PX11A_ARATH
ID PX11A_ARATH Reviewed; 248 AA.
AC Q9FZF1; Q8LGI6;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Peroxisomal membrane protein 11A;
DE AltName: Full=Peroxin-11A;
DE Short=AtPEX11a;
GN Name=PEX11A; Synonyms=PEX11-3; OrderedLocusNames=At1g47750;
GN ORFNames=T2E6.18;
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=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 [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;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
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 [8]
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 [9]
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 [10]
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 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ520106; CAD58677.1; -; mRNA.
DR EMBL; AC012463; AAF99792.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32208.1; -; Genomic_DNA.
DR EMBL; BT024474; ABD19655.1; -; mRNA.
DR EMBL; AK227048; BAE99108.1; -; mRNA.
DR EMBL; AY084249; AAM60843.1; -; mRNA.
DR PIR; B96518; B96518.
DR RefSeq; NP_564514.1; NM_103668.3.
DR AlphaFoldDB; Q9FZF1; -.
DR SMR; Q9FZF1; -.
DR BioGRID; 26411; 1.
DR STRING; 3702.AT1G47750.1; -.
DR TCDB; 1.A.101.1.3; the peroxisomal pore-forming pex11 (pex11) family.
DR TCDB; 3.A.20.1.2; the peroxisomal protein importer (ppi) family.
DR iPTMnet; Q9FZF1; -.
DR PaxDb; Q9FZF1; -.
DR PRIDE; Q9FZF1; -.
DR ProteomicsDB; 226022; -.
DR EnsemblPlants; AT1G47750.1; AT1G47750.1; AT1G47750.
DR GeneID; 841186; -.
DR Gramene; AT1G47750.1; AT1G47750.1; AT1G47750.
DR KEGG; ath:AT1G47750; -.
DR Araport; AT1G47750; -.
DR TAIR; locus:2202430; AT1G47750.
DR eggNOG; KOG4186; Eukaryota.
DR HOGENOM; CLU_080291_0_0_1; -.
DR InParanoid; Q9FZF1; -.
DR OMA; SAWAEFI; -.
DR OrthoDB; 1394894at2759; -.
DR PhylomeDB; Q9FZF1; -.
DR PRO; PR:Q9FZF1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FZF1; baseline and differential.
DR Genevisible; Q9FZF1; AT.
DR GO; GO:0005779; C:integral component of peroxisomal membrane; IDA: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 Membrane; Peroxisome; Peroxisome biogenesis; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..248
FT /note="Peroxisomal membrane protein 11A"
FT /id="PRO_0000330295"
FT TOPO_DOM 1..97
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16636080"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..220
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:16636080"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 242..248
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CONFLICT 9
FT /note="I -> L (in Ref. 1; CAD58677 and 6; AAM60843)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 248 AA; 27677 MW; DE4AA8FED48304F0 CRC64;
MATKAPEKIT KPKDRDFLNH LETYLSKRDG VDKLLKISRY ATKIILASSL IPETRSIIPR
LKSFESSVGV SRKAFRLGKF VQDINALRSS RWDSNHELVL LIIAYGGEGL YYFVEQFIWL
TKSGLIDAKH SKWLQKISAW AELVGYVGSV SIKIRDLRKL NDEESCVAST IEISVSRGLA
CDGEDEKMKM IKEKKTLKVL SILQDLADGL MTIADIRDGK GVLSAPNVIS SAGLFSAIVS
THKNWISC
