ID PSMF1_ARATH Reviewed; 302 AA. AC Q9M330; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 14-DEC-2022, entry version 112. DE RecName: Full=Probable proteasome inhibitor; GN OrderedLocusNames=At3g53970; ORFNames=F5K20_270; 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=11130713; DOI=10.1038/35048706; RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P., RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., RA Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."; RL Nature 408:820-822(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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). CC -!- FUNCTION: Could play an important role in control of proteasome CC function. Inhibits the hydrolysis of protein and peptide substrates by CC the 20S proteasome (By similarity). {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=1; CC Comment=A number of isoforms are produced. According to EST CC sequences.; CC Name=1; CC IsoId=Q9M330-1; Sequence=Displayed; CC -!- SIMILARITY: Belongs to the proteasome inhibitor PI31 family. CC {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; AL132960; CAB88359.1; -; Genomic_DNA. DR EMBL; CP002686; AEE79166.1; -; Genomic_DNA. DR EMBL; AY063998; AAL36354.1; -; mRNA. DR EMBL; AY117182; AAM51257.1; -; mRNA. DR PIR; T45937; T45937. DR RefSeq; NP_190965.1; NM_115257.6. [Q9M330-1] DR AlphaFoldDB; Q9M330; -. DR SMR; Q9M330; -. DR STRING; 3702.AT3G53970.1; -. DR iPTMnet; Q9M330; -. DR PaxDb; Q9M330; -. DR ProteomicsDB; 248903; -. [Q9M330-1] DR EnsemblPlants; AT3G53970.1; AT3G53970.1; AT3G53970. [Q9M330-1] DR GeneID; 824564; -. DR Gramene; AT3G53970.1; AT3G53970.1; AT3G53970. [Q9M330-1] DR KEGG; ath:AT3G53970; -. DR Araport; AT3G53970; -. DR TAIR; locus:2084510; AT3G53970. DR eggNOG; KOG4761; Eukaryota. DR HOGENOM; CLU_079501_0_0_1; -. DR InParanoid; Q9M330; -. DR OMA; NICVEPE; -. DR PhylomeDB; Q9M330; -. DR PRO; PR:Q9M330; -. DR Proteomes; UP000006548; Chromosome 3. DR ExpressionAtlas; Q9M330; baseline and differential. DR Genevisible; Q9M330; AT. DR GO; GO:0005829; C:cytosol; HDA:TAIR. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR. DR GO; GO:0005634; C:nucleus; IDA:TAIR. DR GO; GO:0005886; C:plasma membrane; IDA:TAIR. DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW. DR GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro. DR GO; GO:0070628; F:proteasome binding; IEA:InterPro. DR GO; GO:0071365; P:cellular response to auxin stimulus; IMP:TAIR. DR GO; GO:1901799; P:negative regulation of proteasomal protein catabolic process; IDA:TAIR. DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central. DR InterPro; IPR045128; PI31-like. DR InterPro; IPR021625; PI31_Prot_N. DR PANTHER; PTHR13266; PROTEASOME INHIBITOR; 1. DR Pfam; PF11566; PI31_Prot_N; 1. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Proteasome; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22223895" FT CHAIN 2..302 FT /note="Probable proteasome inhibitor" FT /id="PRO_0000220925" FT REGION 151..188 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 259..302 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:22223895" SQ SEQUENCE 302 AA; 32117 MW; 1DE8CFB5E55914E2 CRC64; MANSQTVMAM IRLARPPFRN NHDKVAFAIH SSFVASGYIL TATGRPAFAD EALSSSSQND VGIEGWNEFE GEYAFVYANP KKGSKKILVK CLAMDDKLLV DAIADGGAEP AHLEIKVGDY AEESNEGDYS AQFKNLDKLV TDLQSEIIDK LDGKPKPVAS RAQSSSETNE EPRYYDDTPN PLGPQIHPSG VVVPPIPGNG GYSDLFPGPG AGMYPGRGGF GDGSMLVGPT DPRFFPFGDG SDRPGFMGPP HPGMPPPGAR FDPYGPPGVP GFEPGRFTRQ PPRGPGGGHP DLEHFPGGSD FI //