PEX2_ARATH
ID PEX2_ARATH Reviewed; 333 AA.
AC Q9CA86; Q8LFI7; Q9M9Z9;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Peroxisome biogenesis protein 2;
DE AltName: Full=E3 ubiquitin-protein ligase PEX2;
DE AltName: Full=Peroxin-2;
DE Short=AtPEX2;
DE Short=AthPEX2;
DE AltName: Full=Pex2p;
GN Name=PEX2; Synonyms=TED3; OrderedLocusNames=At1g79810;
GN ORFNames=F19K16.23, F20B17.23;
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 [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 [2]
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 [3]
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 [4]
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 [5]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP MUTAGENESIS OF VAL-275, AND DISRUPTION PHENOTYPE.
RX PubMed=12130786; DOI=10.1126/science.1073633;
RA Hu J., Aguirre M., Peto C., Alonso J., Ecker J., Chory J.;
RT "A role for peroxisomes in photomorphogenesis and development of
RT Arabidopsis.";
RL Science 297:405-409(2002).
RN [6]
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 [7]
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 [8]
RP FUNCTION.
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 [9]
RP INTERACTION WITH DSK2A AND DSK2B, 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: Might act directly in a photomorphogenetic pathway negatively
CC regulated by DET1, which is involved in peroxisome assembly and matrix
CC protein import. Could be part of a complex responsible for the
CC monoubiquitination of PEX5. Acts as an E3 ubiquitin-protein ligase.
CC {ECO:0000269|PubMed:12130786, ECO:0000269|PubMed:17478547,
CC ECO:0000269|PubMed:20679226, ECO:0000269|PubMed:23336935}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:23336935};
CC -!- SUBUNIT: Interacts with DSK2a and DSK2b. {ECO:0000269|PubMed:23336935}.
CC -!- INTERACTION:
CC Q9CA86; Q9SII9: DSK2A; NbExp=3; IntAct=EBI-4470254, EBI-6860633;
CC Q9CA86; Q9SII8: DSK2B; NbExp=4; IntAct=EBI-4470254, EBI-4433040;
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:12130786,
CC ECO:0000269|PubMed:16169966}. Peroxisome membrane {ECO:0000305};
CC Peripheral membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9CA86-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, flowers, pollen,
CC ovules, seeds and siliques. {ECO:0000269|PubMed:12130786}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development.
CC {ECO:0000269|PubMed:12130786}.
CC -!- DISRUPTION PHENOTYPE: Embryo lethality at the heart stage.
CC {ECO:0000269|PubMed:12130786}.
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=AAF68113.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC010793; AAF68113.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC011717; AAG52254.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36301.1; -; Genomic_DNA.
DR EMBL; AY064063; AAL36419.1; -; mRNA.
DR EMBL; AY096373; AAM20014.1; -; mRNA.
DR EMBL; AY084823; AAM61388.1; -; mRNA.
DR PIR; A96829; A96829.
DR RefSeq; NP_565222.1; NM_106630.3. [Q9CA86-1]
DR AlphaFoldDB; Q9CA86; -.
DR BioGRID; 29538; 5.
DR IntAct; Q9CA86; 3.
DR STRING; 3702.AT1G79810.1; -.
DR PaxDb; Q9CA86; -.
DR PRIDE; Q9CA86; -.
DR ProteomicsDB; 251040; -. [Q9CA86-1]
DR EnsemblPlants; AT1G79810.1; AT1G79810.1; AT1G79810. [Q9CA86-1]
DR GeneID; 844320; -.
DR Gramene; AT1G79810.1; AT1G79810.1; AT1G79810. [Q9CA86-1]
DR KEGG; ath:AT1G79810; -.
DR Araport; AT1G79810; -.
DR TAIR; locus:2017804; AT1G79810.
DR eggNOG; KOG2879; Eukaryota.
DR HOGENOM; CLU_024591_3_0_1; -.
DR OMA; SCFHGFK; -.
DR OrthoDB; 1494604at2759; -.
DR PhylomeDB; Q9CA86; -.
DR PRO; PR:Q9CA86; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9CA86; baseline and differential.
DR Genevisible; Q9CA86; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA: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:0006635; P:fatty acid beta-oxidation; IMP:TAIR.
DR GO; GO:0007031; P:peroxisome organization; IMP:TAIR.
DR GO; GO:0009640; P:photomorphogenesis; 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; IPR018957; Znf_C3HC4_RING-type.
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; PF00097; zf-C3HC4; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Membrane; Metal-binding; Peroxisome;
KW Peroxisome biogenesis; Reference proteome; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..333
FT /note="Peroxisome biogenesis protein 2"
FT /id="PRO_0000056375"
FT ZN_FING 277..318
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT MUTAGEN 275
FT /note="V->M: In ted3; suppressor of the det1 mutant
FT phenotype."
FT /evidence="ECO:0000269|PubMed:12130786"
SQ SEQUENCE 333 AA; 38174 MW; 5A1511BA37B63A19 CRC64;
MTPSTPADDA WIRSYQRLLP ESQSLLASRR SVIPVAISRV NQFDAARLDV EMSAMLKEQL
VKVFTLMKPG MLFQYEPELD AFLEFLIWRF SIWVDKPTPG NALMNLRYRD ERGVVAQHLG
KVRTGLEGPG LTSPQKIWYC VASVGGQYLF SRLQSFSAFR RWGDSEQRPL ARRLWTLVQR
IEGIYKAASF LNLLSFLYTG RYRNLIEKAL KARLVYRSPH MNRSVSFEYM NRQLVWNEFS
EMLLLLLPLL NSSAVKNILS PFAKDKSSST KEDTVTCPIC QVDPAIPFIA LPCQHRYCYY
CIRTRCASAA SFRCLRCNEP VVAIQREGVS SGK
