ECM29_MOUSE
ID ECM29_MOUSE Reviewed; 1840 AA.
AC Q6PDI5; A2ALW0; Q6ZQC9; Q8BSW7; Q8CAH0; Q8R3M6;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Proteasome adapter and scaffold protein ECM29 {ECO:0000250|UniProtKB:Q5VYK3};
DE AltName: Full=Proteasome-associated protein ECM29 homolog;
GN Name=Ecpas; Synonyms=Ecm29, Kiaa0368;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-885 (ISOFORM 2), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1449-1840 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Hypothalamus, and Pituitary;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 612-1840.
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=15496406; DOI=10.1074/jbc.m410444200;
RA Gorbea C., Goellner G.M., Teter K., Holmes R.K., Rechsteiner M.;
RT "Characterization of mammalian Ecm29, a 26 S proteasome-associated protein
RT that localizes to the nucleus and membrane vesicles.";
RL J. Biol. Chem. 279:54849-54861(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=26802743; DOI=10.1093/jb/mvw006;
RA Haratake K., Sato A., Tsuruta F., Chiba T.;
RT "KIAA0368-deficiency affects disassembly of 26S proteasome under oxidative
RT stress condition.";
RL J. Biochem. 159:609-618(2016).
CC -!- FUNCTION: Adapter/scaffolding protein that binds to the 26S proteasome,
CC motor proteins and other compartment specific proteins. May couple the
CC proteasome to different compartments including endosome, endoplasmic
CC reticulum and centrosome. May play a role in ERAD and other enhanced
CC proteolysis (By similarity). Promotes proteasome dissociation under
CC oxidative stress (PubMed:26802743). {ECO:0000250|UniProtKB:Q5VYK3,
CC ECO:0000269|PubMed:26802743}.
CC -!- SUBUNIT: Non-stoichiometric component of the proteasome; associates
CC with the 26S proteasome. Interacts (via N-terminus) with VPS11, VPS26A,
CC VPS36, RAB11FIP4 and RABEP1. Interacts (via C-terminus) with DCTN1,
CC DCTN2, KIF5B, MYH7, MYH10, MYO10 and ARF6.
CC {ECO:0000250|UniProtKB:Q5VYK3}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q5VYK3}. Endoplasmic reticulum-Golgi
CC intermediate compartment {ECO:0000250|UniProtKB:Q5VYK3}. Endosome
CC {ECO:0000250|UniProtKB:Q5VYK3}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q5VYK3}. Nucleus
CC {ECO:0000250|UniProtKB:Q5VYK3}. Endosome, multivesicular body
CC {ECO:0000250|UniProtKB:Q5VYK3}. Cytoplasmic vesicle
CC {ECO:0000250|UniProtKB:Q5VYK3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6PDI5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PDI5-2; Sequence=VSP_013178;
CC -!- TISSUE SPECIFICITY: Widely expressed (at protein level).
CC {ECO:0000269|PubMed:15496406, ECO:0000269|PubMed:26802743}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice are viable, fertile, and do not
CC show any histological abnormalities. Under stressed condition, 26S
CC proteasome dissociates in wild-type cells, but not in cells from
CC deficient mice. {ECO:0000269|PubMed:26802743}.
CC -!- SIMILARITY: Belongs to the ECM29 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC30129.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AL805972; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL806535; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL929394; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC025035; AAH25035.1; -; mRNA.
DR EMBL; BC058684; AAH58684.1; -; mRNA.
DR EMBL; AK030369; BAC26926.1; -; mRNA.
DR EMBL; AK038775; BAC30129.1; ALT_SEQ; mRNA.
DR EMBL; AK129127; BAC97937.1; -; mRNA.
DR CCDS; CCDS18214.1; -. [Q6PDI5-1]
DR RefSeq; NP_759013.2; NM_172381.2. [Q6PDI5-1]
DR RefSeq; XP_006537911.1; XM_006537848.3. [Q6PDI5-2]
DR RefSeq; XP_006537912.1; XM_006537849.3.
DR AlphaFoldDB; Q6PDI5; -.
DR BioGRID; 230950; 44.
DR IntAct; Q6PDI5; 6.
DR STRING; 10090.ENSMUSP00000099953; -.
DR GlyConnect; 2618; 2 N-Linked glycans (1 site).
DR GlyGen; Q6PDI5; 1 site, 2 N-linked glycans (1 site).
DR iPTMnet; Q6PDI5; -.
DR PhosphoSitePlus; Q6PDI5; -.
DR SwissPalm; Q6PDI5; -.
DR CPTAC; non-CPTAC-3973; -.
