PEX14_ARATH
ID PEX14_ARATH Reviewed; 507 AA.
AC Q9FXT6; Q8L620; Q8L9N2; Q9FE40; Q9FT86;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Peroxisomal membrane protein PEX14;
DE AltName: Full=Peroxin-14;
DE Short=AtPEX14;
DE AltName: Full=Peroxisome biogenesis protein 14;
DE AltName: Full=Pex14p;
DE AltName: Full=Protein PEROXISOME DEFECTIVE 2;
GN Name=PEX14; Synonyms=PED2; OrderedLocusNames=At5g62810; ORFNames=MQB2.13;
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].
RA Oh J., Lopez-Huertas E., Charlton W., Baker A.;
RT "The peroxin PEX14 from higher plants. Cloning, expression, localisation
RT and topology.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=11060021; DOI=10.1093/emboj/19.21.5701;
RA Hayashi M., Nito K., Toriyama-Kato K., Kondo M., Yamaya T., Nishimura M.;
RT "AtPex14p maintains peroxisomal functions by determining protein targeting
RT to three kinds of plant peroxisomes.";
RL EMBO J. 19:5701-5710(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
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;
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] OF 113-507.
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 254-507.
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 [8]
RP INDUCTION BY HYDROGEN PEROXIDE.
RC STRAIN=cv. Columbia;
RX PubMed=11118212; DOI=10.1093/emboj/19.24.6770;
RA Lopez-Huertas E., Charlton W.L., Johnson B., Graham I.A., Baker A.;
RT "Stress induces peroxisome biogenesis genes.";
RL EMBO J. 19:6770-6777(2000).
RN [9]
RP FUNCTION, INTERACTION WITH PEX5; PEX7 AND PTS1-CONTAINING PROTEINS, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11978862; DOI=10.1093/pcp/pcf057;
RA Nito K., Hayashi M., Nishimura M.;
RT "Direct interaction and determination of binding domains among peroxisomal
RT import factors in Arabidopsis thaliana.";
RL Plant Cell Physiol. 43:355-366(2002).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17951448; DOI=10.1105/tpc.107.050989;
RA Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T., Antonicelli G.E.,
RA Rasche N., Lueder F., Weckwerth W., Jahn O.;
RT "Proteome analysis of Arabidopsis leaf peroxisomes reveals novel targeting
RT peptides, metabolic pathways, and defense mechanisms.";
RL Plant Cell 19:3170-3193(2007).
RN [11]
RP FUNCTION.
RX PubMed=17478547; DOI=10.1093/pcp/pcm053;
RA Nito K., Kamigaki A., Kondo M., Hayashi M., Nishimura M.;
RT "Functional classification of Arabidopsis peroxisome biogenesis factors
RT proposed from analyses of knockdown mutants.";
RL Plant Cell Physiol. 48:763-774(2007).
RN [12]
RP INDUCTION BY WOUNDING AND JASMONATE.
RX PubMed=18194426; DOI=10.1111/j.1365-3040.2008.01780.x;
RA Castillo M.C., Sandalio L.M., Del Rio L.A., Leon J.;
RT "Peroxisome proliferation, wound-activated responses and expression of
RT peroxisome-associated genes are cross-regulated but uncoupled in
RT Arabidopsis thaliana.";
RL Plant Cell Environ. 31:492-505(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [14]
RP FUNCTION.
RX PubMed=19594707; DOI=10.1111/j.1365-313x.2009.03970.x;
RA Singh T., Hayashi M., Mano S., Arai Y., Goto S., Nishimura M.;
RT "Molecular components required for the targeting of PEX7 to peroxisomes in
RT Arabidopsis thaliana.";
RL Plant J. 60:488-498(2009).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: Controls intracellular transport of both PTS1- and PTS2-
CC containing proteins. Required for the proper targeting of PEX7 to the
CC peroxisome. {ECO:0000269|PubMed:11060021, ECO:0000269|PubMed:11978862,
CC ECO:0000269|PubMed:17478547, ECO:0000269|PubMed:19594707}.
CC -!- SUBUNIT: Interacts with PEX5 (via the WXXXF/Y repeats), but not with
CC PEX7 and PTS1-containing proteins. {ECO:0000269|PubMed:11978862}.
CC -!- INTERACTION:
CC Q9FXT6; Q9FMA3: PEX5; NbExp=3; IntAct=EBI-9536455, EBI-993861;
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000305}; Single-pass
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in flowers, siliques, leaves and roots.
CC {ECO:0000269|PubMed:11978862}.
CC -!- DEVELOPMENTAL STAGE: Expressed at the early stage of germination and
CC during the conversion of glyoxysomes to peroxisomes.
CC {ECO:0000269|PubMed:11978862}.
CC -!- INDUCTION: By wounding and hydrogen peroxide, but not by jasmonate.
CC {ECO:0000269|PubMed:11118212, ECO:0000269|PubMed:18194426}.
