PSMF1_ARATH
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 25-MAY-2022, entry version 111.
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}.
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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 PRIDE; 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; PTHR13266; 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
