT 1148..1181
FT /note="TPR 3"
FT REGION 19..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1212..1277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1212..1227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1231..1245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1247
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 1277 AA; 145166 MW; 1E643F4EE77ED5B5 CRC64;
MSEKKEEVKN ATVKVTVKLP KEDNHSHNTK HLKKTQSSKN NDISFEIGKE SKIQTVLDVL
AMIPSSKYLT NVGLKTIEGD SQLSDEMSIK EIVGEKSELK LQLILKPYSA REALKHVITV
RDFIGFAQET SDGLSEFAIS TGSSFSSLPL GPIKERSKQE EKDEKSDPEE KKNTFKDVTD
EEKLKFNEMV HEVFSSFKNS SINKLLTSES NIITPCVRSL SFAPYNPVPP FYRSKGHLFY
LQIVTLEGES FYITAIPSGF YVNKSNSTKF DPSPKENTDE NAHSSLIYYS LFDLIASRSK
KFISHVQAFE KKLSALDSTS YVRPSNTFLH KPWFVSSLPP NNPDYLRLQT AALDTTPERN
FNDEFQAIKD LTTSTLQDRI EMERLFSKVV HEFSVTAASG AMSIFYSDFV AMNPESPTRD
QIFLKDNIFY SYVSDVSGNY EGKGGDEAAI AASNQDLKTI NILNRLHMHE VRYLLTTVVE
FAGRRILAQT PVPGLLATMG NKIVKDANTG EEVTEDFVND INVKYGLDEG LGKIVYDADF
DSVLEKKFVK AFHLKKHKVN GTELAFSSQS KGIVGFDKRR YILDLANTYP LDINFARQNF
DNIEETGNRY PHRQTLLRPE LVEKWWNNKV EKEGVEFEKA YEENLFSYNP DAYQVEGIED
ANVDEMSNYL QKEVIPSVIQ DYLSGNLSTP YNGEHLADTL HKNGINMRYL GKIIELSQKE
LDSQIVHYEQ NLKAVEQDNK EYEDWEKSYL QKIENMIKER QAKINKLVQE GKEVPKELTE
DLKLNDEEIK KPTDGKPVVV AYDELVPLIK ISELEIVSRS LKHVLKDLSK DVPVFLVPSL
VAYVFNMLVG INYNADPKPE PVDEFYPVNK CSFAKLTRSE LLEAVSKQAF LRFRHQLPSN
WIEAYMENPF TLIRSVSYKF GIQLLNKEYF FTREQLESYK QSLDKKIRNK FVEPPTTFSL
SDLTIIPRVK FSEYTSSVSE EFWAQGASMI NEDKQSALTL LAQSITVLED VNNILHPAVA
EKYLSLSAIY NKLALYPEAI AFCRKACTIY ERVSGIDSFE MMRALTNLAI LEFSNESPYN
ATVVYNRLAE ILKVYELPKI HHPAPTSIFN HLEQLALGVQ DTKLAIEVLG QLSSYVVELE
GKDSLAYGYT ESRLGNLFAA LKDFHRALEH ITVTQGIFTK QLGMNHTHSA QSRQWVNGLS
SLIMDLKQKK QLAQDQMSTT GSNSAGHKKT NHRQKKDDVK PELANKSVDE LLTFIEGDSS
NSKSKNKTNN KKKHGKK
