PSMD4_BOVIN
ID PSMD4_BOVIN Reviewed; 382 AA.
AC Q58DA0; Q0V8P5;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 4;
DE AltName: Full=26S proteasome regulatory subunit RPN10;
GN Name=PSMD4;
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].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) 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. PSMD4 acts as an ubiquitin receptor subunit through ubiquitin-
CC interacting motifs and selects ubiquitin-conjugates for destruction.
CC Displays a preferred selectivity for longer polyubiquitin chains.
CC {ECO:0000250|UniProtKB:P55036}.
CC -!- SUBUNIT: Component of the 19S proteasome regulatory particle complex.
CC The 26S proteasome consists of a 20S core particle (CP) and two 19S
CC regulatory subunits (RP). The regulatory particle is made of a lid
CC composed of 9 subunits, a base containing 6 ATPases and few additional
CC components including PSMD4. Interacts with NUB1. Interacts with SQSTM1.
CC Interacts with UBQLN4. Interacts with UBE3A. Interacts with UBQLN1 (via
CC ubiquitin-like domain). Interacts with DDI2 (By similarity).
CC {ECO:0000250|UniProtKB:P55036}.
CC -!- DOMAIN: The 2 UIM motifs are involved in the binding to a multi-
CC ubiquitin chain in a cooperative way.
CC -!- SIMILARITY: Belongs to the proteasome subunit S5A family.
CC {ECO:0000305}.
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DR EMBL; BT021555; AAX46402.1; -; mRNA.
DR EMBL; BT021697; AAX46544.1; -; mRNA.
DR EMBL; BT021757; AAX46604.1; -; mRNA.
DR EMBL; BT026173; ABG67012.1; -; mRNA.
DR EMBL; BC119964; AAI19965.1; -; mRNA.
DR RefSeq; NP_001013616.2; NM_001013598.2.
DR AlphaFoldDB; Q58DA0; -.
DR BMRB; Q58DA0; -.
DR SMR; Q58DA0; -.
DR BioGRID; 159305; 1.
DR STRING; 9913.ENSBTAP00000008019; -.
DR PaxDb; Q58DA0; -.
DR PeptideAtlas; Q58DA0; -.
DR PRIDE; Q58DA0; -.
DR GeneID; 282016; -.
DR KEGG; bta:282016; -.
DR CTD; 5710; -.
DR eggNOG; KOG2884; Eukaryota.
DR HOGENOM; CLU_033293_0_1_1; -.
DR InParanoid; Q58DA0; -.
DR OrthoDB; 1244685at2759; -.
DR TreeFam; TF106232; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0022624; C:proteasome accessory complex; ISS:UniProtKB.
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 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 SMART; SM00327; VWA; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR PROSITE; PS50330; UIM; 2.
DR PROSITE; PS50234; VWFA; 1.
PE 2: Evidence at transcript level;
KW Isopeptide bond; Phosphoprotein; Proteasome; Reference proteome; Repeat;
KW Ubl conjugation.
FT CHAIN 1..382
FT /note="26S proteasome non-ATPase regulatory subunit 4"
FT /id="PRO_0000239112"
FT DOMAIN 5..188
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 211..230
FT /note="UIM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 282..301
FT /note="UIM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT REGION 197..262
FT /note="Interaction with UBQLN1"
FT /evidence="ECO:0000250|UniProtKB:P55036"
FT REGION 216..220
FT /note="Essential for ubiquitin-binding"
FT REGION 224..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..291
FT /note="Essential for ubiquitin-binding"
FT REGION 301..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 250
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O35226"
FT MOD_RES 253
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O35226"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35226"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55036"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55036"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55036"
FT CROSSLNK 122
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P55036"
SQ SEQUENCE 382 AA; 41384 MW; D15F1208AFD5052F CRC64;
MVLESTMVCV DNSEYMRNGD FLPTRLQAQQ DAVNIVCHSK TRSNPENNVG LITLANDCEV
LTTLTPDTGR ILSKLHTVQP KGKITFCTGI RVAHLALKHR QGKNHKMRII AFVGSPVEDN
EKDLVKLAKR LKKEKVNVDI INFGEEEVNT EKLTAFVNTL NGKDGTGSHL VTVPPGPSLA
DALISSPILA GEGGAMLGLG ASDFEFGVDP SADPELALAL RVSMEEQRQR QEEEARRAAA
ASAAEAGIAT AGTEDSDDAL LKMTISQQEF GRTGLPDLSS MTEEEQIAYA MQMSLQGAEF
GQAESADMDA SSAMDTSEPT KEEDDYDVMQ DPEFLQSVLE NLPGVDPNNE AIRNAMGSLA
SQATKDGKKD KKEEDKKEED KK
