PX11D_ARATH
ID PX11D_ARATH Reviewed; 236 AA.
AC O80845; Q93XZ4;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Peroxisomal membrane protein 11D;
DE AltName: Full=Peroxin-11D;
DE Short=AtPEX11d;
GN Name=PEX11D; OrderedLocusNames=At2g45740; ORFNames=F4I18.28;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 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 FUNCTION, SUBUNIT, INTERACTION WITH FIS1B, AND SUBCELLULAR LOCATION.
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).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-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: Involved in peroxisomal proliferation. Promotes peroxisomal
CC duplication, aggregation or elongation without fission.
CC {ECO:0000269|PubMed:16636080, ECO:0000269|PubMed:17220199,
CC ECO:0000269|PubMed:18539750}.
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:18539750, ECO:0000269|PubMed:20179140}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:17220199,
CC ECO:0000269|PubMed:18539750, ECO:0000269|PubMed:20179140}.
CC -!- TISSUE SPECIFICITY: Expressed in developing siliques.
CC {ECO:0000269|PubMed:16636080, ECO:0000269|PubMed:17220199}.
CC -!- INDUCTION: Up-regulated during senescence.
CC {ECO:0000269|PubMed:17220199}.
CC -!- SIMILARITY: Belongs to the peroxin-11 family. {ECO:0000305}.
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DR EMBL; AC004665; AAC28551.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC10594.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10595.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10596.1; -; Genomic_DNA.
DR EMBL; AY054520; AAK96711.1; -; mRNA.
DR EMBL; AY084943; AAM61504.1; -; mRNA.
DR PIR; T02473; T02473.
DR RefSeq; NP_001031544.1; NM_001036467.3.
DR RefSeq; NP_566055.1; NM_130137.6.
DR RefSeq; NP_850441.1; NM_180110.5.
DR AlphaFoldDB; O80845; -.
DR BioGRID; 4518; 1.
DR STRING; 3702.AT2G45740.1; -.
DR iPTMnet; O80845; -.
DR PaxDb; O80845; -.
DR PRIDE; O80845; -.
DR ProteomicsDB; 226023; -.
DR EnsemblPlants; AT2G45740.1; AT2G45740.1; AT2G45740.
DR EnsemblPlants; AT2G45740.2; AT2G45740.2; AT2G45740.
DR EnsemblPlants; AT2G45740.3; AT2G45740.3; AT2G45740.
DR GeneID; 819182; -.
DR Gramene; AT2G45740.1; AT2G45740.1; AT2G45740.
DR Gramene; AT2G45740.2; AT2G45740.2; AT2G45740.
DR Gramene; AT2G45740.3; AT2G45740.3; AT2G45740.
DR KEGG; ath:AT2G45740; -.
DR Araport; AT2G45740; -.
DR TAIR; locus:2050694; AT2G45740.
DR eggNOG; KOG4186; Eukaryota.
DR HOGENOM; CLU_075417_0_0_1; -.
DR InParanoid; O80845; -.
DR OMA; FCWMAGT; -.
DR OrthoDB; 1394894at2759; -.
DR PhylomeDB; O80845; -.
DR PRO; PR:O80845; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80845; baseline and differential.
DR Genevisible; O80845; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
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: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 Acetylation; Membrane; Peroxisome; Peroxisome biogenesis;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..236
FT /note="Peroxisomal membrane protein 11D"
FT /id="PRO_0000330298"
FT TOPO_DOM 2..92
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16636080"
FT TRANSMEM 93..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 110..207
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:16636080"
FT TRANSMEM 208..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 228..236
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16636080"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 236 AA; 25944 MW; 102FAE6A197A5378 CRC64;
MGTTLDVSRA ELALVVMYLN KAEARDKLCR AIQYGSKFLS GGQPGTAQNV DKSTSLARKV
FRLFKFVNDL HGLISPVPKG TPLPLVLLGK SKNALLSTFL FLDQIVWLGR SGIYKNKERA
ELLGRISLFC WMGSSVCTTL VEVGEMGRLS SSMKKIEKGL KNGNKYQDED YRAKLKKSNE
RSLALIKSAM DIVVAAGLLQ LAPTKITPRV TGAFGFITSI ISCYQLLPTR PKIKTP
