PSMD3_MOUSE
ID PSMD3_MOUSE Reviewed; 530 AA.
AC P14685; Q3TP95; Q99LL7;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 3;
DE AltName: Full=26S proteasome regulatory subunit RPN3;
DE AltName: Full=26S proteasome regulatory subunit S3;
DE AltName: Full=Proteasome subunit p58;
DE AltName: Full=Transplantation antigen P91A;
DE AltName: Full=Tum-P91A antigen;
GN Name=Psmd3; Synonyms=P91a, Tstap91a;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2568889; DOI=10.1016/0092-8674(89)90844-1;
RA Lurquin C., van Pel A., Mariame B., de Plaen E., Szikora J.-P.,
RA Janssens C., Reddehase M.J., Lejeune J., Boon T.;
RT "Structure of the gene of tum- transplantation antigen P91A: the mutated
RT exon encodes a peptide recognized with Ld by cytolytic T cells.";
RL Cell 58:293-303(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Kidney, Lung, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP IDENTIFICATION IN THE 19S PROTEASOME REGULATORY COMPLEX.
RX PubMed=16857966; DOI=10.1161/01.res.0000237386.98506.f7;
RA Gomes A.V., Zong C., Edmondson R.D., Li X., Stefani E., Zhang J.,
RA Jones R.C., Thyparambil S., Wang G.W., Qiao X., Bardag-Gorce F., Ping P.;
RT "Mapping the murine cardiac 26S proteasome complexes.";
RL Circ. Res. 99:362-371(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-426, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Component of the 26S proteasome, a multiprotein complex
CC involved in the ATP-dependent degradation of ubiquitinated proteins.
CC This complex plays a key role in the maintenance of protein homeostasis
CC by removing misfolded or damaged proteins, which could impair cellular
CC functions, and by removing proteins whose functions are no longer
CC required. Therefore, the proteasome participates in numerous cellular
CC processes, including cell cycle progression, apoptosis, or DNA damage
CC repair. {ECO:0000250|UniProtKB:O43242}.
CC -!- SUBUNIT: Component of the 19S proteasome regulatory particle complex
CC (PubMed:16857966). The 26S proteasome consists of a 20S core particle
CC (CP) and two 19S regulatory subunits (RP) (By similarity). The
CC regulatory particle is made of a lid composed of 9 subunits including
CC PSMD3, a base containing 6 ATPases and few additional components (By
CC similarity). Interacts with UBQLN1 (via ubiquitin-like domain) (By
CC similarity). Interacts with ERCC6 (By similarity).
CC {ECO:0000250|UniProtKB:O43242, ECO:0000269|PubMed:16857966}.
CC -!- SIMILARITY: Belongs to the proteasome subunit S3 family. {ECO:0000305}.
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DR EMBL; M25149; AAA37241.1; -; Genomic_DNA.
DR EMBL; AK145488; BAE26466.1; -; mRNA.
DR EMBL; AK164593; BAE37842.1; -; mRNA.
DR EMBL; AK165520; BAE38235.1; -; mRNA.
DR EMBL; AK166683; BAE38942.1; -; mRNA.
DR EMBL; AK166714; BAE38965.1; -; mRNA.
DR EMBL; AK167285; BAE39391.1; -; mRNA.
DR EMBL; AK169690; BAE41307.1; -; mRNA.
DR EMBL; AL590963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466556; EDL16159.1; -; Genomic_DNA.
DR EMBL; BC003197; AAH03197.1; -; mRNA.
DR CCDS; CCDS25359.1; -.
DR PIR; I49504; I49504.
DR RefSeq; NP_033465.1; NM_009439.1.
DR AlphaFoldDB; P14685; -.
DR SMR; P14685; -.
DR BioGRID; 204358; 59.
DR IntAct; P14685; 7.
DR STRING; 10090.ENSMUSP00000017365; -.
DR iPTMnet; P14685; -.
DR PhosphoSitePlus; P14685; -.
DR SwissPalm; P14685; -.
DR EPD; P14685; -.
DR jPOST; P14685; -.
DR MaxQB; P14685; -.
DR PaxDb; P14685; -.
DR PeptideAtlas; P14685; -.
DR PRIDE; P14685; -.
DR ProteomicsDB; 301864; -.
DR Antibodypedia; 28451; 307 antibodies from 29 providers.
DR DNASU; 22123; -.
DR Ensembl; ENSMUST00000017365; ENSMUSP00000017365; ENSMUSG00000017221.
DR GeneID; 22123; -.
DR KEGG; mmu:22123; -.
DR UCSC; uc007lgw.1; mouse.
DR CTD; 5709; -.
DR MGI; MGI:98858; Psmd3.
