ECM29_PONAB
ID ECM29_PONAB Reviewed; 1810 AA.
AC Q5R6J0; Q5RBF0;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 2.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Proteasome adapter and scaffold protein ECM29;
DE AltName: Full=Proteasome-associated protein ECM29 homolog;
DE Flags: Fragment;
GN Name=ECPAS; Synonyms=ECM29, KIAA0368;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex, and Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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. Promotes proteasome dissociation under oxidative stress.
CC {ECO:0000250|UniProtKB:Q5VYK3, ECO:0000250|UniProtKB:Q6PDI5}.
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 -!- SIMILARITY: Belongs to the ECM29 family. {ECO:0000305}.
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DR EMBL; CR858699; CAH90910.1; -; mRNA.
DR EMBL; CR860499; CAH92620.1; -; mRNA.
DR AlphaFoldDB; Q5R6J0; -.
DR STRING; 9601.ENSPPYP00000021840; -.
DR eggNOG; KOG0915; Eukaryota.
DR InParanoid; Q5R6J0; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0030139; C:endocytic vesicle; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005771; C:multivesicular body; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR GO; GO:0060090; F:molecular adaptor activity; IEA:InterPro.
DR GO; GO:0043248; P:proteasome assembly; IEA:InterPro.
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 2: Evidence at transcript level;
KW Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Endoplasmic reticulum;
KW Endosome; Isopeptide bond; Nucleus; Phosphoprotein; Proteasome;
KW Reference proteome; Repeat; Ubl conjugation.
FT CHAIN <1..1810
FT /note="Proteasome adapter and scaffold protein ECM29"
FT /id="PRO_0000212561"
FT REPEAT 1..36
FT /note="HEAT 1"
FT REPEAT 78..115
FT /note="HEAT 2"
FT REPEAT 133..176
FT /note="HEAT 3"
FT REPEAT 297..333
FT /note="HEAT 4"
FT REPEAT 358..397
FT /note="HEAT 5"
FT REPEAT 400..437
FT /note="HEAT 6"
FT REPEAT 440..478
FT /note="HEAT 7"
FT REPEAT 654..691
FT /note="HEAT 8"
FT REPEAT 692..730
FT /note="HEAT 9"
FT REPEAT 754..791
FT /note="HEAT 10"
FT REPEAT 800..839
FT /note="HEAT 11"
FT REPEAT 841..878
FT /note="HEAT 12"
FT REPEAT 902..940
FT /note="HEAT 13"
FT REPEAT 946..983
FT /note="HEAT 14"
FT REPEAT 984..1021
FT /note="HEAT 15"
FT REPEAT 1083..1120
FT /note="HEAT 16"
FT REPEAT 1123..1160
FT /note="HEAT 17"
FT REPEAT 1165..1202
FT /note="HEAT 18"
FT REPEAT 1214..1252
FT /note="HEAT 19"
FT REPEAT 1256..1294
FT /note="HEAT 20"
FT REPEAT 1319..1357
FT /note="HEAT 21"
FT REPEAT 1361..1398
FT /note="HEAT 22"
FT REPEAT 1488..1525
FT /note="HEAT 23"
FT REPEAT 1529..1566
FT /note="HEAT 24"
FT REPEAT 1576..1613
FT /note="HEAT 25"
