PX11C_ARATH
ID PX11C_ARATH Reviewed; 235 AA.
AC Q9LQ73; Q5QT12;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Peroxisomal membrane protein 11C;
DE AltName: Full=Peroxin-11C;
DE Short=AtPEX11c;
GN Name=PEX11C; Synonyms=PEX11-1; OrderedLocusNames=At1g01820;
GN ORFNames=T1N6.24;
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 STRAIN=cv. Columbia;
RA Yamaguchi K., Nishimura M.;
RT "Pex 11 homologue.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
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 [5]
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 [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 FUNCTION, 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 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:20179140}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:17220199, ECO:0000269|PubMed:20179140}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and developing siliques.
CC {ECO:0000269|PubMed:16636080, ECO:0000269|PubMed:17220199}.
CC -!- INDUCTION: Up-regulated during senescence.
CC {ECO:0000269|PubMed:17220199}.
CC -!- MISCELLANEOUS: Can complement the yeast pex11 null mutant.
CC -!- SIMILARITY: Belongs to the peroxin-11 family. {ECO:0000305}.
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DR EMBL; AB022861; BAD83578.1; -; mRNA.
DR EMBL; AJ520104; CAD58675.1; -; mRNA.
DR EMBL; AC009273; AAF78415.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27339.1; -; Genomic_DNA.
DR EMBL; AF332441; AAG48804.1; -; mRNA.
DR EMBL; AY064139; AAL36046.1; -; mRNA.
DR EMBL; AY097406; AAM19922.1; -; mRNA.
DR EMBL; AY086844; AAM63892.1; -; mRNA.
DR PIR; A86150; A86150.
DR RefSeq; NP_563636.1; NM_100065.5.
DR AlphaFoldDB; Q9LQ73; -.
DR BioGRID; 24492; 1.
DR STRING; 3702.AT1G01820.1; -.
DR iPTMnet; Q9LQ73; -.
DR PaxDb; Q9LQ73; -.
DR PRIDE; Q9LQ73; -.
DR ProteomicsDB; 226136; -.
DR EnsemblPlants; AT1G01820.1; AT1G01820.1; AT1G01820.
DR GeneID; 839257; -.
DR Gramene; AT1G01820.1; AT1G01820.1; AT1G01820.
DR KEGG; ath:AT1G01820; -.
DR Araport; AT1G01820; -.
DR TAIR; locus:2198150; AT1G01820.
DR eggNOG; KOG4186; Eukaryota.
DR HOGENOM; CLU_075417_0_0_1; -.
DR InParanoid; Q9LQ73; -.
DR OMA; QDGEYCA; -.
DR OrthoDB; 1394894at2759; -.
DR PhylomeDB; Q9LQ73; -.
DR PRO; PR:Q9LQ73; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LQ73; baseline and differential.
DR Genevisible; Q9LQ73; AT.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
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:0009506; C:plasmodesma; HDA:TAIR.
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..235
FT /note="Peroxisomal membrane protein 11C"
FT /id="PRO_0000330297"
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..206
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:16636080"
FT TRANSMEM 207..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 227..235
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16636080"
FT CONFLICT 124
FT /note="R -> L (in Ref. 2; CAD58675)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 235 AA; 25912 MW; 8DE9422A23181A49 CRC64;
MSTLETTRAE LGLVVVYLNK AEARDKICRA IQYGSKFLSD GQPGTAQNVD KNTSLARKVF
RLFKFVNDLH ALISPVPKGT PLPLVLLGKS KNALLSTFLF LDQIVWLGRT GIYKDKERAE
ILGRISLFCW MGSSVCTSLV EVGELGRLSA SIKKLEKEIG NKDKHQNEQY RAKVEKSNER
SLALIKAGMD VVVAFGLLQL APKKVTPRVT GAFGFASSLI SCYQLLPSHP KSKMV
