ID   ECM29_SCHPO             Reviewed;        1679 AA.
AC   Q9P7H8; Q9P7Y5;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 128.
DE   RecName: Full=Proteasome component ecm29;
GN   Name=ecm29; ORFNames=SPAC1782.01, SPAPYUG7.07;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE 26S
RP   PROTEASOME.
RX   PubMed=20838651; DOI=10.1371/journal.pbio.1000471;
RA   Kouranti I., McLean J.R., Feoktistova A., Liang P., Johnson A.E.,
RA   Roberts-Galbraith R.H., Gould K.L.;
RT   "A global census of fission yeast deubiquitinating enzyme localization and
RT   interaction networks reveals distinct compartmentalization profiles and
RT   overlapping functions in endocytosis and polarity.";
RL   PLoS Biol. 8:708-716(2010).
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the proteasome. {ECO:0000269|PubMed:20838651}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the ECM29 family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB66316.2; -; Genomic_DNA.
DR   PIR; T50091; T50091.
DR   PIR; T50307; T50307.
DR   RefSeq; XP_001713110.1; XM_001713058.2.
DR   AlphaFoldDB; Q9P7H8; -.
DR   BioGRID; 280531; 22.
DR   STRING; 4896.SPAC1782.01.1; -.
DR   MaxQB; Q9P7H8; -.
DR   PaxDb; Q9P7H8; -.
DR   EnsemblFungi; SPAC1782.01.1; SPAC1782.01.1:pep; SPAC1782.01.
DR   PomBase; SPAC1782.01; ecm29.
DR   VEuPathDB; FungiDB:SPAC1782.01; -.
DR   eggNOG; KOG0915; Eukaryota.
DR   HOGENOM; CLU_000880_2_1_1; -.
DR   InParanoid; Q9P7H8; -.
DR   OMA; KFMQLAR; -.
DR   PhylomeDB; Q9P7H8; -.
DR   PRO; PR:Q9P7H8; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR   GO; GO:0032991; C:protein-containing complex; NAS:PomBase.
DR   GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR   GO; GO:0043248; P:proteasome assembly; ISO:PomBase.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR   Gene3D; 1.25.10.10; -; 2.
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; 2.
DR   SUPFAM; SSF48371; SSF48371; 3.
PE   1: Evidence at protein level;
KW   Cytoplasm; Nucleus; Proteasome; Reference proteome; Repeat.
FT   CHAIN           1..1679
FT                   /note="Proteasome component ecm29"
FT                   /id="PRO_0000116846"
FT   REPEAT          27..64
FT                   /note="HEAT 1"
FT   REPEAT          66..103
FT                   /note="HEAT 2"
FT   REPEAT          105..142
FT                   /note="HEAT 3"
FT   REPEAT          314..354
FT                   /note="HEAT 4"
FT   REPEAT          355..392
FT                   /note="HEAT 5"
FT   REPEAT          394..431
FT                   /note="HEAT 6"
FT   REPEAT          513..551
FT                   /note="HEAT 7"
FT   REPEAT          697..734
FT                   /note="HEAT 8"
FT   REPEAT          742..780
FT                   /note="HEAT 9"
FT   REPEAT          840..878
