ID   SEM12_ARATH             Reviewed;          73 AA.
AC   Q9FL96; Q8LD17;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Protein DSS1 HOMOLOG ON CHROMOSOME V {ECO:0000303|PubMed:16415210};
DE            Short=AtDSS1(V) {ECO:0000303|PubMed:16415210};
DE   AltName: Full=Probable 26S proteasome complex subunit sem1-2;
GN   Name=DSS1(V) {ECO:0000303|PubMed:16415210};
GN   OrderedLocusNames=At5g45010 {ECO:0000312|Araport:AT5G45010};
GN   ORFNames=K21C13.20 {ECO:0000312|EMBL:BAB10884.1};
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=9679202; DOI=10.1093/dnares/5.2.131;
RA   Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT   features of the regions of 1,381,565 bp covered by twenty one physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:131-145(1998).
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 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   INTERACTION WITH EER5.
RX   PubMed=19843313; DOI=10.1111/j.1365-313x.2009.04048.x;
RA   Lu Q., Tang X., Tian G., Wang F., Liu K., Nguyen V., Kohalmi S.E.,
RA   Keller W.A., Tsang E.W., Harada J.J., Rothstein S.J., Cui Y.;
RT   "Arabidopsis homolog of the yeast TREX-2 mRNA export complex: components
RT   and anchoring nucleoporin.";
RL   Plant J. 61:259-270(2010).
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 (By similarity). Associates also with
CC       the TREX-2 complex that is required for transcription-coupled mRNA
CC       export (PubMed:19843313). {ECO:0000250|UniProtKB:P60896,
CC       ECO:0000269|PubMed:19843313}.
CC   -!- SUBUNIT: Part of the 26S proteasome (By similarity). Interacts with
CC       BRCA2B (PubMed:16415210). Interacts with EER5 (PubMed:19843313).
CC       Interacts with UCH1 and UCH2 (PubMed:22951400).
CC       {ECO:0000250|UniProtKB:P60896, ECO:0000269|PubMed:16415210,
CC       ECO:0000269|PubMed:19843313, ECO:0000269|PubMed:22951400}.
CC   -!- INTERACTION:
CC       Q9FL96; Q7Y1C4: BRCA2B; NbExp=2; IntAct=EBI-931034, EBI-307707;
CC   -!- SIMILARITY: Belongs to the DSS1/SEM1 family. {ECO:0000305}.
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DR   EMBL; AB010693; BAB10884.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED95188.1; -; Genomic_DNA.
DR   EMBL; AY063839; AAL36195.1; -; mRNA.
DR   EMBL; AY091311; AAM14250.1; -; mRNA.
DR   EMBL; AY086259; AAM64332.1; -; mRNA.
DR   RefSeq; NP_199314.1; NM_123869.4.
DR   AlphaFoldDB; Q9FL96; -.
DR   SMR; Q9FL96; -.
DR   BioGRID; 19781; 6.
DR   IntAct; Q9FL96; 5.
DR   STRING; 3702.AT5G45010.1; -.
DR   iPTMnet; Q9FL96; -.
DR   PaxDb; Q9FL96; -.
DR   PRIDE; Q9FL96; -.
DR   EnsemblPlants; AT5G45010.1; AT5G45010.1; AT5G45010.
DR   GeneID; 834532; -.
DR   Gramene; AT5G45010.1; AT5G45010.1; AT5G45010.
DR   KEGG; ath:AT5G45010; -.
DR   Araport; AT5G45010; -.
DR   TAIR; locus:2155392; AT5G45010.
DR   eggNOG; KOG4764; Eukaryota.
DR   HOGENOM; CLU_141774_1_1_1; -.
DR   InParanoid; Q9FL96; -.
DR   OMA; KFPAEDW; -.
DR   PhylomeDB; Q9FL96; -.
DR   PRO; PR:Q9FL96; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FL96; baseline and differential.
DR   Genevisible; Q9FL96; 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   GO; GO:0042542; P:response to hydrogen peroxide; IEP:TAIR.
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   Proteasome; Reference proteome.
FT   CHAIN           1..73
FT                   /note="Protein DSS1 HOMOLOG ON CHROMOSOME V"
FT                   /id="PRO_0000122966"
FT   CONFLICT        21
FT                   /note="D -> G (in Ref. 4; AAM64332)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   73 AA;  8698 MW;  1546920B05D6FB0C CRC64;
     MAAEPKAAVE VVKVDLFEDD DEFEEFEINE DWLEKEEVKE VSLQWEDDWD DDDVSDDFSR
     QLKKELENAS EKK