位置:首页 > 蛋白库 > PSD3B_ARATH
PSD3B_ARATH
ID   PSD3B_ARATH             Reviewed;         487 AA.
AC   Q9LQR8; Q5XF45;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   25-MAY-2022, entry version 146.
DE   RecName: Full=26S proteasome non-ATPase regulatory subunit 3 homolog B {ECO:0000303|PubMed:14623884};
DE   AltName: Full=26S proteasome regulatory subunit RPN3b {ECO:0000303|PubMed:14623884};
DE            Short=AtRPN3b {ECO:0000303|PubMed:14623884};
DE   AltName: Full=26S proteasome regulatory subunit S3 homolog B;
GN   Name=RPN3B {ECO:0000303|PubMed:14623884};
GN   OrderedLocusNames=At1g75990 {ECO:0000312|Araport:AT1G75990};
GN   ORFNames=T4O12.21 {ECO:0000312|EMBL:AAF26768.2};
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   SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
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, AND SUBUNIT.
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).
RN   [6]
RP   INTERACTION WITH UCH1 AND UCH2.
RX   PubMed=22951400; DOI=10.4161/psb.21899;
RA   Tian G., Lu Q., Kohalmi S.E., Rothstein S.J., Cui Y.;
RT   "Evidence that the Arabidopsis Ubiquitin C-terminal Hydrolases 1 and 2
RT   associate with the 26S proteasome and the TREX-2 complex.";
RL   Plant Signal. Behav. 7:1415-1419(2012).
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|UniProtKB:O43242}.
CC   -!- SUBUNIT: Component of the 19S regulatory particle (RP/PA700) lid
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 (PubMed:14623884, PubMed:20516081).
CC       Interacts with UCH1 and UCH2 (PubMed:22951400).
CC       {ECO:0000269|PubMed:14623884, ECO:0000269|PubMed:20516081,
CC       ECO:0000269|PubMed:22951400}.
CC   -!- TISSUE SPECIFICITY: Preferentially expressed in flowers.
CC       {ECO:0000269|PubMed:14623884}.
CC   -!- SIMILARITY: Belongs to the proteasome subunit S3 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF26768.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AC007396; AAF26768.2; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE35783.1; -; Genomic_DNA.
DR   EMBL; AY057508; AAL09749.1; -; mRNA.
DR   EMBL; BT015771; AAU90061.1; -; mRNA.
DR   PIR; E96788; E96788.
DR   RefSeq; NP_177726.1; NM_106248.4.
DR   AlphaFoldDB; Q9LQR8; -.
DR   SMR; Q9LQR8; -.
DR   BioGRID; 29150; 97.
DR   IntAct; Q9LQR8; 6.
DR   STRING; 3702.AT1G75990.1; -.
DR   iPTMnet; Q9LQR8; -.
DR   PaxDb; Q9LQR8; -.
DR   PRIDE; Q9LQR8; -.
DR   ProteomicsDB; 226232; -.
DR   EnsemblPlants; AT1G75990.1; AT1G75990.1; AT1G75990.
DR   GeneID; 843931; -.
DR   Gramene; AT1G75990.1; AT1G75990.1; AT1G75990.
DR   KEGG; ath:AT1G75990; -.
DR   Araport; AT1G75990; -.
DR   TAIR; locus:2204385; AT1G75990.
DR   eggNOG; KOG2581; Eukaryota.
DR   HOGENOM; CLU_019858_1_0_1; -.
DR   InParanoid; Q9LQR8; -.
DR   OMA; AKRAMRY; -.
DR   OrthoDB; 836599at2759; -.
DR   PhylomeDB; Q9LQR8; -.
DR   PRO; PR:Q9LQR8; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9LQR8; baseline and differential.
DR   Genevisible; Q9LQR8; AT.
DR   GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR   GO; GO:0000502; C:proteasome complex; IDA:TAIR.
DR   GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IBA:GO_Central.
DR   GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR   GO; GO:0030163; P:protein catabolic process; TAS:TAIR.
DR   GO; GO:0042176; P:regulation of protein catabolic process; IEA:InterPro.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   InterPro; IPR013586; 26S_Psome_reg_C.
DR   InterPro; IPR000717; PCI_dom.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF01399; PCI; 1.
DR   Pfam; PF08375; Rpn3_C; 1.
DR   SMART; SM00088; PINT; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS50250; PCI; 1.
PE   1: Evidence at protein level;
KW   Proteasome; Reference proteome.
FT   CHAIN           1..487
FT                   /note="26S proteasome non-ATPase regulatory subunit 3
FT                   homolog B"
FT                   /id="PRO_0000173823"
FT   DOMAIN          239..420
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          452..487
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        452..476
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   487 AA;  55591 MW;  366216141CB5E22A CRC64;
     MTQDVEMKDN QTPTQSVVSA PTSTLQNLKE IAALIDTGSY TKEVRRIARA VRLTVGLRRK
     LTGSVISSFL DFALVPGSEA HTRLSSFVPK SDEHDMEVDT ASSNSQAPPK HLPAELEIYC
     YFIVLLFLID QKKYNEAKVC STASIARLKS VNRRTVDVIA SKLYFYYSLS YELTNDLAEI
     RSTLLALHHS ATLRHDELGQ ETLLNLLLRN YLHYNLYDQA EKLRSKAPRF EAHSNQQFCR
     YLFYLGKIRT IQLEYTDAKE SLLQAARKAP VASLGFRIQC NKWAIIVRLL LGEIPERSIF
     TQKGMEKTLR PYFELTNAVR IGDLELFGKI QEKFAKTFAE DRTHNLIVRL RHNVIRTGLR
     NISISYSRIS LQDVAQKLRL NSANPVADAE SIVAKAIRDG AIDATIDHKN GCMVSKETGD
     IYSTNEPQTA FNSRIAFCLN MHNEAVRALR FPPNTHREKE SEEKRREMKQ QEEELAKYMA
     EEDDDDF
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024