PSMD1_DICDI
ID PSMD1_DICDI Reviewed; 975 AA.
AC Q54JM5;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 1;
GN Name=psmD1; ORFNames=DDB_G0287953;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16512674; DOI=10.1021/pr050350q;
RA Reinders Y., Schulz I., Graef R., Sickmann A.;
RT "Identification of novel centrosomal proteins in Dictyostelium discoideum
RT by comparative proteomic approaches.";
RL J. Proteome Res. 5:589-598(2006).
CC -!- FUNCTION: Acts as a regulatory subunit of the 26 proteasome which is
CC involved in the ATP-dependent degradation of ubiquitinated proteins.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the proteasome subunit S1 family. {ECO:0000305}.
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DR EMBL; AAFI02000105; EAL63468.1; -; Genomic_DNA.
DR RefSeq; XP_636972.1; XM_631880.1.
DR AlphaFoldDB; Q54JM5; -.
DR SMR; Q54JM5; -.
DR BioGRID; 1251384; 1.
DR IntAct; Q54JM5; 1.
DR STRING; 44689.DDB0232977; -.
DR PaxDb; Q54JM5; -.
DR EnsemblProtists; EAL63468; EAL63468; DDB_G0287953.
DR GeneID; 8626381; -.
DR KEGG; ddi:DDB_G0287953; -.
DR dictyBase; DDB_G0287953; psmD1.
DR eggNOG; KOG2062; Eukaryota.
DR HOGENOM; CLU_002323_0_0_1; -.
DR InParanoid; Q54JM5; -.
DR OMA; MIMVQQN; -.
DR PhylomeDB; Q54JM5; -.
DR Reactome; R-DDI-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-DDI-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-DDI-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR Reactome; R-DDI-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-DDI-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-DDI-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-DDI-2467813; Separation of Sister Chromatids.
DR Reactome; R-DDI-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-DDI-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-DDI-4641258; Degradation of DVL.
DR Reactome; R-DDI-5632684; Hedgehog 'on' state.
DR Reactome; R-DDI-5658442; Regulation of RAS by GAPs.
DR Reactome; R-DDI-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-DDI-5689603; UCH proteinases.
DR Reactome; R-DDI-5689880; Ub-specific processing proteases.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR Reactome; R-DDI-68949; Orc1 removal from chromatin.
DR Reactome; R-DDI-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-DDI-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-DDI-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-DDI-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-DDI-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-DDI-8951664; Neddylation.
DR Reactome; R-DDI-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-DDI-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-DDI-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:Q54JM5; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005776; C:autophagosome; IDA:dictyBase.
DR GO; GO:0005764; C:lysosome; IDA:dictyBase.
DR GO; GO:0005634; C:nucleus; ISS:dictyBase.
DR GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IBA:GO_Central.
DR GO; GO:0034515; C:proteasome storage granule; IBA:GO_Central.
DR GO; GO:0004175; F:endopeptidase activity; ISS:dictyBase.
DR GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0042176; P:regulation of protein catabolic process; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:dictyBase.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR016642; 26S_Psome_Rpn2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002015; Proteasome/cyclosome_rpt.
DR InterPro; IPR035266; PSMD1.
DR InterPro; IPR040623; RPN2_C.
DR PANTHER; PTHR10943:SF2; PTHR10943:SF2; 1.
DR Pfam; PF01851; PC_rep; 2.
DR Pfam; PF18004; RPN2_C; 1.
DR PIRSF; PIRSF015947; 26S_Psome_Rpn2; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Proteasome; Reference proteome; Repeat.
FT CHAIN 1..975
FT /note="26S proteasome non-ATPase regulatory subunit 1"
FT /id="PRO_0000327453"
FT REPEAT 393..426
FT /note="PC 1"
FT REPEAT 431..464
FT /note="PC 2"
FT REPEAT 465..499
FT /note="PC 3"
FT REPEAT 500..534
FT /note="PC 4"
FT REPEAT 536..569
FT /note="PC 5"
FT REPEAT 570..605
FT /note="PC 6"
FT REPEAT 606..638
FT /note="PC 7"
FT REPEAT 640..674
FT /note="PC 8"
FT REPEAT 675..715
FT /note="PC 9"
FT REPEAT 718..748
FT /note="PC 10"
FT REGION 272..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 832..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 922..975
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..879
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 936..962
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 975 AA; 107938 MW; FCB91CE5C5DAEDC5 CRC64;
MVAINSVSNY LSLLDEDQLE LKSYSLEKLD SCVDEFWSEI ASSSIDKIKS LSVNKQFPKH
ELASLVLSKV YYNLSDFPNS MEYALSAGSL FNVLSKSEYI ETLLYKFIDE YIKLRTSTNK
DTVINPHLES IVMGMFDRCF KEGSYKQALG IAIEARRLDI IEKAISQSGN VNSMLSYCLH
ICNVSVNNRH FRHSVLGILV NLHLAQEKPD YLSVVQCLIF LDNHIEVATI LLSLIKKDEE
SLLLAYQIGF DLFQNSTQQF LLNVRNRLPP VEKKSTTTTT TTPASDSMEI DIDSGNEKSG
GSSSFEQRLE RLHSILIGDV SIGMNLEFLY RNCSTDMHIL QSMKTTSELH KGAIFYSGTL
FANALMHAGT TRDTFLRSNI EWLYKSTHWT KFSAISSLGV INKGHIKESK SLLKTYLPGA
SVNQTPYSES GSLYALGLIH ASHGEEIIDY LVEKLHINNA ILHHGASLGL GLAAMATGRD
DLYEDLKSVL YNDDAVSGEA AGLAMGLVML GSGAKKAIEE MLAYAHETQH EKTIRSLSMG
LAFLMYGKEE SADTLIEQMI GDKDPLIRYG GMYAIAFAYC GTGHNDALRK LLHVAVSDGT
DSVRRAAVTC IGFVLSRQPE KCPKAIALLA ESYNPHVRYG AAFALGIACA GTGQRDALEI
LKSLTTDSVG YVKQAAWISM AMVLIQTSKE LVPEAETARK LFATCISDKR EDSMSKFGAV
LAFGVIDAGG RNSTIQLHSP SGHKNMNAIV GIAGFLQFWY WFPMTHFMGL ALTPTSIIGL
NKNLEMPVFT FKSNCRPSLF AYPPETKPST TSSTNKIETA ILSYSRKNKL QSSRSAMNID
QDVEKKEKEE KEAKEKEAKE KEEKEAAKAE EKEPLFERKS NPARIVPRQL QYVQFDDARY
QPIKKSPAIG IVMLRDLTPN EPEQLVVKEK PETKQETVGN QSGTATATAS LPNATTTTSP
TLPEPSTPEP FEFTE
