PSMD1_CHICK
ID PSMD1_CHICK Reviewed; 955 AA.
AC Q5F418;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
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; ORFNames=RCJMB04_3m24;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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.
CC {ECO:0000250|UniProtKB:Q99460}.
CC -!- SIMILARITY: Belongs to the proteasome subunit S1 family. {ECO:0000305}.
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DR EMBL; AJ851482; CAH65116.1; -; mRNA.
DR RefSeq; NP_001012618.2; NM_001012600.3.
DR AlphaFoldDB; Q5F418; -.
DR SMR; Q5F418; -.
DR STRING; 9031.ENSGALP00000012405; -.
DR PaxDb; Q5F418; -.
DR GeneID; 424926; -.
DR KEGG; gga:424926; -.
DR CTD; 5707; -.
DR VEuPathDB; HostDB:geneid_424926; -.
DR eggNOG; KOG2062; Eukaryota.
DR InParanoid; Q5F418; -.
DR OrthoDB; 235012at2759; -.
DR PhylomeDB; Q5F418; -.
DR PRO; PR:Q5F418; -.
DR Proteomes; UP000000539; Unplaced.
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:0034515; C:proteasome storage granule; IBA:GO_Central.
DR GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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 Proteasome; Reference proteome; Repeat.
FT CHAIN 1..955
FT /note="26S proteasome non-ATPase regulatory subunit 1"
FT /id="PRO_0000312651"
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..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 839..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 932..955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..876
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 941..955
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 955 AA; 106063 MW; AB3920991DCF749C CRC64;
MITSAAGIIS LLDEEEPQLK EFALHKLNAV VNDFWAEISE SVDKIEVLYE DEGFRSRQFA
ALVASKVFYH LGAFEESLNY ALGAGDLFNV NDNSEYVETI IAKCIDHYTK QCVENAELPE
GEKKPVDERL EGIVNKMFQR CLDDHKYKQA IGIALETRRL DIFEKTILES NDVPGMLAYS
LKLCMSLMQN KQFRNKVLRV LVKIYMNLEK PDFINVCQCL IFLDDPQAVS DILEKLVKED
NLLMAYQICF DLYESASQQF LSSVIQNLRT VGTPIASVPG STNTGTVPGS EKDSDAMEAE
EKPGSTCVGK SAEINPEPKD QISKMIKILS 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 ITCPKVSQFR QLYSKVINDK
HDDVMAKFGA ILAQGILDAG GHNVIISLQS RTGHTHMPSV VGVLVFTQFW FWFPLSHFLS
LAFTPTCVIG LNKDLKMPKV QYKSNCKPST FAYPPPLEVP KEKEKEKVST AVLSITAKAK
KKEKEKEKEK KEEEKMEVDE TEKKDEKEKK KEPEPNFQLL DNPARVMPAQ LKVLTMTESC
RYQPFKPLSI GGIIILKDTS EDMEELVEPV AAHGPKIEEE EQEPEPPEPF EYIDD