CC -!- SIMILARITY: Belongs to the peroxin-14 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM20492.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAM65879.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ251524; CAC14740.1; -; mRNA.
DR EMBL; AB037538; BAB17667.1; -; Genomic_DNA.
DR EMBL; AB037539; BAB17668.1; -; mRNA.
DR EMBL; AB009053; BAB10850.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97660.1; -; Genomic_DNA.
DR EMBL; AK227047; BAE99107.1; -; mRNA.
DR EMBL; AY099641; AAM20492.1; ALT_INIT; mRNA.
DR EMBL; BT003409; AAO30072.1; -; mRNA.
DR EMBL; AY088340; AAM65879.1; ALT_INIT; mRNA.
DR RefSeq; NP_201087.3; NM_125676.5.
DR AlphaFoldDB; Q9FXT6; -.
DR SMR; Q9FXT6; -.
DR BioGRID; 21645; 1.
DR ELM; Q9FXT6; -.
DR IntAct; Q9FXT6; 2.
DR MINT; Q9FXT6; -.
DR STRING; 3702.AT5G62810.1; -.
DR TCDB; 3.A.20.1.2; the peroxisomal protein importer (ppi) family.
DR iPTMnet; Q9FXT6; -.
DR PaxDb; Q9FXT6; -.
DR PRIDE; Q9FXT6; -.
DR ProteomicsDB; 236309; -.
DR EnsemblPlants; AT5G62810.1; AT5G62810.1; AT5G62810.
DR GeneID; 836402; -.
DR Gramene; AT5G62810.1; AT5G62810.1; AT5G62810.
DR KEGG; ath:AT5G62810; -.
DR Araport; AT5G62810; -.
DR TAIR; locus:2170688; AT5G62810.
DR eggNOG; KOG2629; Eukaryota.
DR HOGENOM; CLU_038637_0_0_1; -.
DR InParanoid; Q9FXT6; -.
DR OMA; FHWSHAI; -.
DR OrthoDB; 1044274at2759; -.
DR PhylomeDB; Q9FXT6; -.
DR PRO; PR:Q9FXT6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FXT6; baseline and differential.
DR Genevisible; Q9FXT6; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:1990429; C:peroxisomal importomer complex; IBA:GO_Central.
DR GO; GO:0005778; C:peroxisomal membrane; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0007031; P:peroxisome organization; IMP:TAIR.
DR GO; GO:0016560; P:protein import into peroxisome matrix, docking; IBA:GO_Central.
DR GO; GO:0006625; P:protein targeting to peroxisome; TAS:TAIR.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR025655; PEX14.
DR InterPro; IPR006785; Pex14_N.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR23058; PTHR23058; 2.
DR Pfam; PF04695; Pex14_N; 1.
PE 1: Evidence at protein level;
KW Membrane; Peroxisome; Peroxisome biogenesis; Protein transport;
KW Reference proteome; Translocation; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..507
FT /note="Peroxisomal membrane protein PEX14"
FT /id="PRO_0000403360"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..65
FT /note="Involved in interaction with PEX5"
FT /evidence="ECO:0000269|PubMed:11978862"
FT REGION 78..97
FT /note="Involved in interaction with PEX5"
FT /evidence="ECO:0000269|PubMed:11978862"
FT REGION 288..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 69..72
FT /note="RVRG -> KVRS (in Ref. 1; CAC14740)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="Q -> R (in Ref. 1; CAC14740)"
FT /evidence="ECO:0000305"
FT CONFLICT 442
FT /note="V -> A (in Ref. 2; BAB17667, 1; CAC14740 and 7;
FT AAM65879)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 507 AA; 55595 MW; B00A96B5BE68B5C1 CRC64;
MATHQQTQPP SDFPALADEN SQIPEATKPA NEVQQATIAQ DPPTSVFKNS EPIREDQIQN
AIKFLSHPRV RGSPVIHRRS FLERKGLTKE EIDEAFRRVP DPPPSSQTTV TTSQDGQQAV
STVQPQAMQP VVAAPAPLIV TPQAAFLSRF RWYHAILAVG VLAASGAGTA VFIKRSLIPR
FKSWVQRIML EEETDPLKKA DAKPSLAEEA VAAAKAASAA ASDVARVSQE MMITKNEERK
YFEDLTHLLG VQVQEMKSLS NNIRKLEGQS NNIPKIYSAD QEVYNGSVTT ARKPYTNGSN
VDYDTRSARS ASPPAAPADS SAPPHPKSYM DIMSMIQRGE KPSNIREIND MPPNPNQPLS
DPRIAPKSKP WDYGQAPQDE SSNGQWWQQK NPRSTDFGYE TTTAARFTAN QNETSTMEPA
AFQRQRSWVP PQPPPVAMAE AVEAIRRPKP QAKIDQEAAA SDGQSGVSDE LQKITKFSES
GGDGSGGIKI AEIQEETEQQ HISQEGN