DR EPD; Q6PDI5; -.
DR jPOST; Q6PDI5; -.
DR MaxQB; Q6PDI5; -.
DR PaxDb; Q6PDI5; -.
DR PeptideAtlas; Q6PDI5; -.
DR PRIDE; Q6PDI5; -.
DR ProteomicsDB; 277437; -. [Q6PDI5-1]
DR ProteomicsDB; 277438; -. [Q6PDI5-2]
DR Antibodypedia; 29523; 45 antibodies from 15 providers.
DR DNASU; 230249; -.
DR Ensembl; ENSMUST00000102889; ENSMUSP00000099953; ENSMUSG00000050812. [Q6PDI5-1]
DR GeneID; 230249; -.
DR KEGG; mmu:230249; -.
DR UCSC; uc008sze.1; mouse. [Q6PDI5-1]
DR UCSC; uc008szf.1; mouse. [Q6PDI5-2]
DR CTD; 23392; -.
DR MGI; MGI:2140220; Ecpas.
DR VEuPathDB; HostDB:ENSMUSG00000050812; -.
DR eggNOG; KOG0915; Eukaryota.
DR GeneTree; ENSGT00940000153612; -.
DR HOGENOM; CLU_000880_2_0_1; -.
DR InParanoid; Q6PDI5; -.
DR OMA; FFAMHEE; -.
DR OrthoDB; 392862at2759; -.
DR PhylomeDB; Q6PDI5; -.
DR TreeFam; TF314213; -.
DR BioGRID-ORCS; 230249; 3 hits in 72 CRISPR screens.
DR PRO; PR:Q6PDI5; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q6PDI5; protein.
DR Bgee; ENSMUSG00000050812; Expressed in hindlimb stylopod muscle and 255 other tissues.
DR ExpressionAtlas; Q6PDI5; baseline and differential.
DR Genevisible; Q6PDI5; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0030139; C:endocytic vesicle; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR GO; GO:0005770; C:late endosome; ISO:MGI.
DR GO; GO:0005771; C:multivesicular body; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0070628; F:proteasome binding; ISO:MGI.
DR GO; GO:0043248; P:proteasome assembly; IEA:InterPro.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISO:MGI.
DR Gene3D; 1.25.10.10; -; 4.
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; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW Endoplasmic reticulum; Endosome; Isopeptide bond; Nucleus; Phosphoprotein;
KW Proteasome; Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..1840
FT /note="Proteasome adapter and scaffold protein ECM29"
FT /id="PRO_0000212560"
FT REPEAT 28..65
FT /note="HEAT 1"
FT REPEAT 107..144
FT /note="HEAT 2"
FT REPEAT 162..199
FT /note="HEAT 3"
FT REPEAT 327..363
FT /note="HEAT 4"
FT REPEAT 388..427
FT /note="HEAT 5"
FT REPEAT 430..467
FT /note="HEAT 6"
FT REPEAT 470..508
FT /note="HEAT 7"
FT REPEAT 722..760
FT /note="HEAT 8"
FT REPEAT 773..810
FT /note="HEAT 9"
FT REPEAT 830..869
FT /note="HEAT 10"
FT REPEAT 871..908
FT /note="HEAT 11"
FT REPEAT 932..970
FT /note="HEAT 12"
FT REPEAT 976..1013
FT /note="HEAT 13"
FT REPEAT 1014..1051
FT /note="HEAT 14"
FT REPEAT 1113..1150
FT /note="HEAT 15"
FT REPEAT 1153..1190
FT /note="HEAT 16"
FT REPEAT 1195..1232
FT /note="HEAT 17"
FT REPEAT 1244..1282
FT /note="HEAT 18"
FT REPEAT 1286..1324
FT /note="HEAT 19"
FT REPEAT 1349..1387
FT /note="HEAT 20"
FT REPEAT 1391..1428
FT /note="HEAT 21"
FT REPEAT 1518..1555
FT /note="HEAT 22"
FT REPEAT 1559..1596
