PSMD3_BOVIN
ID PSMD3_BOVIN Reviewed; 534 AA.
AC Q2KJ46;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 3;
DE AltName: Full=26S proteasome regulatory subunit RPN3;
GN Name=PSMD3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). 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}.
CC -!- SIMILARITY: Belongs to the proteasome subunit S3 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC105526; AAI05527.1; -; mRNA.
DR RefSeq; NP_001039365.1; NM_001045900.1.
DR AlphaFoldDB; Q2KJ46; -.
DR SMR; Q2KJ46; -.
DR BioGRID; 161586; 1.
DR STRING; 9913.ENSBTAP00000028608; -.
DR PaxDb; Q2KJ46; -.
DR PeptideAtlas; Q2KJ46; -.
DR PRIDE; Q2KJ46; -.
DR Ensembl; ENSBTAT00000028608; ENSBTAP00000028608; ENSBTAG00000021461.
DR GeneID; 504937; -.
DR KEGG; bta:504937; -.
DR CTD; 5709; -.
DR VEuPathDB; HostDB:ENSBTAG00000021461; -.
DR VGNC; VGNC:33467; PSMD3.
DR eggNOG; KOG2581; Eukaryota.
DR GeneTree; ENSGT00940000153653; -.
DR HOGENOM; CLU_019858_1_2_1; -.
DR InParanoid; Q2KJ46; -.
DR OMA; ENFGPQF; -.
DR OrthoDB; 836599at2759; -.
DR TreeFam; TF106110; -.
DR Reactome; R-BTA-6798695; Neutrophil degranulation.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000021461; Expressed in retina and 105 other tissues.
DR GO; GO:0022624; C:proteasome accessory complex; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Isopeptide bond; Phosphoprotein; Proteasome; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..534
FT /note="26S proteasome non-ATPase regulatory subunit 3"
FT /id="PRO_0000283070"
FT DOMAIN 286..465
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..34
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..521
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 418
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43242"
FT MOD_RES 430
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43242"
FT CROSSLNK 38
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:O43242"
FT CROSSLNK 38
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:O43242"
SQ SEQUENCE 534 AA; 60957 MW; AF342D567F29FEB0 CRC64;
MKQEGSARRR GADKAKPPPG GGEQEPPPPP APQDVEMKEE AAAGGGSTGE TAGKTAAAAA
EHSQRELDTV TLEDIKEHVK QLEKAVSGKE PRFVLRALRM LPSTSRRLNH YVLYKAVHGF
FTSNNATRDF LLPFLEEPMD TEADLQFRPR TGKAASAPLL PEVEAYLQLL MVIFLMNSKR
YKEAQKISDD LMQKISTQNR RALDLVAAKC YYYHARVYEF LDKLDVVRSF LHARLRTATL
RHDTDGQATL LNLLLRNYLH YSLYDQAEKL VSKSVFPEQA NNNEWARYLY YTGRIKAIQL
EYSEARRTMT NALRKAPQHT AVGFKQTVHK LLIVVELLLG EIPDRLQFRQ PSLKRSLMPY
FLLTQAVRTG NLAKFNQVLD QFGEKFQADG TYTLIIRLRH NVIKTGVRMI SLSYSRISLA
DIAQKLQLDS PEDAEFIVAK AIRDGVIEAS INHEKGYVQS KEMIDIYSTR EPQLAFHQRI
SFCLDIHNMS VKAMRFPPKS YNKDLESAEE RREREQQDLE FAKEMAEDDD DSFP
