PSMD2_PONAB
ID PSMD2_PONAB Reviewed; 908 AA.
AC Q5R9I6;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 2;
GN Name=PSMD2;
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=Brain cortex;
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:Q13200}.
CC -!- FUNCTION: Binds to the intracellular domain of tumor necrosis factor
CC type 1 receptor. The binding domain of TRAP1 and TRAP2 resides outside
CC the death domain of TNFR1. {ECO:0000250|UniProtKB:Q13200}.
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 PSMD2 (By similarity). Interacts with RPGRIP1L (By
CC similarity). Interacts with CRY1 in a KDM8-dependent manner (By
CC similarity). {ECO:0000250|UniProtKB:Q13200,
CC ECO:0000250|UniProtKB:Q8VDM4}.
CC -!- SIMILARITY: Belongs to the proteasome subunit S2 family. {ECO:0000305}.
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DR EMBL; CR859401; CAH91574.1; -; mRNA.
DR EMBL; CR859332; CAH91509.1; -; mRNA.
DR RefSeq; NP_001125887.1; NM_001132415.1.
DR AlphaFoldDB; Q5R9I6; -.
DR SMR; Q5R9I6; -.
DR STRING; 9601.ENSPPYP00000016052; -.
DR Ensembl; ENSPPYT00000016696; ENSPPYP00000016052; ENSPPYG00000014354.
DR GeneID; 100172819; -.
DR KEGG; pon:100172819; -.
DR CTD; 5708; -.
DR eggNOG; KOG2005; Eukaryota.
DR GeneTree; ENSGT00940000153386; -.
DR HOGENOM; CLU_008705_1_0_1; -.
DR InParanoid; Q5R9I6; -.
DR OrthoDB; 229956at2759; -.
DR Proteomes; UP000001595; Chromosome 3.
DR GO; GO:0022624; C:proteasome accessory complex; ISS:UniProtKB.
DR GO; GO:0005838; C:proteasome regulatory particle; IEA:Ensembl.
DR GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR GO; GO:0042176; P:regulation of protein catabolic process; IEA:InterPro.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR016643; 26S_Psome_Rpn1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002015; Proteasome/cyclosome_rpt.
DR InterPro; IPR041433; RPN1_C.
DR InterPro; IPR040892; RPN1_N.
DR PANTHER; PTHR10943:SF11; PTHR10943:SF11; 1.
DR Pfam; PF01851; PC_rep; 2.
DR Pfam; PF18051; RPN1_C; 1.
DR Pfam; PF17781; RPN1_RPN2_N; 1.
DR PIRSF; PIRSF015965; 26S_Psome_Rpn1; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Phosphoprotein; Proteasome; Reference proteome; Repeat.
FT CHAIN 1..908
FT /note="26S proteasome non-ATPase regulatory subunit 2"
FT /id="PRO_0000289998"
FT REPEAT 409..442
FT /note="PC 1"
FT REPEAT 443..479
FT /note="PC 2"
FT REPEAT 480..514
FT /note="PC 3"
FT REPEAT 517..551
FT /note="PC 4"
FT REPEAT 560..589
FT /note="PC 5"
FT REPEAT 692..723
FT /note="PC 6"
FT REPEAT 742..757
FT /note="PC 7"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDM4"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13200"
FT MOD_RES 24
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13200"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13200"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13200"
FT MOD_RES 194
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q13200"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13200"
FT MOD_RES 363
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13200"
FT MOD_RES 551
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDM4"
SQ SEQUENCE 908 AA; 100230 MW; 3599E54B84737A5D CRC64;
MEEGGRDKAP VQPQQSPAAA LGGTDEKPSG KERRDAGDKD KEQELSEEDK QLQDELEMLV
ERLGEKDTSL YRPALEELRR QIRSSTTSMT SVPKPLKFLR PHYGKLKEIY ENMAPGENKR
FAADIISVLA MTMSGERECL KYRLVGSQEE LASWGHEYVR HLAGEVAKEW QELDDAEKVQ
REPLLTLVKE IIPYNMAHNA EHEACDLLME IEQVDMLEKD IDENAYAKVC LYLTSCVNYV
PEPENSALLR CALGVFRKFS RFPEALRLAL MLNDMELVED IFTSCKDVVV QKQMAFMLGR
HGVFLELSED VEEYEDLTEI MSNVQLNSNF LALARELDIM EPKVPDDIYK THLENNRFGG
SGSQVDSARM NLASSFVNGF VNAAFGQDKL LTDDGNKWLY KNKDHGMLSA AASLGMILLW
DVDGGLTQID KYLYSSEDYI KSGALLACGI VNSGVRNECD PALALLSDYV LHNSNTMRLG
SIFGLGLAYA GSNREDVLTL LLPVMGDSKS SMEVAGVTAL ACGMIAVGSC NGDVTSTILQ
TIMEKSETEL KDTYARWLPL GLGLNHLGKG EAIEAILAAL EVVSEPFRSF ANTLVDVCAY
AGSGNVLKVQ QLLHICSEHF DSKEKEEDKD KKEKKDKDKK EAPADMGAHQ GVAVLGIALI
AMGEEIGAEM ALRTFGHLLR YGEPTLRRAV PLALALISVS NPRLNILDTL SKFSHDADPE
VSYNSIFAMG MVGSGTNNAR LAAMLRQLAQ YHAKDPNNLF MVRLAQGLTH LGKGTLTLCP
YHSDRQLMSQ VAVAGLLTVL VSFLDVRNII LGKSHYVLYG LVAAMQPRML VTFDEELRPL
PVSVRVGQAV DVVGQAGKPK TITGFQTHTT PVLLAHGERA ELATEEFLPV TPILEGFVIL
RKNPNYDL
