ECM29_YEAST
ID ECM29_YEAST Reviewed; 1868 AA.
AC P38737; D3DKT8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Proteasome component ECM29;
DE AltName: Full=Extracellular mutant protein 29;
GN Name=ECM29; OrderedLocusNames=YHL030W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [2]
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 [3]
RP IDENTIFICATION.
RX PubMed=9335584; DOI=10.1093/genetics/147.2.435;
RA Lussier M., White A.-M., Sheraton J., di Paolo T., Treadwell J.,
RA Southard S.B., Horenstein C.I., Chen-Weiner J., Ram A.F.J., Kapteyn J.C.,
RA Roemer T.W., Vo D.H., Bondoc D.C., Hall J., Zhong W.-W., Sdicu A.-M.,
RA Davies J., Klis F.M., Robbins P.W., Bussey H.;
RT "Large scale identification of genes involved in cell surface biosynthesis
RT and architecture in Saccharomyces cerevisiae.";
RL Genetics 147:435-450(1997).
RN [4]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN
RP PROTEASOME COMPLEX.
RX PubMed=12408819; DOI=10.1016/s1097-2765(02)00638-x;
RA Leggett D.S., Hanna J., Borodovsky A., Crosas B., Schmidt M., Baker R.T.,
RA Walz T., Ploegh H., Finley D.;
RT "Multiple associated proteins regulate proteasome structure and function.";
RL Mol. Cell 10:495-507(2002).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1692, 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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Stabilizes the proteasome holoenzyme, probably by tethering
CC the 20S proteolytic core particle and the 19S regulatory particle. The
CC proteasome is a multicatalytic proteinase complex which is
CC characterized by its ability to cleave peptides with Arg, Phe, Tyr,
CC Leu, and Glu adjacent to the leaving group at neutral or slightly basic
CC pH. The proteasome has an ATP-dependent proteolytic activity.
CC {ECO:0000269|PubMed:12408819}.
CC -!- SUBUNIT: Component of the proteasome. ECM29 binds to both proteasome
CC 19S and 20S particles. {ECO:0000269|PubMed:12408819}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2950 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ECM29 family. {ECO:0000305}.
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DR EMBL; U11583; AAB65042.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06655.1; -; Genomic_DNA.
DR PIR; S48938; S48938.
DR RefSeq; NP_011833.1; NM_001179110.1.
DR AlphaFoldDB; P38737; -.
DR BioGRID; 36392; 228.
DR DIP; DIP-6563N; -.
DR IntAct; P38737; 56.
DR MINT; P38737; -.
DR STRING; 4932.YHL030W; -.
DR iPTMnet; P38737; -.
DR MaxQB; P38737; -.
DR PaxDb; P38737; -.
DR PRIDE; P38737; -.
DR EnsemblFungi; YHL030W_mRNA; YHL030W; YHL030W.
DR GeneID; 856355; -.
DR KEGG; sce:YHL030W; -.
DR SGD; S000001022; ECM29.
DR VEuPathDB; FungiDB:YHL030W; -.
DR eggNOG; KOG0915; Eukaryota.
DR GeneTree; ENSGT00940000153612; -.
DR HOGENOM; CLU_000880_1_1_1; -.
DR InParanoid; P38737; -.
DR OMA; TWRSQIA; -.
DR BioCyc; YEAST:G3O-31050-MON; -.
DR PRO; PR:P38737; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38737; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000502; C:proteasome complex; IDA:SGD.
DR GO; GO:0060090; F:molecular adaptor activity; IDA:SGD.
DR GO; GO:0043248; P:proteasome assembly; IDA:SGD.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 3.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR024372; Ecm29.
DR PANTHER; PTHR23346:SF19; PTHR23346:SF19; 1.
