PEX10_ARATH
ID PEX10_ARATH Reviewed; 381 AA.
AC Q9SYU4; O65895; Q8LBN2; Q8S8Q5; Q9M400;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Peroxisome biogenesis factor 10;
DE AltName: Full=PER10;
DE AltName: Full=Peroxin-10;
DE AltName: Full=Peroxisomal biogenesis factor 10;
DE Short=AtPEX10;
DE Short=AthPEX10;
DE AltName: Full=Peroxisome assembly protein 10;
DE AltName: Full=Pex10p;
GN Name=PEX10; OrderedLocusNames=At2g26350; ORFNames=T9J22.2;
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 Schumann U., Gietl C., Schmid M.;
RT "Sequence analysis of a cDNA encoding Pex10p, a zinc-binding peroxisomal
RT integral membrane protein from Arabidopsis thaliana.";
RL (er) Plant Gene Register PGR99-025(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=10961948; DOI=10.1042/bst0280499;
RA Baker A., Charlton W., Johnson B., Lopez-Huertas E., Oh J., Sparkes I.,
RA Thomas J.;
RT "Biochemical and molecular approaches to understanding protein import into
RT peroxisomes.";
RL Biochem. Soc. Trans. 28:499-504(2000).
RN [3]
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 [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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [6]
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 [7]
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 [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, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=14576288; DOI=10.1104/pp.103.031252;
RA Sparkes I.A., Brandizzi F., Slocombe S.P., El-Shami M., Hawes C., Baker A.;
RT "An Arabidopsis pex10 null mutant is embryo lethal, implicating peroxisomes
RT in an essential role during plant embryogenesis.";
RL Plant Physiol. 133:1809-1819(2003).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12883010; DOI=10.1073/pnas.1633697100;
RA Schumann U., Wanner G., Veenhuis M., Schmid M., Gietl C.;
RT "AthPEX10, a nuclear gene essential for peroxisome and storage organelle
RT formation during Arabidopsis embryogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:9626-9631(2003).
RN [11]
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=16169966; DOI=10.1104/pp.105.065094;
RA Sparkes I.A., Hawes C., Baker A.;
RT "AtPEX2 and AtPEX10 are targeted to peroxisomes independently of known
RT endoplasmic reticulum trafficking routes.";
RL Plant Physiol. 139:690-700(2005).
RN [12]
RP INTERACTION WITH PEX19-1.
RX PubMed=16923726; DOI=10.1080/09687860600738221;
RA Hadden D.A., Phillipson B.A., Johnston K.A., Brown L.A., Manfield I.W.,
RA El-Shami M., Sparkes I.A., Baker A.;
RT "Arabidopsis PEX19 is a dimeric protein that binds the peroxin PEX10.";
RL Mol. Membr. Biol. 23:325-336(2006).
RN [13]
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 [14]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF CYS-342; HIS-344;
RP CYS-347 AND CYS-350.
RX PubMed=17215364; DOI=10.1073/pnas.0610402104;
RA Schumann U., Prestele J., O'Geen H., Brueggeman R., Wanner G., Gietl C.;
RT "Requirement of the C3HC4 zinc RING finger of the Arabidopsis PEX10 for
RT photorespiration and leaf peroxisome contact with chloroplasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1069-1074(2007).
RN [15]
RP FUNCTION, AND MUTAGENESIS OF GLY-93 AND PRO-126.
RX PubMed=20679226; DOI=10.1073/pnas.1009174107;
RA Prestele J., Hierl G., Scherling C., Hetkamp S., Schwechheimer C.,
RA Isono E., Weckwerth W., Wanner G., Gietl C.;
RT "Different functions of the C3HC4 zinc RING finger peroxins PEX10, PEX2,
RT and PEX12 in peroxisome formation and matrix protein import.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:14915-14920(2010).
RN [16]
RP FUNCTION, AND COFACTOR.
RX PubMed=23336935; DOI=10.1111/jipb.12014;
RA Kaur N., Zhao Q., Xie Q., Hu J.;
RT "Arabidopsis RING peroxins are E3 ubiquitin ligases that interact with two
RT homologous ubiquitin receptor proteins(F).";
RL J. Integr. Plant Biol. 55:108-120(2013).
CC -!- FUNCTION: Involved in the formation of peroxisomes, lipid bodies and
CC protein bodies. Required for normal-shaped peroxisomes that can
CC physically associate with the outer membrane of the chloroplast
CC envelope. Not involved in beta-oxidation and glyoxylate cycle. Acts as
CC an E3 ubiquitin-protein ligase. {ECO:0000269|PubMed:12883010,
CC ECO:0000269|PubMed:14576288, ECO:0000269|PubMed:17215364,
CC ECO:0000269|PubMed:17478547, ECO:0000269|PubMed:20679226,
CC ECO:0000269|PubMed:23336935}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:23336935};
CC -!- SUBUNIT: Interacts (via C-terminus) with PEX19-1.
CC {ECO:0000269|PubMed:16923726}.
CC -!- INTERACTION:
CC Q9SYU4; Q9SRQ3: PEX19-1; NbExp=2; IntAct=EBI-1151983, EBI-1151789;
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:14576288,
CC ECO:0000269|PubMed:16169966}. Peroxisome membrane {ECO:0000305};
CC Peripheral membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, flowers and
CC siliques. {ECO:0000269|PubMed:14576288}.
CC -!- DEVELOPMENTAL STAGE: Increased expression in early post-germinative
CC growth.
CC -!- INDUCTION: Up-regulated by hydrogen peroxide.
CC {ECO:0000269|PubMed:11118212}.
