PSMD1_PONAB
ID PSMD1_PONAB Reviewed; 953 AA.
AC Q5R5S4;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 1;
DE AltName: Full=26S proteasome regulatory subunit RPN2;
DE AltName: Full=26S proteasome regulatory subunit S1;
GN Name=PSMD1;
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:Q99460}.
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 PSMD1. Interacts with ADRM1. Interacts with ZFAND1
CC (By similarity). {ECO:0000250|UniProtKB:Q99460}.
CC -!- SIMILARITY: Belongs to the proteasome subunit S1 family. {ECO:0000305}.
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DR EMBL; CR860782; CAH92892.1; -; mRNA.
DR RefSeq; NP_001126695.1; NM_001133223.1.
DR AlphaFoldDB; Q5R5S4; -.
DR SMR; Q5R5S4; -.
DR STRING; 9601.ENSPPYP00000014825; -.
DR PRIDE; Q5R5S4; -.
DR Ensembl; ENSPPYT00000015422; ENSPPYP00000014825; ENSPPYG00000013261.
DR GeneID; 100173695; -.
DR KEGG; pon:100173695; -.
DR CTD; 5707; -.
DR eggNOG; KOG2062; Eukaryota.
DR GeneTree; ENSGT00940000153386; -.
DR HOGENOM; CLU_002323_0_0_1; -.
DR InParanoid; Q5R5S4; -.
DR OMA; MIMVQQN; -.
DR OrthoDB; 235012at2759; -.
DR TreeFam; TF105742; -.
DR Proteomes; UP000001595; Chromosome 2B.
DR GO; GO:0022624; C:proteasome accessory complex; ISS:UniProtKB.
DR GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0042176; P:regulation of protein catabolic process; IEA:InterPro.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR016642; 26S_Psome_Rpn2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002015; Proteasome/cyclosome_rpt.
DR InterPro; IPR035266; PSMD1.
DR InterPro; IPR040623; RPN2_C.
DR PANTHER; PTHR10943:SF2; PTHR10943:SF2; 1.
DR Pfam; PF01851; PC_rep; 3.
DR Pfam; PF18004; RPN2_C; 1.
DR PIRSF; PIRSF015947; 26S_Psome_Rpn2; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Phosphoprotein; Proteasome; Reference proteome; Repeat.
FT CHAIN 1..953
FT /note="26S proteasome non-ATPase regulatory subunit 1"
FT /id="PRO_0000312650"
FT REPEAT 403..436
FT /note="PC 1"
FT REPEAT 441..474
FT /note="PC 2"
FT REPEAT 476..510
FT /note="PC 3"
FT REPEAT 511..545
FT /note="PC 4"
FT REPEAT 547..580
FT /note="PC 5"
FT REPEAT 581..616
FT /note="PC 6"
FT REPEAT 617..649
FT /note="PC 7"
FT REPEAT 651..685
FT /note="PC 8"
FT REPEAT 686..726
FT /note="PC 9"
FT REPEAT 729..761
FT /note="PC 10"
FT REGION 279..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 839..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 930..953
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..874
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..953
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine; partial"
FT /evidence="ECO:0000250|UniProtKB:Q99460"
FT MOD_RES 273
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99460"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99460"
FT MOD_RES 310
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99460"
FT MOD_RES 311
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99460"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99460"
FT MOD_RES 720
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q3TXS7"
FT MOD_RES 830
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99460"
FT MOD_RES 834
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99460"
SQ SEQUENCE 953 AA; 105806 MW; 14613DCF6CA9E5FD CRC64;
MITSAAGIIS LLDEDEPQLK EFALHKLNAV VNDFWAEISE SVDKIEVLYE DEGFRSRQFA
ALVASKVFYH LGAFEESLNY ALGAGDLFNV NDNSEYVETI IAKCIDHYTK QCVENADLPE
GEKKPIDQRL EGIVNKMFQR CLDDHKYKQA IGIALETRRL DVFEKTILES NDVPGMLAYS
LKLCMSLMQN KQFRNKVLRV LVKIYMNLEK PDFINVCQCL IFLDDPQAVS DILEKLVKED
NLLMAYQICF DLYESASQQF LSSVIQNLRT VGTPIASVPG STNTGTVPGS EKDSDSMETE
EKTGSAFVGK TPEASPEPKD QTLKMIKILS GEMAIELHLQ FLIRNNNTDL MILKNTKDAV
RNSVCHTATV IANSFMHCGT TSDQFLRDNL EWLARATNWA KFTATASLGV IHKGHEKEAL
QLMATYLPKD TSPGSAYQEG GGLYALGLIH ANHGGDIIDY LLNQLKNASN DIVRHGGSLG
LGLAAMGTAR QDVYDLLKTN LYQDDAVTGE AAGLALGLVM LGSKNAQAIE DMVGYAQETQ
HEKILRGLAV GIALVMYGRM EEADALIESL CRDKDPILRR SGMYTVAMAY CGSGNNKAIR
RLLHVAVSDV NDDVRRAAVE SLGFILFRTP EQCPSVVSLL SESYNPHVRY GAAMALGICC
AGTGNKEAIN LLEPMTNDPV NYVRQGALIA SALIMIQQTE ITCPKVNQFR QLYSKVINDK
HDDVMAKFGA ILAQGILDAG GHNVTISLQS RTGHTHMPSV VGVLVFTQFW FWFPLSHFLS
LAYTPTCVIG LNKDLKMPKV QYKSNCKPST FAYPAPLEVP KEKEKEKVST AVLSITAKAK
KKEKEKEKKE EEKMEVDEAE KKEEKEKKKE PEPNFQLLDN PARVMPAQLK VLTMPETCRY
QPFKPLSIGG IIILKDTSED IEELVEPVAA HGPKIEEEEQ EPEPPEPFEY IDD