PSMD4_CAEEL
ID PSMD4_CAEEL Reviewed; 346 AA.
AC O61742;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 4 {ECO:0000250|UniProtKB:P55036};
DE AltName: Full=26S proteasome regulatory subunit rpn-10 {ECO:0000305};
GN Name=rpn-10 {ECO:0000312|WormBase:B0205.3};
GN ORFNames=B0205.3 {ECO:0000312|WormBase:B0205.3};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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).
RN [2] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17050737; DOI=10.1091/mbc.e06-05-0437;
RA Shimada M., Kanematsu K., Tanaka K., Yokosawa H., Kawahara H.;
RT "Proteasomal ubiquitin receptor RPN-10 controls sex determination in
RT Caenorhabditis elegans.";
RL Mol. Biol. Cell 17:5356-5371(2006).
RN [3] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20453865; DOI=10.1038/nmeth.1460;
RA Hamer G., Matilainen O., Holmberg C.I.;
RT "A photoconvertible reporter of the ubiquitin-proteasome system in vivo.";
RL Nat. Methods 7:473-478(2010).
RN [4] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22105480; DOI=10.1038/cr.2011.182;
RA Zhou Q., Li H., Xue D.;
RT "Elimination of paternal mitochondria through the lysosomal degradation
RT pathway in C. elegans.";
RL Cell Res. 21:1662-1669(2011).
RN [5] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=26828939; DOI=10.1371/journal.pgen.1005823;
RA Keith S.A., Maddux S.K., Zhong Y., Chinchankar M.N., Ferguson A.A.,
RA Ghazi A., Fisher A.L.;
RT "Graded proteasome dysfunction in Caenorhabditis elegans activates an
RT adaptive response involving the conserved skn-1 and elt-2 transcription
RT factors and the autophagy-lysosome pathway.";
RL PLoS Genet. 12:E1005823-E1005823(2016).
CC -!- FUNCTION: Binds and presumably selects ubiquitin-conjugates for
CC destruction (By similarity). Required for protein degradation and
CC ubiquitin-proteasome system (UBS) function and regulates proteasomal
CC subunit expression (PubMed:20453865, PubMed:22105480, PubMed:26828939).
CC Involvement in UBS might be cell type specific (PubMed:20453865).
CC Regulator of the autophagy-lysosome pathway that may confer resistance
CC to autophagy by regulating the expression of autophagy-related proteins
CC such as lgg-1, and by regulating lysosome formation, possibly by
CC modulating elt-2 activity (PubMed:26828939). Required for fertility,
CC sperm production, and sex determination through regulation of tra-2
CC protein (PubMed:17050737). Plays a role in the elimination of paternal
CC mitochondria in fertilized eggs (PubMed:22105480).
CC {ECO:0000250|UniProtKB:P55036, ECO:0000269|PubMed:17050737,
CC ECO:0000269|PubMed:20453865, ECO:0000269|PubMed:22105480,
CC ECO:0000269|PubMed:26828939}.
CC -!- SUBUNIT: The 26S proteasome is composed of a core protease, known as
CC the 20S proteasome, capped at one or both ends by the 19S regulatory
CC complex (RC). The RC is composed of at least 18 different subunits in
CC two subcomplexes, the base and the lid, which form the portions
CC proximal and distal to the 20S proteolytic core, respectively.
CC {ECO:0000250|UniProtKB:P14685}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26828939}. Nucleus
CC {ECO:0000269|PubMed:26828939}.
CC -!- TISSUE SPECIFICITY: Broadly expressed with high expression in the
CC pharynx, intestine, hypodermis and spermatheca and weak expression in
CC the excretory cell, body wall muscle, vulva and somatic gonad.
CC {ECO:0000269|PubMed:26828939}.
