PSMD2_BOVIN
ID PSMD2_BOVIN Reviewed; 908 AA.
AC P56701; A7E3R5; Q2HJE3; Q9TRA7;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 2;
DE AltName: Full=26S proteasome regulatory subunit RPN1;
DE AltName: Full=26S proteasome regulatory subunit S2;
DE AltName: Full=26S proteasome subunit p97;
DE AltName: Full=Tumor necrosis factor type 1 receptor-associated protein 2;
GN Name=PSMD2; Synonyms=TRAP2;
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] OF 2-908.
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 9-26; 51-66; 98-105; 142-153; 169-189 AND 432-442.
RX PubMed=8774743; DOI=10.1111/j.1432-1033.1996.0912u.x;
RA Tsurumi C., Shimizu Y., Saeki M., Kato S., DeMartino G.N., Slaughter C.A.,
RA Fujimuro M., Yokosawa H., Yamasaki M., Hendil K.B., Toh-e A., Tanahashi N.,
RA Tanaka K.;
RT "cDNA cloning and functional analysis of the p97 subunit of the 26S
RT proteasome, a polypeptide identical to the type-1 tumor-necrosis-factor-
RT receptor-associated protein-2/55.11.";
RL Eur. J. Biochem. 239:912-921(1996).
RN [4]
RP PROTEIN SEQUENCE OF 9-26.
RX PubMed=8063704; DOI=10.1016/s0021-9258(17)31904-x;
RA DeMartino G.N., Moomaw C.R., Zagnitko O.P., Proske R.J., Chu-Ping M.,
RA Afendis S.J., Swaffield J.C., Slaughter C.A.;
RT "PA700, an ATP-dependent activator of the 20 S proteasome, is an ATPase
RT containing multiple members of a nucleotide-binding protein family.";
RL J. Biol. Chem. 269:20878-20884(1994).
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; BT030686; ABS45002.1; -; mRNA.
DR EMBL; BC105524; AAI05525.1; -; mRNA.
DR RefSeq; NP_001094667.1; NM_001101197.1.
DR AlphaFoldDB; P56701; -.
DR SMR; P56701; -.
DR BioGRID; 196351; 1.
DR STRING; 9913.ENSBTAP00000007436; -.
DR PaxDb; P56701; -.
DR PeptideAtlas; P56701; -.
DR PRIDE; P56701; -.
DR Ensembl; ENSBTAT00000007436; ENSBTAP00000007436; ENSBTAG00000005660.
DR GeneID; 539784; -.
DR KEGG; bta:539784; -.
DR CTD; 5708; -.
DR VEuPathDB; HostDB:ENSBTAG00000005660; -.
DR VGNC; VGNC:33466; PSMD2.
DR eggNOG; KOG2005; Eukaryota.
DR GeneTree; ENSGT00940000153386; -.
DR HOGENOM; CLU_008705_1_0_1; -.
DR InParanoid; P56701; -.
DR OMA; KTVYKHM; -.
DR OrthoDB; 229956at2759; -.
DR TreeFam; TF105739; -.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000005660; Expressed in granulosa cell and 105 other tissues.
DR ExpressionAtlas; P56701; baseline and differential.
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; 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 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Phosphoprotein; Proteasome;
KW Reference proteome; Repeat.
FT CHAIN 1..908
FT /note="26S proteasome non-ATPase regulatory subunit 2"
FT /id="PRO_0000173809"
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 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; 100258 MW; 45775EF917B610A0 CRC64;
MEEGGRDKAP LQPQQPPATS PGSGDEKPSG KERRDAGDKD KEQELSEEDK QLQDELEMLV
ERLGEKDTSL YRPALEELRR QIRSSTTSMT SVPKPLKFLR PHYGKLKEIY ENMAPGENKR
FAADIISVLA MTMSGERECL KYRLVGSQEE LASWGHEYVR HLAGEVAKEW QELDDAEKTQ
REPLLTLVKE IVPYNMAHNA 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