FT /note="HEAT 23"
FT REPEAT 1659..1696
FT /note="HEAT 24"
FT REPEAT 1780..1823
FT /note="HEAT 25"
FT REGION 187..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 825
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VYK3"
FT MOD_RES 831
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5VYK3"
FT CROSSLNK 1034
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:Q5VYK3"
FT VAR_SEQ 1..7
FT /note="METGSDS -> MYHIDCR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013178"
FT CONFLICT 1446
FT /note="D -> E (in Ref. 2; AAH25035 and 4; BAC97937)"
FT /evidence="ECO:0000305"
FT CONFLICT 1449
FT /note="V -> F (in Ref. 4; BAC26926)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1840 AA; 203703 MW; 7FCB7FFDBFD1539D CRC64;
METGSDSDQL ERVFLRLGHA ETDEQLQNII SKFLPPVLLK LSSTQEGVRK KVMELLVHLN
KRIKSRPKIQ LPVETLLVQY QDPAAVSFVT NFTIIYVKMG YPRLPVEKQC ELAPTLLTAM
EGKPQPQQDS LMHLLIPTLF HMKYPAESSK SASPFNLAEK PKTVQLLLDF MLDVLLMPYG
YVLNESQSRQ NSSSSSQGSS SNSGGGSGIP QPPPGMSFYA AKRVIGDNPW TPEQLEQCKL
GIVKFIEAEQ VPELEAVLHL VIASSDTRHS VATAADLELK SKQSLIDWNN PAIINKMYKV
YLGDIPLKTK EGAVLKPELK RDPVSTRVKL KIVPHLLRSR QAAETFPANI QVVYDGLFGT
NTNSKLRTLS LQFVHHICLT CPEIKIKPLG PMLLNGLTKL INEYKEDPKL LSMAYSAVGK
LSSRMPHLFT KDIALVQQLF EALCKEEPET RLAIQEALSM MVGAYSTLEG AQRTLMEALV
ASYLIKPEVQ VRQVAVKFAS TVFPSDHIPS RYLLLLAAGD PREEVHGEAQ RVLRCLPGRN
KKESASKQMP SFPEMVYYIQ EKASHRMKTP VKYMTGTTVL PFNPAAFGEI VLYLRMCLAH
SAGVVPTSQS LADMQDHAPA IGRYIRALMS SSQATASSSN KSGETNPVQI YTGLLQQLLA
GVGGLPVMYC LLEAVSVYPE KLATKFVDKT EWIKSLMSSS KEEMRELAAL FYSVVVSTVS
GIELKSMIEQ LIKATKDNHS PEVQHGSLLA LGFTVGRYLA KKRVRMAEQH DLETDADLLP
EQEEIIRSAT ETIGSFLDST SPLLAIAACT ALGEIGRNGP LPIPSEGSGF TKLHLVESLL
NRIPSSKETN KMKERAIQTL GYFPVGDGVF PHQKLLLQGL MDSVEAKQIE LQFTIGEAIT
SAAIGTNSVA ARDAWLVTEE EYIPPAGAKV NDVVPWVLDV ILNKHIISPN PHVRQAACIW
LLSLVRKLST HREVKSHLKE IQSAFVSVLS ENDELSQDVA SKGLGLVYEL GNEQDQQELV
STLVETLMTG KRVKHEVSGE TVVFQGGGLG KTPDGQGLST YKELCSLASD LSQPDLVYKF
MNLANHHAMW NSRKGAAFGF NVIATRAGEQ LAPFLPQLVP RLYRYQFDPN LGIRQAMTSI
WNALVTDKSM VDKYLKEILQ DLIKNLTSNM WRVRESSCLA LNDLLRGRPL DDVIDKLPEM
WETLFRVQDD IKESVRKAAE LALKTLSKVC VKMCDPAKGA AGQRTIAVLL PCLLDKGMMS
PVTEVRALSI NTLVKISKSA GAMLKPHAPK LIPALLESLS VLEPQVLNYL SLRATEQEKD
VMDSARLSAA KSSPMMETIN MCLQYLDVSV LGELVPRLCE LIRSGVGLGT KGGCASVIVS
LTTQCPQDLT PYSGKLMSAL LSGLTDRNSV IQKSCAFAMG HLVRTSRDSS TEKLLQKLNG
WYMEKDEPVY KTSCALTIHA IGRYSPDVLK NHAKEVLPLA FLGMHEIADE EKSEKEECNM
WTEVWQENVP GSFGGIRLYL QELITITQKA LQSQSWKMKA QGAIAMASIS KQTSSLVPPY
LGMILSALMQ GLAGRTWAGK EELLKAIACV VTACSTELEK SVPNQPTTNE ILQAVLKECC
KENLKYKIVA ISCAADVLKA TKEDRFQEFS DIVIPLIKKN SLESMGVRTT KAEDENEKER
ELQLESLLGA FESLGKAWPR NPDTQRCYRQ ELCKLMCERL RLSTWKVQLG VLQSMNAFFQ
GLMLLEEEHA DPEALAEILL ETCKSITYSL ENKTYSSVRT EALSVVELLL KKLEEAKQWE
SLTAECRGLL IESLATMETD NRPELQEKAS VLKKTLESLE