CC -!- DISRUPTION PHENOTYPE: Temperature-dependent increase in lifespan with a
CC modest increase at 20 degrees Celsius and a 30% increase in mean
CC lifespan at 25 degrees Celsius compared to wild-type animals
CC (PubMed:26828939). Reduced fertility with no sperm produced in the
CC spermatheca, accumulation of a sex-determination protein tra-2 in the
CC intestine, no embryos in the uterus, and an increase in the development
CC time to adulthood as evidenced by an expansion of the proximal oocytes
CC at a young adult stage (PubMed:17050737, PubMed:26828939). Reduced
CC ubiquitin-proteasome system function (UBS), particularly in dorsorectal
CC neurons (PubMed:20453865, PubMed:26828939). Enhanced protein stability
CC and increased resistance to protostasis in response to thermal stress
CC and oxidative stress induced by tert-butyl hydroperoxide
CC (PubMed:26828939). Irregular autophagy-lysosome pathway function with
CC increased autophagy coupled with fewer intestinal lysosomes and reduced
CC lysosomal function (PubMed:26828939). RNAi-mediated knockdown of skn-1
CC or elt-2 in the null mutant results in animals which are smaller and
CC that developmentally arrest before adulthood (PubMed:26828939). RNAi-
CC mediated knockdown results in reduced egg laying, abnormal gonad
CC morphology with expansion of the proximal gonad greater than that of
CC wild-type animals, and defective degradation of polyubiquitinated
CC proteins and leads to an accumulation of these proteins
CC (PubMed:17050737). Also results in delayed removal of paternal
CC mitochondria until 4-fold stage of embryonic development
CC (PubMed:22105480). {ECO:0000269|PubMed:17050737,
CC ECO:0000269|PubMed:20453865, ECO:0000269|PubMed:22105480,
CC ECO:0000269|PubMed:26828939}.
CC -!- SIMILARITY: Belongs to the proteasome subunit S5A family.
CC {ECO:0000305}.
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DR EMBL; BX284601; CCD61298.1; -; Genomic_DNA.
DR RefSeq; NP_492809.1; NM_060408.4.
DR AlphaFoldDB; O61742; -.
DR SMR; O61742; -.
DR IntAct; O61742; 23.
DR MINT; O61742; -.
DR STRING; 6239.B0205.3.1; -.
DR EPD; O61742; -.
DR PaxDb; O61742; -.
DR PeptideAtlas; O61742; -.
DR EnsemblMetazoa; B0205.3.1; B0205.3.1; WBGene00004466.
DR GeneID; 172977; -.
DR KEGG; cel:CELE_B0205.3; -.
DR UCSC; B0205.3.1; c. elegans.
DR CTD; 172977; -.
DR WormBase; B0205.3; CE26355; WBGene00004466; rpn-10.
DR eggNOG; KOG2884; Eukaryota.
DR GeneTree; ENSGT00530000064050; -.
DR HOGENOM; CLU_033293_0_0_1; -.
DR InParanoid; O61742; -.
DR OMA; RIVIFVC; -.
DR OrthoDB; 1244685at2759; -.
DR PhylomeDB; O61742; -.
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-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; O61742; -.
DR PRO; PR:O61742; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00004466; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IBA:GO_Central.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IMP:WormBase.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:WormBase.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR003903; UIM_dom.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF02809; UIM; 2.
DR Pfam; PF13519; VWA_2; 1.
DR SMART; SM00726; UIM; 2.
DR SUPFAM; SSF53300; SSF53300; 1.
DR PROSITE; PS50330; UIM; 2.
PE 2: Evidence at transcript level;
KW Cytoplasm; Nucleus; Proteasome; Reference proteome; Repeat.
FT CHAIN 1..346
FT /note="26S proteasome non-ATPase regulatory subunit 4"
FT /evidence="ECO:0000305"
FT /id="PRO_0000436780"
FT DOMAIN 5..190
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 216..235
FT /note="UIM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 273..292
FT /note="UIM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT REGION 290..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 346 AA; 37348 MW; ADAFB35DE60BDE48 CRC64;
MVQESTMICV DNSEYMRNGD FQPTRLQSQQ DAVNLVTQCK LRANPENAVG ILSMANSVQV
LSSLSTEQGR LMMKNHSIEP FGKCNFIAGI KIAHLALKHR QNRNHKMRVV LFIGSPLEEI
EMNELVKIAK KMKKEKVLCD VIMFGENESD GHEKFSTFVD TLNGKEGSGS SLIVVPQGSS
LTDALLQSSV CKNEDGQAAF GGGGNGMDNA FGMDVENDPD LALALRVSME EERARQAAAA
AANGGAADSG ADAEVAAAAA AVPLEEMDMG AMTEEQQLEW ALRLSMQENA PAEQPQVQHE
QMDVDGAPAV GGDNLDDLMN NPELLQQIVD DLPAANAEKD DDKEKK
