PSD1B_ARATH
ID PSD1B_ARATH Reviewed; 1001 AA.
AC Q9MAT0; Q6XBM5;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 147.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 1 homolog B;
DE AltName: Full=26S proteasome regulatory subunit RPN2b;
DE Short=AtRPN2b;
DE AltName: Full=26S proteasome regulatory subunit S1 homolog B;
GN Name=RPN2B; OrderedLocusNames=At1g04810; ORFNames=F13M7.20;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-996, SUBUNIT, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=cv. Columbia;
RX PubMed=14623884; DOI=10.1074/jbc.m311977200;
RA Yang P., Fu H., Walker J., Papa C.M., Smalle J., Ju Y.-M., Vierstra R.D.;
RT "Purification of the Arabidopsis 26 S proteasome: biochemical and molecular
RT analyses revealed the presence of multiple isoforms.";
RL J. Biol. Chem. 279:6401-6413(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, CHARACTERIZATION OF THE 26S PROTEASOME
RP COMPLEX, SUBUNIT, UBIQUITINATION AT LYS-166, AND CLEAVAGE OF INITIATOR
RP METHIONINE.
RX PubMed=20516081; DOI=10.1074/jbc.m110.136622;
RA Book A.J., Gladman N.P., Lee S.S., Scalf M., Smith L.M., Vierstra R.D.;
RT "Affinity purification of the Arabidopsis 26 S proteasome reveals a diverse
RT array of plant proteolytic complexes.";
RL J. Biol. Chem. 285:25554-25569(2010).
CC -!- FUNCTION: Acts as a regulatory subunit of the 26 proteasome which is
CC involved in the ATP-dependent degradation of ubiquitinated proteins.
CC {ECO:0000250}.
CC -!- SUBUNIT: Component of the 19S regulatory particle (RP/PA700) base
CC subcomplex of the 26S proteasome. The 26S proteasome is composed of a
CC core protease (CP), known as the 20S proteasome, capped at one or both
CC ends by the 19S regulatory particle (RP/PA700). The RP/PA700 complex is
CC composed of at least 17 different subunits in two subcomplexes, the
CC base and the lid, which form the portions proximal and distal to the
CC 20S proteolytic core, respectively. {ECO:0000269|PubMed:14623884,
CC ECO:0000269|PubMed:20516081}.
CC -!- SIMILARITY: Belongs to the proteasome subunit S1 family. {ECO:0000305}.
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DR EMBL; AC004809; AAF40455.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27746.1; -; Genomic_DNA.
DR EMBL; BT004007; AAO42045.1; -; mRNA.
DR EMBL; AY242527; AAP73043.1; -; mRNA.
DR PIR; C86181; C86181.
DR RefSeq; NP_171973.1; NM_100359.3.
DR AlphaFoldDB; Q9MAT0; -.
DR SMR; Q9MAT0; -.
DR BioGRID; 24644; 103.
DR IntAct; Q9MAT0; 7.
DR STRING; 3702.AT1G04810.1; -.
DR iPTMnet; Q9MAT0; -.
DR PaxDb; Q9MAT0; -.
DR PRIDE; Q9MAT0; -.
DR ProMEX; Q9MAT0; -.
DR ProteomicsDB; 226352; -.
DR EnsemblPlants; AT1G04810.1; AT1G04810.1; AT1G04810.
DR GeneID; 839409; -.
DR Gramene; AT1G04810.1; AT1G04810.1; AT1G04810.
DR KEGG; ath:AT1G04810; -.
DR Araport; AT1G04810; -.
DR TAIR; locus:2010672; AT1G04810.
DR eggNOG; KOG2062; Eukaryota.
DR HOGENOM; CLU_002323_0_0_1; -.
DR InParanoid; Q9MAT0; -.
DR OMA; DLRPHEP; -.
DR OrthoDB; 235012at2759; -.
DR PhylomeDB; Q9MAT0; -.
DR PRO; PR:Q9MAT0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9MAT0; baseline and differential.
