SEM11_ARATH
ID SEM11_ARATH Reviewed; 74 AA.
AC Q9XIR8;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Protein DELETION OF SUV3 SUPPRESSOR 1(I) {ECO:0000303|PubMed:16415210};
DE Short=AtDSS1(I) {ECO:0000303|PubMed:16415210};
DE AltName: Full=Probable 26S proteasome complex subunit sem1-1;
GN Name=DSS1(I) {ECO:0000303|PubMed:16415210};
GN OrderedLocusNames=At1g64750 {ECO:0000312|Araport:AT1G64750};
GN ORFNames=F13O11.6 {ECO:0000312|EMBL:AAD38250.1};
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 [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION, AND INTERACTION WITH BRCA2A AND BRCA2B.
RX PubMed=16415210; DOI=10.1104/pp.105.075838;
RA Dray E., Siaud N., Dubois E., Doutriaux M.P.;
RT "Interaction between Arabidopsis Brca2 and its partners Rad51, Dmc1, and
RT Dss1.";
RL Plant Physiol. 140:1059-1069(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [7]
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: Subunit of the 26S proteasome which plays a role in
CC ubiquitin-dependent proteolysis. {ECO:0000250|UniProtKB:P60896}.
CC -!- SUBUNIT: Part of the 26S proteasome (By similarity). Interacts with
CC BRCA2A and BRCA2B (PubMed:16415210). Interacts with UCH1 and UCH2
CC (PubMed:22951400). Can form a tripartite complex with both RAD51 and
CC BRCA2B or both DMC1 and BRCA2B (PubMed:16415210).
CC {ECO:0000250|UniProtKB:P60896, ECO:0000269|PubMed:16415210,
CC ECO:0000269|PubMed:22951400}.
CC -!- INTERACTION:
CC Q9XIR8; Q7Y1C5: BRCA2A; NbExp=2; IntAct=EBI-931045, EBI-307680;
CC Q9XIR8; Q7Y1C4: BRCA2B; NbExp=2; IntAct=EBI-931045, EBI-307707;
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=Q9XIR8-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the DSS1/SEM1 family. {ECO:0000305}.
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DR EMBL; AC006193; AAD38250.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34280.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34281.1; -; Genomic_DNA.
DR EMBL; AY065373; AAL38814.1; -; mRNA.
DR EMBL; AY096483; AAM20123.1; -; mRNA.
DR EMBL; AY085437; AAM62664.1; -; mRNA.
DR PIR; F96670; F96670.
DR RefSeq; NP_564839.1; NM_105149.4. [Q9XIR8-1]
DR RefSeq; NP_974090.1; NM_202361.1. [Q9XIR8-1]
DR AlphaFoldDB; Q9XIR8; -.
DR BioGRID; 28004; 4.
DR IntAct; Q9XIR8; 6.
DR iPTMnet; Q9XIR8; -.
DR PRIDE; Q9XIR8; -.
DR EnsemblPlants; AT1G64750.1; AT1G64750.1; AT1G64750. [Q9XIR8-1]
DR EnsemblPlants; AT1G64750.2; AT1G64750.2; AT1G64750. [Q9XIR8-1]
DR GeneID; 842783; -.
DR Gramene; AT1G64750.1; AT1G64750.1; AT1G64750. [Q9XIR8-1]
DR Gramene; AT1G64750.2; AT1G64750.2; AT1G64750. [Q9XIR8-1]
DR KEGG; ath:AT1G64750; -.
DR Araport; AT1G64750; -.
DR HOGENOM; CLU_141774_1_1_1; -.
DR InParanoid; Q9XIR8; -.
DR OMA; EDWVENE; -.
DR PhylomeDB; Q9XIR8; -.
DR PRO; PR:Q9XIR8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9XIR8; baseline and differential.
DR Genevisible; Q9XIR8; AT.
DR GO; GO:0000502; C:proteasome complex; IBA:GO_Central.
DR GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IEA:InterPro.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0006406; P:mRNA export from nucleus; IEA:InterPro.
DR GO; GO:0043248; P:proteasome assembly; IEA:InterPro.
DR InterPro; IPR007834; DSS1_SEM1.
DR PANTHER; PTHR16771; PTHR16771; 1.
DR Pfam; PF05160; DSS1_SEM1; 1.
DR SMART; SM01385; DSS1_SEM1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Proteasome; Reference proteome.
FT CHAIN 1..74
FT /note="Protein DELETION OF SUV3 SUPPRESSOR 1(I)"
FT /id="PRO_0000122965"
FT REGION 35..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 74 AA; 8859 MW; F76AAF00BEE8818A CRC64;
MAAEPKAATA EVVKMDLFED DDEFEEFEIN EDWLEKEEVK EVSQQWEDDW DDDDVNDDFS
RQLRKELENG TDKK
