PX11E_ARATH
ID PX11E_ARATH Reviewed; 231 AA.
AC Q84JW1; Q5QT11; Q9LEW9;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Peroxisomal membrane protein 11E;
DE AltName: Full=Peroxin-11E;
DE Short=AtPEX11e;
GN Name=PEX11E; Synonyms=PEX11-2; OrderedLocusNames=At3g61070;
GN ORFNames=T27I15.160;
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].
RC TISSUE=Seedling;
RA El Shami M., Baker A.;
RT "AtPEX11 and peroxisome proliferation in Arabidopsis thaliana.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [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 FUNCTION, TOPOLOGY, TISSUE SPECIFICITY, AND NOMENCLATURE.
RX PubMed=16636080; DOI=10.1242/jcs.02904;
RA Lingard M.J., Trelease R.N.;
RT "Five Arabidopsis peroxin 11 homologs individually promote peroxisome
RT elongation, duplication or aggregation.";
RL J. Cell Sci. 119:1961-1972(2006).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND GENE
RP FAMILY.
RX PubMed=17220199; DOI=10.1105/tpc.106.045831;
RA Orth T., Reumann S., Zhang X., Fan J., Wenzel D., Quan S., Hu J.;
RT "The PEROXIN11 protein family controls peroxisome proliferation in
RT Arabidopsis.";
RL Plant Cell 19:333-350(2007).
RN [7]
RP SUBUNIT, AND INTERACTION WITH FIS1B.
RX PubMed=18539750; DOI=10.1105/tpc.107.057679;
RA Lingard M.J., Gidda S.K., Bingham S., Rothstein S.J., Mullen R.T.,
RA Trelease R.N.;
RT "Arabidopsis PEROXIN11c-e, FISSION1b, and DYNAMIN-RELATED PROTEIN3A
RT cooperate in cell cycle-associated replication of peroxisomes.";
RL Plant Cell 20:1567-1585(2008).
RN [8]
RP INTERACTION WITH ARC5 AND FIS1B, SUBCELLULAR LOCATION, AND
RP SELF-INTERACTION.
RX PubMed=20179140; DOI=10.1105/tpc.109.071324;
RA Zhang X., Hu J.;
RT "The Arabidopsis chloroplast division protein DYNAMIN-RELATED PROTEIN5B
RT also mediates peroxisome division.";
RL Plant Cell 22:431-442(2010).
CC -!- FUNCTION: Involved in peroxisomal proliferation. Promotes peroxisomal
CC duplication, aggregation or elongation without fission.
CC {ECO:0000269|PubMed:16636080, ECO:0000269|PubMed:17220199}.
CC -!- SUBUNIT: Homooligomer. Interacts with ARC5 and FIS1B on peroxisomes.
CC {ECO:0000269|PubMed:18539750, ECO:0000269|PubMed:20179140}.
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|PubMed:17220199,
CC ECO:0000269|PubMed:20179140}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:17220199, ECO:0000269|PubMed:20179140}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves and developing siliques.
CC {ECO:0000269|PubMed:16636080, ECO:0000269|PubMed:17220199}.
CC -!- INDUCTION: Up-regulated during sensecence. Down-regulated in seedlings
CC by transition from dark to light. {ECO:0000269|PubMed:17220199}.
CC -!- MISCELLANEOUS: Can complement the yeast pex11 null mutant.
CC -!- SIMILARITY: Belongs to the peroxin-11 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB94143.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ520105; CAD58676.1; -; mRNA.
DR EMBL; AL358732; CAB94143.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE80148.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80149.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80150.1; -; Genomic_DNA.
DR EMBL; BT002962; AAO22773.1; -; mRNA.
DR EMBL; BT004439; AAO42433.1; -; mRNA.
DR PIR; T50528; T50528.
DR RefSeq; NP_001078322.1; NM_001084853.2.
DR RefSeq; NP_001190149.1; NM_001203220.1.
DR RefSeq; NP_191666.2; NM_115971.3.
DR AlphaFoldDB; Q84JW1; -.
DR BioGRID; 10593; 4.
DR STRING; 3702.AT3G61070.3; -.
DR SwissPalm; Q84JW1; -.
DR PaxDb; Q84JW1; -.
DR PRIDE; Q84JW1; -.
DR ProteomicsDB; 224821; -.
DR EnsemblPlants; AT3G61070.1; AT3G61070.1; AT3G61070.
DR EnsemblPlants; AT3G61070.2; AT3G61070.2; AT3G61070.
DR EnsemblPlants; AT3G61070.3; AT3G61070.3; AT3G61070.
DR GeneID; 825279; -.
DR Gramene; AT3G61070.1; AT3G61070.1; AT3G61070.
DR Gramene; AT3G61070.2; AT3G61070.2; AT3G61070.
DR Gramene; AT3G61070.3; AT3G61070.3; AT3G61070.
DR KEGG; ath:AT3G61070; -.
DR Araport; AT3G61070; -.
DR TAIR; locus:2101012; AT3G61070.
DR eggNOG; KOG4186; Eukaryota.
DR HOGENOM; CLU_075417_0_0_1; -.
DR InParanoid; Q84JW1; -.
DR OMA; RISFFSW; -.
DR OrthoDB; 1394894at2759; -.
DR PhylomeDB; Q84JW1; -.
DR PRO; PR:Q84JW1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q84JW1; baseline and differential.
DR Genevisible; Q84JW1; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005779; C:integral component of peroxisomal membrane; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005778; C:peroxisomal membrane; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0007623; P:circadian rhythm; IEP:TAIR.
DR GO; GO:0016559; P:peroxisome fission; IDA:UniProtKB.
DR GO; GO:0007031; P:peroxisome organization; IMP:TAIR.
DR GO; GO:0044375; P:regulation of peroxisome size; IDA:UniProtKB.
DR InterPro; IPR008733; PEX11.
DR Pfam; PF05648; PEX11; 1.
PE 1: Evidence at protein level;
KW Membrane; Peroxisome; Peroxisome biogenesis; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..231
FT /note="Peroxisomal membrane protein 11E"
FT /id="PRO_0000330299"
FT TOPO_DOM 1..91
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16636080"
FT TRANSMEM 92..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 109..202
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:16636080"
FT TRANSMEM 203..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..231
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16636080"
FT CONFLICT 230..231
FT /note="TP -> KS (in Ref. 1; CAD58676)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 231 AA; 25512 MW; 5B1D737E1F9AC4B7 CRC64;
MTTLDLTRAE LALIVLYLNK AEARDKICRA IQYGSKFLSG GQPGTAQTVD KNTSLARKVF
RLFKFVNDFH GLISPVPKGT PLPLVLLGKS KNALLSTFLF LDQIVWLGRS GIYKNKERTE
LLGRISLFCW LGSSVCTSAV EIGELGRLSS SMKKMEKELK ADDELYRAKL QKSNDRTLAL
IKSSMDIIVA IGLLQLAPKT ISPRVTGAFG FTTSLISCYQ LLPSRPKLKT P
