TMA17_YEAST
ID TMA17_YEAST Reviewed; 150 AA.
AC Q12513; D6VRP0;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Translation machinery-associated protein 17;
DE AltName: Full=ATPase-dedicated chaperone of 17 kDa;
DE Short=ADC17;
GN Name=TMA17; OrderedLocusNames=YDL110C; ORFNames=D2320;
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=8923743;
RX DOI=10.1002/(sici)1097-0061(199610)12:13%3c1377::aid-yea35%3e3.0.co;2-r;
RA Boskovic J., Soler-Mira A., Garcia-Cantalejo J.M., Ballesta J.P.G.,
RA Jimenez A., Remacha M.A.;
RT "The sequence of a 16,691 bp segment of Saccharomyces cerevisiae chromosome
RT IV identifies the DUN1, PMT1, PMT5, SRP14 and DPR1 genes, and five new open
RT reading frames.";
RL Yeast 12:1377-1384(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 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 [5]
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBUNIT.
RX PubMed=16702403; DOI=10.1101/gad.1422006;
RA Fleischer T.C., Weaver C.M., McAfee K.J., Jennings J.L., Link A.J.;
RT "Systematic identification and functional screens of uncharacterized
RT proteins associated with eukaryotic ribosomal complexes.";
RL Genes Dev. 20:1294-1307(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-68, AND
RP IDENTIFICATION BY 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, 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).
RN [10]
RP DISRUPTION PHENOTYPE, FUNCTION, INTERACTION WITH RPT6, AND INDUCTION.
RX PubMed=25042801; DOI=10.1016/j.molcel.2014.06.017;
RA Hanssum A., Zhong Z., Rousseau A., Krzyzosiak A., Sigurdardottir A.,
RA Bertolotti A.;
RT "An inducible chaperone adapts proteasome assembly to stress.";
RL Mol. Cell 55:566-577(2014).
CC -!- FUNCTION: ATPase-dedicated chaperone that assists the formation of the
CC RPT6-RPT3 ATPase pair, an early step in proteasome assembly. Plays a
CC key role in maintaining homeostatic proteasome levels and adjusting
CC proteasome assembly when demands increase, such as during proteasome
CC stresses. Function overlaps with RPN14. {ECO:0000269|PubMed:25042801}.
CC -!- SUBUNIT: Interacts with RPT6. Interacts with the 40S and 60S ribosomal
CC subunits. {ECO:0000269|PubMed:16702403, ECO:0000269|PubMed:25042801}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: Expression is increased in absence of RPN14 and upon
CC treatment with tunicamycin, an agent which causes accumulation of
CC misfolded proteins in the endoplasmic reticulum.
CC {ECO:0000269|PubMed:25042801}.
CC -!- DISRUPTION PHENOTYPE: Decreases cell fitness. Causes severe growth
CC defects and an overload of polyubiquitinated conjugates when associated
CC with a RPT6 thermosensitive proteasome mutant.
CC {ECO:0000269|PubMed:25042801}.
CC -!- MISCELLANEOUS: Present with 2110 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X95644; CAA64902.1; -; Genomic_DNA.
DR EMBL; Z74158; CAA98677.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11750.1; -; Genomic_DNA.
DR PIR; S67652; S67652.
DR RefSeq; NP_010173.1; NM_001180169.1.
DR PDB; 6QL5; EM; 2.80 A; M/N/O/P/Q/R=3-150.
DR PDB; 6QL7; X-ray; 4.60 A; M/N/O/P/Q/R/m/n/o/p/q/r=1-150.
DR PDBsum; 6QL5; -.
DR PDBsum; 6QL7; -.
DR AlphaFoldDB; Q12513; -.
DR SMR; Q12513; -.
DR BioGRID; 31952; 100.
DR DIP; DIP-1801N; -.
DR IntAct; Q12513; 3.
DR MINT; Q12513; -.
DR STRING; 4932.YDL110C; -.
DR iPTMnet; Q12513; -.
DR MaxQB; Q12513; -.
DR PaxDb; Q12513; -.
DR PRIDE; Q12513; -.
DR EnsemblFungi; YDL110C_mRNA; YDL110C; YDL110C.
DR GeneID; 851448; -.
DR KEGG; sce:YDL110C; -.
DR SGD; S000002268; TMA17.
DR VEuPathDB; FungiDB:YDL110C; -.
DR eggNOG; ENOG502S4G9; Eukaryota.
DR HOGENOM; CLU_141797_0_0_1; -.
DR InParanoid; Q12513; -.
DR OMA; NAPNSVY; -.
DR BioCyc; YEAST:G3O-29511-MON; -.
DR BRENDA; 2.3.1.86; 984.
DR PRO; PR:Q12513; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q12513; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:SGD.
DR GO; GO:0070682; P:proteasome regulatory particle assembly; IDA:SGD.
DR InterPro; IPR038966; TMA17.
DR PANTHER; PTHR40422; PTHR40422; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..150
FT /note="Translation machinery-associated protein 17"
FT /id="PRO_0000240701"
FT REGION 110..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
SQ SEQUENCE 150 AA; 16771 MW; 376C8F333EEE2E84 CRC64;
MCSAGGIRRP IQIEEFKTAI SGMSDMELAQ IKTEIENSIN HLQRSNARLG KYIAKLEGAD
DRLEADDSDD LENIDSGDLA LYKDSVRENE IVLNNYNERV DALEQETVYR KTGHGKSKHE
VEAKDNTNKG PDVDMDNSNV DVVTPNSIFI