FT                   /note="HEAT 10"
FT   REPEAT          884..921
FT                   /note="HEAT 11"
FT   REPEAT          1023..1060
FT                   /note="HEAT 12"
FT   REPEAT          1089..1127
FT                   /note="HEAT 13"
FT   REPEAT          1160..1198
FT                   /note="HEAT 14"
FT   REPEAT          1202..1239
FT                   /note="HEAT 15"
FT   REPEAT          1267..1305
FT                   /note="HEAT 16"
FT   REPEAT          1309..1346
FT                   /note="HEAT 17"
FT   REPEAT          1467..1504
FT                   /note="HEAT 18"
FT   REPEAT          1509..1546
FT                   /note="HEAT 19"
FT   REPEAT          1600..1639
FT                   /note="HEAT 20"
SQ   SEQUENCE   1679 AA;  190968 MW;  231F431CA8D028E7 CRC64;
     MAENELRLLN NAELKLALAE SEDSFQSLVS VFLCPILLKL DSPHESVRNK TISIANHIMT
     RLNNNAQAIL PLEALVSQYV EANQPLRKRF LLAFISIGEK RIPCSENLAL LQICLNHVNE
     YPLVLLTLTI RLLRFSKPTS AITCSNDVIL SLSSFYLIQK DQRIFSDLQF SQKTVDYRLS
     LLRWIHLSSW PSNWKWLAYF FASADSHSEV ARLADEFTRD SGLPDLENLS HVNVLLDIAL
     DKFRIEALHA NFSVSISLRN KAIQHLLKSK IAANTDKAIN CIEFILEAPP SMQPRLIQFT
     RWVVDKADPN FLKPKAAMIL EKILSILSSN IIQSDLLRGF LYTTIGLLTK VDNHLITNSL
     LTNLLTSLQS ELPDVRVSID EALSIIIPYY SNFRFSNELL PVLEPFIFDS PESPAAYCAL
     RFVLVAFPFD YLPARFICLK VQNPFVFHHS FIEEAKKGLN LSQWVQYNSV YSTNEAQEED
     KVRAASYPSA SEVISFILSD HDLKKFWESN AAEYCLAILE FIERCIYYSA DRSLELYDND
     KLSSIDALLI QDSKLREMVS EKCISLSNFN VFLEYVFYGT LLMHFEPTYA LSRLVSFAPP
     EVTFSLPELD FLTSVFNFPL ALRNTATRIL GIILSTKDST RISEVLSSCF TIISTSNNKN
     DNFFKAETAL LIIGYTISYL AAQTNSAAVD SFILNSGSIK EFFSVLLEYL GSNVLHKKTT
     SLAIYKELFV YFTRDWITSY GVDFDEILNV LLRFLKEVED TNVKVECLHV ISRMSLSFSD
     DEMAEKILKA IYVTYHMDSP DILFASAEAM SILAGGHRNV FVKSTCPIFF QKQLDNYKAD
     HYCFTLDFIL TDCVNSPKPL LRRASSLWLF YIVRYCEPQT YTMTRLNDIY HSFLSFLVTQ
     DDFVQDTASR GLKAMYDVLE GDERKSFTDN LISTIAADRV DEKTKAPLDA DTALFTTNKG
     TVATYKDICS LASESGNPDL IYSFLSIAGN SSLWQARKGL ASGISYLGIP EDQKRKTFSF
     DTSKSSSLLK KLYRFKHDPN PDVAKTMGEI WDTLVPSDLN LASHRKYLVE DCLEFMGSRS
     WRDRESSVNT LVSLLSNVPV TEYLNQLEDI WNMSFRTLDD IKESVREASF PLCKLLARSV
     IQSLEKTSHN TSPSGICKGK RIVSVALPFL LKHAYDQAKE VRSLTYSTIT ELVRTGNSTL
     TSFVPAIMQV MLEYLTEYES KAATFLDFHA KNYSIKQENI DNARTSAVQS SSMMDTLEKC
     IGLLDESSMQ TLYPILNRMI AKPGGVPTKI GSAQVVMLLV IRRGPLVKQF ASKLLQSLKS
     SCFDRNAAVS DAFASAIGYL LRVCPLEIAS QTCQEIIDKF YDGNTNEQII SSKLTVYASR
     YAPDVFLNLG SLFFPFIFFG KHSSSISING VLSKAWDELS SAGSSVNLYS EEIILLIQKN
     LIVTKWDVKR PAAAALLEFV NTSRLTYRQN DIYVLLNETM KDKSWPGKEL LLEAYVKFLI
     KYPEFIKSQK MEEVHQVIVR EFKRRNIVYK SHAMESVGEL LSDENYRELD LYELSLNECG
     TFLQKEWFDK DDELNLEEKI ALQRNSVYAM FNSSRPGNKN CNEMLLTYLS NALDENYLHW
     NVKLAILKNA PHLKKIMSNE EFLLYKDILY RCYEDNPSPK AKDYAEVIFG ENYLSVLRN