PSMD2_DICDI
ID PSMD2_DICDI Reviewed; 893 AA.
AC Q54BC6;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 2;
GN Name=psmD2; ORFNames=DDB_G0293752;
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 PROTEIN SEQUENCE OF 2-13; 111-121; 351-371; 460-497; 666-689; 724-731 AND
RP 805-855, CLEAVAGE OF INITIATOR METHIONINE, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=AX2;
RA Bienvenut W.V., Ura S., Insall R.H.;
RL Submitted (JUL-2009) to UniProtKB.
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 S2 family. {ECO:0000305}.
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DR EMBL; AAFI02000219; EAL60553.1; -; Genomic_DNA.
DR RefSeq; XP_628968.1; XM_628966.1.
DR AlphaFoldDB; Q54BC6; -.
DR SMR; Q54BC6; -.
DR BioGRID; 1254399; 1.
DR STRING; 44689.DDB0232978; -.
DR PaxDb; Q54BC6; -.
DR EnsemblProtists; EAL60553; EAL60553; DDB_G0293752.
DR GeneID; 8629396; -.
DR KEGG; ddi:DDB_G0293752; -.
DR dictyBase; DDB_G0293752; psmD2.
DR eggNOG; KOG2005; Eukaryota.
DR HOGENOM; CLU_008705_1_0_1; -.
DR InParanoid; Q54BC6; -.
DR OMA; KTVYKHM; -.
DR PhylomeDB; Q54BC6; -.
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:Q54BC6; -.
DR Proteomes; UP000002195; Chromosome 6.
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:0030234; F:enzyme regulator activity; IEA:InterPro.
DR GO; GO:0006972; P:hyperosmotic response; IEP:dictyBase.
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 Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR016643; 26S_Psome_Rpn1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002015; Proteasome/cyclosome_rpt.
DR InterPro; IPR041433; RPN1_C.
DR InterPro; IPR040892; RPN1_N.
DR PANTHER; PTHR10943:SF1; PTHR10943:SF1; 1.
DR Pfam; PF01851; PC_rep; 1.
DR Pfam; PF18051; RPN1_C; 1.
DR Pfam; PF17781; RPN1_RPN2_N; 1.
DR PIRSF; PIRSF015965; 26S_Psome_Rpn1; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Proteasome; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 2..893
FT /note="26S proteasome non-ATPase regulatory subunit 2"
FT /id="PRO_0000327454"
FT REPEAT 412..445
FT /note="PC 1"
FT REPEAT 446..482
FT /note="PC 2"
FT REPEAT 483..517
FT /note="PC 3"
FT REPEAT 522..555
FT /note="PC 4"
FT REPEAT 562..583
FT /note="PC 5"
FT REPEAT 666..700
FT /note="PC 6"
FT REPEAT 701..735
FT /note="PC 7"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 893 AA; 98366 MW; 89C887C081711687 CRC64;
MPQKEVTIPV PAKGGSNKEE DKKDNKDTEE KNTTTNTTTK DNKKDKKKDK KEETLSPEDE
KLKNDLELLV ERSRDEKEEI ALAALEALKT EIRSSTSSMT SVPKPLKFLR NHYSTLVDIY
KNSKEGKAKT SLADILSVLA MANGNDERDT LKYKLLGSGE AIASWGHEYV KHLATEIGVE
YDIKKEENQS VEDLLKLVDE IVPFQMTHNA EPEACDLLLE VEQLSKIFQY IDENNYSRVC
LYLFKCSYYV PGPDDINILK VCVEIYIKMK QYPDALRVAM KISDPELITE IFKLVENNKS
ILQQLGFLVA RQKIVPDNFN YDSISDIINN SKLSEYFMNL ATDLDIREPK LPEEIFQSHL
DSTSAIADSA RMNLASSFVN AFVNAGFGKD KLMTAEEDTK WWFKNRELGI LSTVASTGMV
VLWDIDGGLT KIDKFLYSQE KHCSNGALMA IGMLTSGIRS EMDPALSLLA EHINSSNTGT
RISAIFGLGL AYAGTQRQDL MSLLSPCLDD DKEKMEFIGI VGLALGLIFI GSCDPELSTL
FVQTLIQRGT AASESHARFL HLGLGLLYLG KQDAAELALE TLKAIEGKGG EYARLTVEAC
AYAGTGNVLK VQNMLHFCSD GQENPHHGLA VLSIALIAMG EELGSDMCLR MFDHLLQKGN
VHIKRAIPLA LGLLSPSNPR IAIMDILSKL SHDNDPEVAQ GAILSLGLIG AGTNNARIGG
MLRALAVFYG KDVHLFFVRI AQGLLHLGKG TMTINPYHSD RTLMSPVAVG GLLALLHAGL
DIKNILSTQS HYLFFSIVCS MYPRMLMTLD EDLKPLPVSV RVGQSVDIVG LAGKPKTITG
FQTHTTPVLL GYNERAELAT DDYIPLTNIL EGIVILKPNP NASVTSPLAS KKN