DR Genevisible; Q9MAT0; AT.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000502; C:proteasome complex; IDA:TAIR.
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:0030163; P:protein catabolic process; TAS:TAIR.
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; IPR040623; RPN2_C.
DR Pfam; PF01851; PC_rep; 1.
DR Pfam; PF18004; RPN2_C; 1.
DR PIRSF; PIRSF015947; 26S_Psome_Rpn2; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Acetylation; Isopeptide bond; Phosphoprotein; Proteasome;
KW Reference proteome; Repeat; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O48844,
FT ECO:0000305|PubMed:20516081"
FT CHAIN 2..1001
FT /note="26S proteasome non-ATPase regulatory subunit 1
FT homolog B"
FT /id="PRO_0000423177"
FT REPEAT 412..447
FT /note="PC 1"
FT REPEAT 452..485
FT /note="PC 2"
FT REPEAT 487..521
FT /note="PC 3"
FT REPEAT 522..555
FT /note="PC 4"
FT REPEAT 557..590
FT /note="PC 5"
FT REPEAT 591..626
FT /note="PC 6"
FT REPEAT 627..659
FT /note="PC 7"
FT REPEAT 661..695
FT /note="PC 8"
FT REPEAT 696..736
FT /note="PC 9"
FT REPEAT 739..771
FT /note="PC 10"
FT REGION 853..896
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 954..1001
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O48844"
FT MOD_RES 889
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48844"
FT CROSSLNK 166
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:20516081"
SQ SEQUENCE 1001 AA; 108866 MW; 2272E859EBCCD8B8 CRC64;
MAAAMVSSAG GLLAMLNEPH PSLKLHALSY LIRLVDQFWP EISTSVPIIE SLYEDEEFDQ
HQRQLAALLA SKVFYYLGEL NDSLSYALGA GSLFDVSEDS DYIHTLLSKA IDEYAILRSK
AVESSEVVEI DPRLVAIVER MLDKCITDGK YQQAMGIAIE CRRLDKLEEA IIKSENVQGT
LSYCINVSHS FVNQREYRHE VLRLLVNVYQ KLASPDYLSI CQCLMFLDEP QGVASILEKL
LRSENKDDAL LAFQISFDLV QNEHQAFLMS VRDRLPAPKT RPVEAIQAVE TSTAQNENTA
GDVQMADETP SQTIVHETDP VDAVYAERLT KAKGILSGET SIQLTLQFLY SHNKSDLLIL
KTIKQSVEMR NSVCHSATIY ANAIMHAGTT VDTFLRENLD WLSRATNWAK FSATAGLGVI
HRGHLQQGRS LMAPYLPQGG AGGGGSPYSE GGALYALGLI HANHGEGIKQ FLRDSLRSTS
VEVIQHGACL GLGLAALGTA DEDIYDDIKS VLYTDSAVAG EAAGISMGLL LVGTATDKAS
EMLAYAHETQ HEKIIRGLAL GIALTVYGRE EGADTLIEQM TRDQDPIIRY GGMYALALAY
SGTANNKAIR QLLHFAVSDV SDDVRRTAVL ALGFVLYSDP EQTPRIVSLL SESYNPHVRY
GAALAVGISC AGTGLSEAIS LLEPLTSDVV DFVRQGALIA MAMVMVQISE ASDSRVGAFR
RQLEKIILDK HEDTMSKMGA ILASGILDAG GRNVTIRLLS KTKHDKVTAV IGLTVFSQFW
YWYPLIYFIS LAFSPTAFIG LNYDLKVPKF EFMSHAKPSL FEYPKPTTVA TANTAAKLPT
AVLSTSAKAK AKAKKEAEQK AKAENSGNEA GKANAASDEK EAESMQVDST ATTVEKKVEP
EATFEILVNP ARVVPSQEKY IKLMEDSRYV PMKLAPSGFV LLRDLRPHEP EVLSLTDAPT
STASPAVGAE AAGQAQQAAT TSAMAIDDEP QPPQAFEYAS P