CC -!- DISRUPTION PHENOTYPE: Embryo lethality at the heart stage.
CC {ECO:0000269|PubMed:12883010, ECO:0000269|PubMed:14576288,
CC ECO:0000269|PubMed:17215364}.
CC -!- MISCELLANEOUS: Travels directly from the cytosol to the peroxisomes.
CC -!- SIMILARITY: Belongs to the pex2/pex10/pex12 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM14959.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF119572; AAD18035.1; -; mRNA.
DR EMBL; AJ276134; CAB87983.1; -; mRNA.
DR EMBL; AC002505; AAC14514.2; -; Genomic_DNA.
DR EMBL; AC004484; AAM14959.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC07828.1; -; Genomic_DNA.
DR EMBL; AK117879; BAC42519.1; -; mRNA.
DR EMBL; BT005340; AAO63404.1; -; mRNA.
DR EMBL; AY087109; AAM64667.1; -; mRNA.
DR PIR; T00968; T00968.
DR RefSeq; NP_001323819.1; NM_001336060.1.
DR RefSeq; NP_565621.1; NM_128192.2.
DR AlphaFoldDB; Q9SYU4; -.
DR SMR; Q9SYU4; -.
DR BioGRID; 2527; 3.
DR IntAct; Q9SYU4; 3.
DR STRING; 3702.AT2G26350.1; -.
DR TCDB; 3.A.20.1.2; the peroxisomal protein importer (ppi) family.
DR PaxDb; Q9SYU4; -.
DR PRIDE; Q9SYU4; -.
DR ProteomicsDB; 236427; -.
DR EnsemblPlants; AT2G26350.1; AT2G26350.1; AT2G26350.
DR GeneID; 817175; -.
DR Gramene; AT2G26350.1; AT2G26350.1; AT2G26350.
DR KEGG; ath:AT2G26350; -.
DR Araport; AT2G26350; -.
DR TAIR; locus:2057780; AT2G26350.
DR eggNOG; KOG0317; Eukaryota.
DR HOGENOM; CLU_041707_0_0_1; -.
DR InParanoid; Q9SYU4; -.
DR OMA; RNWIKYN; -.
DR OrthoDB; 1593722at2759; -.
DR PhylomeDB; Q9SYU4; -.
DR PRO; PR:Q9SYU4; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SYU4; baseline and differential.
DR Genevisible; Q9SYU4; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005778; C:peroxisomal membrane; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IMP:TAIR.
DR GO; GO:0007031; P:peroxisome organization; IMP:TAIR.
DR GO; GO:0010381; P:peroxisome-chloroplast membrane tethering; IMP:TAIR.
DR GO; GO:0009853; P:photorespiration; IMP:TAIR.
DR GO; GO:0016558; P:protein import into peroxisome matrix; IMP:TAIR.
DR GO; GO:0006513; P:protein monoubiquitination; IDA:TAIR.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR006845; Pex_N.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF04757; Pex2_Pex12; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Membrane; Metal-binding; Peroxisome; Peroxisome biogenesis;
KW Reference proteome; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..381
FT /note="Peroxisome biogenesis factor 10"
FT /id="PRO_0000056382"
FT ZN_FING 327..365
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 93
FT /note="G->E: Deformed peroxisomes, but no effect on
FT contacts with chloroplasts and on protein import."
FT /evidence="ECO:0000269|PubMed:20679226"
FT MUTAGEN 126
FT /note="P->S: No effects on peroxisome shape, contacts with
FT chloroplasts and protein import."
FT /evidence="ECO:0000269|PubMed:20679226"
FT MUTAGEN 342
FT /note="C->G: Embryo lethality; when associated with L-344;
FT G-347 and G-350."
FT /evidence="ECO:0000269|PubMed:17215364"
FT MUTAGEN 344
FT /note="H->L: Embryo lethality; when associated with G-342;
FT G-347 and G-350."
FT /evidence="ECO:0000269|PubMed:17215364"
FT MUTAGEN 347
FT /note="C->G: Embryo lethality; when associated with G-342;
FT L-344 and G-350."
FT /evidence="ECO:0000269|PubMed:17215364"
FT MUTAGEN 350
FT /note="C->G: Embryo lethality; when associated with G-342;
FT L-344 and G-347."
FT /evidence="ECO:0000269|PubMed:17215364"
FT CONFLICT 184
FT /note="M -> K (in Ref. 2; CAB87983 and 7; AAM64667)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="P -> L (in Ref. 2; CAB87983)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="F -> S (in Ref. 7; AAM64667)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="K -> N (in Ref. 7; AAM64667)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 381 AA; 42614 MW; 41AFF2C25E65584A CRC64;
MRLNGDSGPG QDEPGSSGFH GGIRRFPLAA QPEIMRAAEK DDQYASFIHE ACRDAFRHLF
GTRIALAYQK EMKLLGQMLY YVLTTGSGQQ TLGEEYCDII QVAGPYGLSP TPARRALFIL
YQTAVPYIAE RISTRAATQA VTFDESDEFF GDSHIHSPRM IDLPSSSQVE TSTSVVSRLN
DRLMRSWHRA IQRWPVVLPV AREVLQLVLR ANLMLFYFEG FYYHISKRAS GVRYVFIGKQ
LNQRPRYQIL GVFLLIQLCI LAAEGLRRSN LSSITSSIQQ ASIGSYQTSG GRGLPVLNEE
GNLITSEAEK GNWSTSDSTS TEAVGKCTLC LSTRQHPTAT PCGHVFCWSC IMEWCNEKQE
CPLCRTPNTH SSLVCLYHSD F
