PSMD1_CAEEL
ID PSMD1_CAEEL Reviewed; 965 AA.
AC Q18115; Q18114;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-JAN-2003, sequence version 4.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 1;
DE AltName: Full=26S proteasome regulatory subunit rpn-2;
GN Name=rpn-2; ORFNames=C23G10.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b;
CC IsoId=Q18115-1; Sequence=Displayed;
CC Name=a;
CC IsoId=Q18115-2; Sequence=VSP_041849;
CC -!- SIMILARITY: Belongs to the proteasome subunit S1 family. {ECO:0000305}.
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DR EMBL; FO080630; CCD65306.1; -; Genomic_DNA.
DR EMBL; FO080630; CCD65298.1; -; Genomic_DNA.
DR RefSeq; NP_498346.2; NM_065945.5. [Q18115-1]
DR RefSeq; NP_498347.3; NM_065946.5. [Q18115-2]
DR AlphaFoldDB; Q18115; -.
DR SMR; Q18115; -.
DR BioGRID; 41098; 58.
DR IntAct; Q18115; 10.
DR STRING; 6239.C23G10.4b.2; -.
DR EPD; Q18115; -.
DR PaxDb; Q18115; -.
DR PeptideAtlas; Q18115; -.
DR EnsemblMetazoa; C23G10.4a.1; C23G10.4a.1; WBGene00004459. [Q18115-2]
DR EnsemblMetazoa; C23G10.4b.1; C23G10.4b.1; WBGene00004459. [Q18115-1]
DR GeneID; 175877; -.
DR KEGG; cel:CELE_C23G10.4; -.
DR UCSC; C23G10.4a.1; c. elegans. [Q18115-1]
DR CTD; 175877; -.
DR WormBase; C23G10.4a; CE40437; WBGene00004459; rpn-2. [Q18115-2]
DR WormBase; C23G10.4b; CE31311; WBGene00004459; rpn-2. [Q18115-1]
DR eggNOG; KOG2062; Eukaryota.
DR GeneTree; ENSGT00940000153386; -.
DR InParanoid; Q18115; -.
DR OMA; MIMVQQN; -.
DR OrthoDB; 235012at2759; -.
DR PhylomeDB; Q18115; -.
DR Reactome; R-CEL-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-CEL-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-CEL-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-CEL-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-CEL-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-CEL-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-CEL-382556; ABC-family proteins mediated transport.
DR Reactome; R-CEL-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-CEL-4641258; Degradation of DVL.
DR Reactome; R-CEL-5632684; Hedgehog 'on' state.
DR Reactome; R-CEL-5689603; UCH proteinases.
DR Reactome; R-CEL-5689880; Ub-specific processing proteases.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-68949; Orc1 removal from chromatin.
DR Reactome; R-CEL-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-CEL-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-CEL-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-CEL-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-CEL-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-CEL-8951664; Neddylation.
DR Reactome; R-CEL-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-CEL-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-CEL-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q18115; -.
DR PRO; PR:Q18115; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00004459; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005938; C:cell cortex; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0072686; C:mitotic spindle; IDA:WormBase.
DR GO; GO:0031965; C:nuclear membrane; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0005886; C:plasma membrane; IDA:WormBase.
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:0005080; F:protein kinase C binding; IPI:WormBase.
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; 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; 3.
DR Pfam; PF18004; RPN2_C; 1.
DR PIRSF; PIRSF015947; 26S_Psome_Rpn2; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 3: Inferred from homology;
KW Alternative splicing; Proteasome; Reference proteome; Repeat.
FT CHAIN 1..965
FT /note="26S proteasome non-ATPase regulatory subunit 1"
FT /id="PRO_0000173803"
FT REPEAT 380..413
FT /note="PC 1"
FT REPEAT 418..452
FT /note="PC 2"
FT REPEAT 454..488
FT /note="PC 3"
FT REPEAT 489..523
FT /note="PC 4"
FT REPEAT 560..595
FT /note="PC 5"
FT REPEAT 630..664
FT /note="PC 6"
FT REPEAT 665..706
FT /note="PC 7"
FT REPEAT 708..738
FT /note="PC 8"
FT REGION 836..889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 943..965
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..855
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 858..885
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 872..965
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_041849"
SQ SEQUENCE 965 AA; 106008 MW; 3015F13EF0D9B6DB CRC64;
MLTLLNRWRS QPGGASNAAA FIRVLESPKS AVTDKVLVLK AFNDWDVLVN TWFEVADALP
AVEQLLDNNT FPEHSSAALL VSKVYFCLEQ YERALEFALR GDFNVVPATR TGLGNDAEYV
NKIIETAIDT YKTLSKQGSG IPQKLRDLID RIVARNLDKR EIWFVISLGF ETTNLAMIDR
AISAMPADLT IKNQTTLVET LNRVVNGAFD RSFRFQVIDT VIKTYLKCPS PDMSKICECY
VLTDNAEAAA DTITSLIAKS LSTRAYQIAF DLYETASQGF LDRVLKRFQQ QDARDEKSME
KIHSILKGHE TVKAYLDFFV RHNHTDSVLM EEIKENIRTA SAHNALLISN GLMQYGTTCD
DFLRNNLNWV SKATNWNKFN AVASLGLIHH GQESSAMKVL EPYLPKESVE GFGFKEGGAM
LAYGLIHAKH GDATAMSTLA QWLKTAENEP VRHGACLGFG VAGLGSSSVS NYEKVREVLQ
RDEAVSGESA GIAMGLIMAG HLNQEVFNEL KQYTVDTQHD KTQRGIRTGL ACAAFGLQGD
AEPYIKEAIG AKSNPMLRST GICMLSMAYA GTGSPDVVRR LLEKVATDPN LDVKRYATIG
IGFVLSKDPS TCLSYVAMLT EHFNGHVRYG AAMALGIACA GTGNMEAIAL IEPMISDKEG
FVRKGALLSL ALIMCQQTDY TCPKVNGFRK QLLKKIGEKN EDSLVKFGAI IAQGLLDIGG
QNAAVTMQNS DKQPDMGSMV GMMCFLHGWF WHSMHFFIAL AAKPSCLVMM NENLKIPVLD
YICHANSQKF AYPPRAESKK DKDVKKIETV VLSITGKKNA SKKLIAEEKK RREAAASASS
AAAAPSSSST SGTAPAAEDE KMEVDQPGKS KKEKAPEKDT KPLHRLQNPA RVIPAQRQLI
SISDARAYSP MKPLYKGGII VADRVDKERE EKLVSEVVTQ VNTPASSGNT ENKPHSTFEI
NINDF