DR Pfam; PF13001; Ecm29; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Nucleus; Phosphoprotein; Proteasome;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..1868
FT /note="Proteasome component ECM29"
FT /id="PRO_0000212558"
FT REPEAT 32..69
FT /note="HEAT 1"
FT REPEAT 116..153
FT /note="HEAT 2"
FT REPEAT 256..292
FT /note="HEAT 3"
FT REPEAT 313..351
FT /note="HEAT 4"
FT REPEAT 384..422
FT /note="HEAT 5"
FT REPEAT 439..476
FT /note="HEAT 6"
FT REPEAT 590..627
FT /note="HEAT 7"
FT REPEAT 707..745
FT /note="HEAT 8"
FT REPEAT 748..780
FT /note="HEAT 9"
FT REPEAT 781..818
FT /note="HEAT 10"
FT REPEAT 846..885
FT /note="HEAT 11"
FT REPEAT 945..982
FT /note="HEAT 12"
FT REPEAT 988..1025
FT /note="HEAT 13"
FT REPEAT 1030..1067
FT /note="HEAT 14"
FT REPEAT 1137..1174
FT /note="HEAT 15"
FT REPEAT 1178..1215
FT /note="HEAT 16"
FT REPEAT 1272..1311
FT /note="HEAT 17"
FT REPEAT 1361..1398
FT /note="HEAT 18"
FT REPEAT 1422..1459
FT /note="HEAT 19"
FT REPEAT 1503..1540
FT /note="HEAT 20"
FT REPEAT 1544..1581
FT /note="HEAT 21"
FT REPEAT 1649..1687
FT /note="HEAT 22"
FT REPEAT 1746..1785
FT /note="HEAT 23"
FT REPEAT 1830..1867
FT /note="HEAT 24"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 1692
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 1868 AA; 210431 MW; ACB44C8A2FAD5C61 CRC64;
MSISSDEAKE KQLVEKAELR LAIADSPQKF ETNLQTFLPP LLLKLASPHA SVRTAVFSAL
KNLISRINTL PQVQLPVRAL IVQAKEPNLA AQQDSTNVRL YSLLLASKGI DRLSLQDRQQ
LLPLVVSNIS CLTGTVAARM FHILLKLILE WVAPQESSHE QEEFVQFLQL DNDGFSFLMR
QFTRFFLLVP SKQVQVSQQP LSRGYTCPGL SLTDVAFFTY DAGVTFNKEQ LNKFKKAIFQ
FVCRGMAATQ TIEQSPRMIE LMEFLCVVST DSTNLSDDAA QFMKRFPMPY ENEEFITFLQ
TLYIGNTANG RPPVKAILQE KILSILNRSH FATTKAECIS LICSIGLHSS EYKLRSLTLS
FIRHVAKLNY KNLNPASSSP SSTDFSTCIV SLIRNNLHAE GWPKLQLGPQ TPAFNTAILQ
RQLQYETLGD ILKRDFELVS DLSYIEFLFE SLKNDLPQFR SSIQESLLSL VGHLSILPQQ
SKLKLKNLLR KNLSIDEQQR EDNNDAVNSI MALKFVSIKF TNAAFPFHDP EARLFNIWGT
VRTNRFDIIE ESFKGLQPFW FRVNNASINT SATVKTSDLL GSHLSETEFP PFREFLQVLI
DQLDSEAASI TRKSLNNAVR FSKQCLISNA IYGKKTMVIQ DEDWSVRIDK ALELDDTVVS
RVNEMVQGMN DDIFIRYLTL LSNEFTATNS KGEQIAIFPY QDPIFGSVLL TLLNFVSNNV
LRRLEILVPD LYHLVIMKFQ SLSDNDLAVC ATIIGIISTA IADSTHVKRI TKIAQSQTMA
ETYVASYVVP RLYLKDQTNH IESDSILNLL NILTTHLSHP GTNKDMILKL VCQVTKFGLL
LQVSAQERKD FLKKVMDTIQ DKLINDVTAI QTWSYLSLYS TDLENSSLFQ EKLLETNVSK
QNDFLFSVGE SLSVVAGKWS SKYLIKQIDI PNFNVEIMQQ KFPATNVTTI LDEIFSGCDS
TKPSLRKASC IWLLSYIQYL GHLPEVSSKC NDIHLRFMRF LADRDEFIQD SAARGLSLVY
EIGGSDLKES MVKGLLKSFT ESTAGSASTS ATGISGSVSE ETELFEPGVL NTGDGSISTY
KDILNLASEV GDPALVYKFM SLAKSSALWS SRKGIAFGLG AIMSKSSLEE LLLKDQQTAK
KLIPKLYRYR FDPFQAVSRS MTDIWNTLIP ESSLTISLYF NDILDELLCG MANKEWRVRE
ASTSALLQLI QSQPQEKFSE KMLKIWTMAF RTMDDIKDSV REVGTKFTTV LAKILARSID
VEKGVNPTKS KEILDNILPF LWGPHGLNSD AEEVRNFALT TLIDLVKHSP GAIKPFTPKL
IYDFITLFSS IEPQVINYLA LNAANYNIDA NVIDTQRKNG VTNSPLFQTI EKLINNSDDC
MMEEIINVVI KASRKSVGLP SKVASSLVII ILVKRYSIEM KPYSGKLLKV CLTMFEDRNE
SVNIAFAISM GYLFKVSALD KCIKYSEKLI TKYFEPTSTE NNKKVVGTAI DSILNYAKSE
FDNVASVFMP LIFIACNDED KDLETLYNKI WTEASSSGAG TVKLYLPEIL NVLCVNIKSN
DFSIRKTCAK SVIQLCGGIN DSIPYPQIVK LFDISREALS GRSWDGKEHI VAALVSLTEK
FSQTVADNND LQESINHVMY TEVSRKSMKY VKKILPLYAR YINVNPQEET ITFLIEKAKE
MIRLLGSESD DSEGSIKQTS DESTIKRIKP NTEITQKSSK ENIENEEYVI NLLKVSVDIC
NNSKSRYPMN LLEFIIDEIA YLFHNDRIIH TWRTQLAASE IGISIVGRFS TISSADFIQN
VGRLWDQTFP INCNKETIEN VKLQMIKFGG LIIQKIPSLQ NNIEENLRLL NSIDSTSRIE
LELKNIGL
