PSMD8_PONAB
ID PSMD8_PONAB Reviewed; 289 AA.
AC Q5RE15;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 8;
DE AltName: Full=26S proteasome regulatory subunit RPN12;
DE Flags: Fragment;
GN Name=PSMD8;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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:P48556}.
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 including PSMD8, a base containing 6 ATPases and
CC few additional components. Interacts with DDI2 (By similarity).
CC Interacts with TASOR (By similarity). {ECO:0000250|UniProtKB:P48556,
CC ECO:0000250|UniProtKB:Q9CX56}.
CC -!- SIMILARITY: Belongs to the proteasome subunit S14 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAH89992.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CR857724; CAH89992.1; ALT_INIT; mRNA.
DR AlphaFoldDB; Q5RE15; -.
DR SMR; Q5RE15; -.
DR STRING; 9601.ENSPPYP00000011119; -.
DR eggNOG; KOG3151; Eukaryota.
DR InParanoid; Q5RE15; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0022624; C:proteasome accessory complex; ISS:UniProtKB.
DR GO; GO:0005838; C:proteasome regulatory particle; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR InterPro; IPR006746; 26S_Psome_Rpn12.
DR InterPro; IPR033464; CSN8_PSD8_EIF3K.
DR InterPro; IPR000717; PCI_dom.
DR PANTHER; PTHR12387; PTHR12387; 1.
DR Pfam; PF10075; CSN8_PSD8_EIF3K; 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..289
FT /note="26S proteasome non-ATPase regulatory subunit 8"
FT /id="PRO_0000233270"
FT DOMAIN 101..270
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48556"
FT CROSSLNK 236
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P48556"
FT NON_TER 1
SQ SEQUENCE 289 AA; 32806 MW; FF24A44DD05FC557 CRC64;
RKMAAAAVNG AAGFSSSGPA ATSGAVLQAA TGMYEQLKGE WNRKSPNLSK CGEELGRLKL
VLLELNFLPT TGTKLTKQQL ILARDILEIG AQWSILRKDI PSFERYMAQL KCYYFDYKEQ
LPESAYMHQL LGLNLLFLLS QNRVAEFHTE LERLPAKDIQ TNVYIKHPVS LEQYLMEGSY
NKVFLAKGNI PAESYAFFID ILLDTIRDEI AGCIEKAYEK ILFTEATRIL FFNTPKKMTD
YAKKRGWVLG PNNYYSFASQ QQKPEDTTIP STELAKQVIE YARQLEMIV