FT REPEAT 1617..1654
FT /note="HEAT 26"
FT REPEAT 1750..1793
FT /note="HEAT 27"
FT REGION 158..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 795
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VYK3"
FT MOD_RES 801
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5VYK3"
FT CROSSLNK 1004
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:Q5VYK3"
FT CONFLICT 878
FT /note="P -> S (in Ref. 1; CAH90910)"
FT /evidence="ECO:0000305"
FT CONFLICT 1221
FT /note="S -> P (in Ref. 1; CAH90910)"
FT /evidence="ECO:0000305"
FT CONFLICT 1457
FT /note="A -> I (in Ref. 1; CAH90910)"
FT /evidence="ECO:0000305"
FT NON_TER 1
SQ SEQUENCE 1810 AA; 200260 MW; CA1B833AE74E5E6F CRC64;
ISKFLPPVLL KLSSTQEGVR KKVMELLVHL NKRIKSPPKI QLPVETLLVQ YQDPAAVSFV
TNFTIIYVKM GYPRLPVEKQ CELAPTLLTA MEGKPRPQQD SLMHLLIPTL FHMKYPVESS
KSASPFNLAE KPKTVQLLLD FMLDVLLMPY GYVLNESQSR QNSSSAQGSS SNSGGGSGIP
QPPPGMSFYA AKRVIGDNPW TPEQLEQCKL GIVKFIEAEQ VPELEAVLHL VIASSDTRHS
VATAADLELK SKQSLIDWNN PAIINKMYKV YLGDIPLKTK EGAVLKPELK RDPVSTRVKL
KIVPHLLRSR QAAETFPANI QVVYDGLFGT NTNSKLRTLS LQFVHHICIT CPEIKIKPLG
PMLLNGLTKL INEYKEDPKL LSMAYSAVGK LSSRMPHLFT KDIALVQQLF EALCKEEPET
RLAIQEALSM MVGAYSTLEG AQRTLMEALV ASYLIKPEVQ VRQVAVKFAS TVFPSDHIPS
RYLLLLAAGD PREEVHGEAQ RVLRCLPGRN RKESTSEQMP SFPEMVYYIQ EKASHRMKTP
VKYMTGTTVL PFNPAAFGEI VLYLRMCLAH SAGVVPTSQS LADMQDHAPA IGRYIRTLMS
SGQTAPSSSN KSGETNPVQI YIGLLQQLLA GVGGLPVMYC LLEAVSVYPE KLATKFVDKT
EWIKSLMNSS KEEMRELAAL FYSVVVSTVS GNELKSMIEQ LIKTTKDNHS PEIQHGSLLA
LGFTVGRYLA KKKMRMSEQQ DLERNADTLP DQEELIQSAT ETIGSFLDST SPLLAIAACT
ALGEIGRNGP LPIPSEGSGF TKLHLVESLL SRIPSSKETN KMKERAIQTL GYFPVGDGDF
PHQKLLLQGL MDSVEAKQIE LQFTIGEAIT SAAIGTSPVA ARDAWQVTEE EYTPPAGAKV
NDVVPWVLDV ILNKHIISPN PHVRQAACIW LLSLVRKLST HKEVKSHLKE IQSAFVSVLS
ENDELSQDVA SKGLGLVYEL GNEQDQQELV STLVETLMTG KRVKHEVSGE TVVFQGGALG
KTPDGQGLST YKELCSLASD LSQPDLVYKF MNLANHHAMW NSRKGAAFGF NVIATRAGEQ
LAPFLPQLVP RLYRYQFDPN LGIRQAMTSI WNALVTDKSM VDKYLKEILQ DLVKNLTSNT
WRVRESSCLA LNDLLRGRPL DDIIDKLPEI WETLFRVQDD IKESVRKAAE LALKTLSKVC
VKMCDPAKGA AGQRTIAALL SCLLDKGMMS PVTEVRALSI NTLVKISKSA GAMLKPHAPK
LIPALLESLS VLEPQVLNYL SLRATEQEKA AMDSARLSAA KSSPMMETIN MCLQYLDVSV
LGELVPRLCE LIRSGVGLGT KGGCASVIVS LTTQCPQDLT PYSGKLMSAL LSGLTDRNSV
IQKSCAFAMG HLVRTSRDSS TEKLLQKLNG WYMEKEEPIY KTSCALTIHA IGRYSPDVLK
NHAKEVLPLA FLGMHEAADE EKSEKEECNL WTEVWQENVP GSFGGIRLYL QELITITQKA
LQSQSWKMKA QGAIAMASIA KQTSSLVPPY LGMILTALLQ GLAGRTWAGK EELLKAIACV
VTAYSAELEK SVPNQPSTNE ILQAVLKECS KENLKYKIVA ISCAADVLKA TKEDRFQEFS
DIVIPLIKKN SLESSGVRTT KNEEENEKEK ELQLEYLLGA FESLGKAWPR NAETQRCYRQ
ELCKLMCERL KLSTWKVQLG VLQSMNAFFQ GLMLLEEEHA DPEALAEILL ETCKSITYSL
ENKTYSSVRT EALSVIELLL KKLEESKQWE CLTSECRVLL IESLATMEPD SRPGLQEKAA
LLKKTLENLE
