PX11B_ARATH
ID PX11B_ARATH Reviewed; 227 AA.
AC Q9STY0;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Peroxisomal membrane protein 11B;
DE AltName: Full=Peroxin-11B;
DE Short=AtPEX11b;
GN Name=PEX11B; Synonyms=PEX11-4; OrderedLocusNames=At3g47430;
GN ORFNames=T21L8.180;
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 roots, leaves and developing siliques.
CC {ECO:0000269|PubMed:16636080, ECO:0000269|PubMed:17220199}.
CC -!- INDUCTION: In seedlings by transition from dark to light. Up-regulated
CC during senescence. {ECO:0000269|PubMed:17220199}.
CC -!- SIMILARITY: Belongs to the peroxin-11 family. {ECO:0000305}.
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DR EMBL; AJ520107; CAD58678.1; -; mRNA.
DR EMBL; AL096860; CAB51215.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78280.1; -; Genomic_DNA.
DR EMBL; BT002033; AAN72044.1; -; mRNA.
DR EMBL; BT006271; AAP13379.1; -; mRNA.
DR PIR; T12998; T12998.
DR RefSeq; NP_190327.1; NM_114611.4.
DR AlphaFoldDB; Q9STY0; -.
DR SMR; Q9STY0; -.
DR BioGRID; 9217; 5.
DR IntAct; Q9STY0; 4.
DR STRING; 3702.AT3G47430.1; -.
DR iPTMnet; Q9STY0; -.
DR PaxDb; Q9STY0; -.
DR PRIDE; Q9STY0; -.
DR ProteomicsDB; 226134; -.
DR EnsemblPlants; AT3G47430.1; AT3G47430.1; AT3G47430.
DR GeneID; 823897; -.
DR Gramene; AT3G47430.1; AT3G47430.1; AT3G47430.
DR KEGG; ath:AT3G47430; -.
DR Araport; AT3G47430; -.
DR TAIR; locus:2099590; AT3G47430.
DR eggNOG; KOG4186; Eukaryota.
DR HOGENOM; CLU_080291_0_0_1; -.
DR InParanoid; Q9STY0; -.
DR OMA; LVHWHVE; -.
DR OrthoDB; 1394894at2759; -.
DR PhylomeDB; Q9STY0; -.
DR PRO; PR:Q9STY0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9STY0; baseline and differential.
DR Genevisible; Q9STY0; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005779; C:integral component of peroxisomal membrane; IEA:InterPro.
DR GO; GO:0005778; C:peroxisomal membrane; IDA:TAIR.
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..227
FT /note="Peroxisomal membrane protein 11B"
FT /id="PRO_0000330296"
FT TOPO_DOM 1..85
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16636080"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107..201
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:16636080"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..227
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16636080"
SQ SEQUENCE 227 AA; 25598 MW; FCDFB3F651B5D259 CRC64;
MSLDTVDKLV VFLAKRDGID KLVKTFQYVA KLACWHVEAT RPEAADRFKK WEVASGLSRK
AFRTGRSLTG FNALRRNPGA TPMIRFLAVL ANSGEMVYFF FDHFLWLSRI GSIDAKLAKK
MSFISAFGES FGYTFFIIID CIFIKQRLKS LKKLQHSTDE PKEEIGAKIS EIRGDIVMRL
MGISANVADL LIALAEIHPN PFCNHTITLG ISGLVSAWAG WYRNWPS
