PSA1B_ARATH
ID PSA1B_ARATH Reviewed; 277 AA.
AC O23712;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 2.
DT 25-MAY-2022, entry version 170.
DE RecName: Full=Proteasome subunit alpha type-1-B;
DE AltName: Full=20S proteasome alpha subunit F-2;
DE AltName: Full=Proteasome component 2B;
DE AltName: Full=Proteasome subunit alpha type-6;
GN Name=PAF2; Synonyms=PRC2B, PRS1; OrderedLocusNames=At1g47250;
GN ORFNames=F8G22.3;
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 [MRNA], GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=9611183; DOI=10.1093/genetics/149.2.677;
RA Fu H., Doelling J.H., Arendt C.S., Hochstrasser M., Vierstra R.D.;
RT "Molecular organization of the 20S proteasome gene family from Arabidopsis
RT thaliana.";
RL Genetics 149:677-692(1998).
RN [2]
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-277.
RC STRAIN=cv. Columbia;
RX PubMed=9373170; DOI=10.1016/s0014-5793(97)01228-3;
RA Parmentier Y., Bouchez D., Fleck J., Genschik P.;
RT "The 20S proteasome gene family in Arabidopsis thaliana.";
RL FEBS Lett. 416:281-285(1997).
RN [6]
RP SUBUNIT.
RX PubMed=10363660; DOI=10.1023/a:1006926322501;
RA Fu H., Girod P.-A., Doelling J.H., van Nocker S., Hochstrasser M.,
RA Finley D., Vierstra R.D.;
RT "Structure and functional analyses of the 26S proteasome subunits from
RT plants.";
RL Mol. Biol. Rep. 26:137-146(1999).
RN [7]
RP SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
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 [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19453443; DOI=10.1111/j.1365-313x.2009.03914.x;
RA Sung D.-Y., Kim T.-H., Komives E.A., Mendoza-Cozatl D.G., Schroeder J.I.;
RT "ARS5 is a component of the 26S proteasome complex, and negatively
RT regulates thiol biosynthesis and arsenic tolerance in Arabidopsis.";
RL Plant J. 59:802-812(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, CHARACTERIZATION OF THE 26S PROTEASOME
RP COMPLEX, SUBUNIT, AND ACETYLATION AT MET-1.
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: The proteasome is a multicatalytic proteinase complex which
CC is characterized by its ability to cleave peptides with Arg, Phe, Tyr,
CC Leu, and Glu adjacent to the leaving group at neutral or slightly basic
CC pH. The proteasome has an ATP-dependent proteolytic activity. May play
CC a role in thiol biosynthesis and arsenic tolerance in association with
CC PAF1/ARS5. {ECO:0000269|PubMed:19453443}.
CC -!- SUBUNIT: Component of the 20S core complex of the 26S proteasome. The
CC 26S proteasome is composed of a core protease (CP), known as the 20S
CC proteasome, capped at one or both ends by the 19S regulatory particle
CC (RP/PA700). The 20S proteasome core is composed of 28 subunits that are
CC arranged in four stacked rings, resulting in a barrel-shaped structure.
CC The two end rings are each formed by seven alpha subunits, and the two
CC central rings are each formed by seven beta subunits. The catalytic
CC chamber with the active sites is on the inside of the barrel.
CC {ECO:0000269|PubMed:10363660, ECO:0000269|PubMed:14623884,
CC ECO:0000269|PubMed:20516081}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Do not show arsenic tolerance phenotype.
CC {ECO:0000269|PubMed:19453443}.
CC -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|PROSITE-
CC ProRule:PRU00808}.
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DR EMBL; AF043527; AAC32063.1; -; mRNA.
DR EMBL; AC079677; AAG52642.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32143.1; -; Genomic_DNA.
DR EMBL; AY057649; AAL15280.1; -; mRNA.
DR EMBL; AY141996; AAM98260.1; -; mRNA.
DR EMBL; Y13182; CAA73625.1; -; mRNA.
DR PIR; T51975; T51975.
DR RefSeq; NP_175158.1; NM_103619.5.
DR AlphaFoldDB; O23712; -.
DR SMR; O23712; -.
DR BioGRID; 26353; 69.
DR IntAct; O23712; 1.
DR STRING; 3702.AT1G47250.1; -.
DR MEROPS; T01.976; -.
DR iPTMnet; O23712; -.
DR PaxDb; O23712; -.
DR PRIDE; O23712; -.
DR ProteomicsDB; 226303; -.
DR EnsemblPlants; AT1G47250.1; AT1G47250.1; AT1G47250.
DR GeneID; 841128; -.
DR Gramene; AT1G47250.1; AT1G47250.1; AT1G47250.
DR KEGG; ath:AT1G47250; -.
DR Araport; AT1G47250; -.
DR TAIR; locus:2036746; AT1G47250.
DR eggNOG; KOG0863; Eukaryota.
DR HOGENOM; CLU_035750_8_0_1; -.
DR InParanoid; O23712; -.
DR OMA; NDEIICH; -.
DR OrthoDB; 1222564at2759; -.
DR PhylomeDB; O23712; -.
DR PRO; PR:O23712; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O23712; baseline and differential.
DR Genevisible; O23712; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0000502; C:proteasome complex; IDA:TAIR.
DR GO; GO:0005839; C:proteasome core complex; IBA:GO_Central.
DR GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; ISS:UniProtKB.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd03749; proteasome_alpha_type_1; 1.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR023332; Proteasome_alpha-type.
DR InterPro; IPR035144; Proteasome_alpha1.
DR InterPro; IPR000426; Proteasome_asu_N.
DR InterPro; IPR001353; Proteasome_sua/b.
DR PANTHER; PTHR11599:SF162; PTHR11599:SF162; 1.
DR Pfam; PF00227; Proteasome; 1.
DR Pfam; PF10584; Proteasome_A_N; 1.
DR SMART; SM00948; Proteasome_A_N; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR PROSITE; PS00388; PROTEASOME_ALPHA_1; 1.
DR PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Isopeptide bond; Nucleus; Proteasome;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..277
FT /note="Proteasome subunit alpha type-1-B"
FT /id="PRO_0000124073"
FT REGION 237..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:20516081"
FT CROSSLNK 51
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P34066"
SQ SEQUENCE 277 AA; 30410 MW; C5FBCE302217C521 CRC64;
MFRNQYDTDV TTWSPTGRLF QVEYAMEAVK QGSAAIGLRS RSHVVLACVN KAQSELSSHQ
RKIFKVDDHI GVAIAGLTAD GRVLSRYMRS ESINHSFTYE SPLPVGRLVV HLADKAQVCT
QRSWKRPYGV GLLVGGLDES GAHLYYNCPS GNYFEYQAFA IGSRSQAAKT YLERKFESFQ
ESSKEDLIKD AIMAIRETLQ GETLKSSLCT VSVLGVDEPF HFLDQESIQK VIDTFEKVPE
EEEDAGEGEA EPEAAPGAAG TGEQGGSGDQ DVAPMEI