DR VEuPathDB; HostDB:ENSMUSG00000017221; -.
DR eggNOG; KOG2581; Eukaryota.
DR GeneTree; ENSGT00940000153653; -.
DR HOGENOM; CLU_019858_1_2_1; -.
DR InParanoid; P14685; -.
DR OMA; ENFGPQF; -.
DR OrthoDB; 836599at2759; -.
DR PhylomeDB; P14685; -.
DR TreeFam; TF106110; -.
DR Reactome; R-MMU-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-MMU-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-MMU-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-MMU-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-MMU-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-MMU-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-MMU-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-MMU-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-MMU-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-MMU-202424; Downstream TCR signaling.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-MMU-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-MMU-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-MMU-382556; ABC-family proteins mediated transport.
DR Reactome; R-MMU-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-MMU-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-MMU-4641257; Degradation of AXIN.
DR Reactome; R-MMU-4641258; Degradation of DVL.
DR Reactome; R-MMU-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-MMU-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-MMU-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-MMU-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-MMU-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-MMU-5632684; Hedgehog 'on' state.
DR Reactome; R-MMU-5658442; Regulation of RAS by GAPs.
DR Reactome; R-MMU-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-MMU-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-MMU-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-MMU-5689603; UCH proteinases.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-68867; Assembly of the pre-replicative complex.
DR Reactome; R-MMU-68949; Orc1 removal from chromatin.
DR Reactome; R-MMU-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-MMU-69481; G2/M Checkpoints.
DR Reactome; R-MMU-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-MMU-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-MMU-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-MMU-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-MMU-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-MMU-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-MMU-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-MMU-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-9020702; Interleukin-1 signaling.
DR Reactome; R-MMU-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-MMU-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR BioGRID-ORCS; 22123; 26 hits in 70 CRISPR screens.
DR ChiTaRS; Psmd3; mouse.
DR PRO; PR:P14685; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P14685; protein.
DR Bgee; ENSMUSG00000017221; Expressed in ectoplacental cone and 261 other tissues.
DR ExpressionAtlas; P14685; baseline and differential.
DR Genevisible; P14685; MM.
DR GO; GO:0022624; C:proteasome accessory complex; IDA:UniProtKB.
DR GO; GO:0000502; C:proteasome complex; ISO:MGI.
DR GO; GO:0005838; C:proteasome regulatory particle; IDA:MGI.
DR GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IBA:GO_Central.
DR GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR GO; GO:0042176; P:regulation of protein catabolic process; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR013586; 26S_Psome_reg_C.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR035267; PSMD3.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10758:SF2; PTHR10758:SF2; 1.
DR Pfam; PF01399; PCI; 1.
DR Pfam; PF08375; Rpn3_C; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW Isopeptide bond; Phosphoprotein; Proteasome; Reference proteome;
KW Tumor antigen; Ubl conjugation.
FT CHAIN 1..530
FT /note="26S proteasome non-ATPase regulatory subunit 3"
FT /id="PRO_0000173817"
FT DOMAIN 282..461
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..517
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 414
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43242"
FT MOD_RES 426
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 36
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:O43242"
FT CROSSLNK 36
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:O43242"
FT CONFLICT 12..13
FT /note="AD -> H (in Ref. 1; AAA37241)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="R -> H (in Ref. 1; AAA37241)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 530 AA; 60718 MW; CAB9C9AA3A0EEC8D CRC64;
MKQEGSARRR GADKAKPPPG GEQEPPPPAP QDVEMKEEAA AGSGSTGEGD GKAAATEHSQ
RELDTVTLED IKEHVRQLEK AVSGKEPRFV LRALRMLPST SRRLNHYVLY KAVHGFFTSN
NATRDFLLPF LEEPMDTEAD LQFRPRTGKA ASAPLLPEVE AYLQLLMVIF LMNSKRYKEA
QKISDDLMQK ISTQNRRALD LVAAKCYYYH ARVYEFLDKL DVVRSFLHAR LRTATLRHDA
DGQATLLNLL LRNYLHYSLY DQAEKLVSKS VFPEQANNNE WARYLYYTGR IKAIQLEYSE
ARRTMTNALR KAPQHTAVGF KQTVHKLLIV VELLLGEIPD RLQFRQPSLK RSLMPYFLLT
QAVRTGNLAK FNQVLDQFGE KFQTDGTYTL IIRLRHNVIK TGVRMISLSY SRISLADIAQ
KLQLDSPEDA EFIVAKAIRD GVIEASINHE KGYVQSKEMI DIYSTREPQL AFHQRISFCL
DIHNMSVKAM RFPPKSYNKD LESAEERRER EQQDLEFAKE MAEDDDDSFP
