PEX22_ARATH
ID PEX22_ARATH Reviewed; 283 AA.
AC Q9LSX7; Q8LCS2;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Peroxisome biogenesis protein 22;
DE AltName: Full=Peroxin-22;
DE Short=AtPEX22;
GN Name=PEX22; OrderedLocusNames=At3g21865; ORFNames=MSD21.24;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 133-283.
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 [6]
RP FUNCTION, AND INTERACTION WITH PEX4.
RX PubMed=16272432; DOI=10.1105/tpc.105.035691;
RA Zolman B.K., Monroe-Augustus M., Silva I.D., Bartel B.;
RT "Identification and functional characterization of Arabidopsis PEROXIN4 and
RT the interacting protein PEROXIN22.";
RL Plant Cell 17:3422-3435(2005).
RN [7]
RP IDENTIFICATION.
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=19246395; DOI=10.1073/pnas.0811329106;
RA Lingard M.J., Monroe-Augustus M., Bartel B.;
RT "Peroxisome-associated matrix protein degradation in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:4561-4566(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: May be tethered PEX4 to the peroxisome membrane and may be
CC involved in a late step of the matrix protein import. Does not play a
CC role in the biogenesis of the peroxisomal membrane.
CC {ECO:0000269|PubMed:16272432, ECO:0000269|PubMed:19246395}.
CC -!- SUBUNIT: Interacts with PEX4. {ECO:0000269|PubMed:16272432}.
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000250}; Single-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peroxin-22 family. {ECO:0000305}.
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DR EMBL; AB025634; BAB02849.1; -; Genomic_DNA.
DR EMBL; AP000739; BAB02849.1; JOINED; Genomic_DNA.
DR EMBL; CP002686; AEE76560.1; -; Genomic_DNA.
DR EMBL; AY063961; AAL36317.1; -; mRNA.
DR EMBL; AY096402; AAM20042.1; -; mRNA.
DR EMBL; AY086434; AAM67361.1; -; mRNA.
DR RefSeq; NP_566696.2; NM_113082.4.
DR PDB; 6XOD; X-ray; 2.01 A; B=111-283.
DR PDBsum; 6XOD; -.
DR AlphaFoldDB; Q9LSX7; -.
DR SMR; Q9LSX7; -.
DR BioGRID; 7073; 1.
DR IntAct; Q9LSX7; 1.
DR STRING; 3702.AT3G21865.1; -.
DR iPTMnet; Q9LSX7; -.
DR PaxDb; Q9LSX7; -.
DR PRIDE; Q9LSX7; -.
DR ProteomicsDB; 236312; -.
DR DNASU; 821741; -.
DR EnsemblPlants; AT3G21865.1; AT3G21865.1; AT3G21865.
DR GeneID; 821741; -.
DR Gramene; AT3G21865.1; AT3G21865.1; AT3G21865.
DR KEGG; ath:AT3G21865; -.
DR Araport; AT3G21865; -.
DR TAIR; locus:2093029; AT3G21865.
DR eggNOG; ENOG502QQ8Q; Eukaryota.
DR HOGENOM; CLU_069239_0_0_1; -.
DR InParanoid; Q9LSX7; -.
DR OMA; ENAGIFM; -.
DR OrthoDB; 1190418at2759; -.
DR PhylomeDB; Q9LSX7; -.
DR PRO; PR:Q9LSX7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LSX7; baseline and differential.
DR Genevisible; Q9LSX7; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007031; P:peroxisome organization; IMP:TAIR.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR037485; PEX22.
DR PANTHER; PTHR34126; PTHR34126; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Membrane; Peroxisome; Peroxisome biogenesis;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..283
FT /note="Peroxisome biogenesis protein 22"
FT /id="PRO_0000404534"
FT TRANSMEM 45..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 66..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 186
FT /note="R -> K (in Ref. 5; AAM67361)"
FT /evidence="ECO:0000305"
FT HELIX 127..135
FT /evidence="ECO:0007829|PDB:6XOD"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:6XOD"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:6XOD"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:6XOD"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:6XOD"
FT HELIX 169..178
FT /evidence="ECO:0007829|PDB:6XOD"
FT STRAND 179..186
FT /evidence="ECO:0007829|PDB:6XOD"
FT HELIX 190..202
FT /evidence="ECO:0007829|PDB:6XOD"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:6XOD"
FT STRAND 216..221
FT /evidence="ECO:0007829|PDB:6XOD"
FT HELIX 222..232
FT /evidence="ECO:0007829|PDB:6XOD"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:6XOD"
FT HELIX 242..248
FT /evidence="ECO:0007829|PDB:6XOD"
FT TURN 249..251
FT /evidence="ECO:0007829|PDB:6XOD"
FT STRAND 253..258
FT /evidence="ECO:0007829|PDB:6XOD"
FT STRAND 270..274
FT /evidence="ECO:0007829|PDB:6XOD"
FT HELIX 276..280
FT /evidence="ECO:0007829|PDB:6XOD"
SQ SEQUENCE 283 AA; 31399 MW; 9B8E5B52BFB86259 CRC64;
MAESSSPSPT EEIVRLIKRL SAYVAFKMSS LFSTTSIRNL DSRSIGAIAG LAIAVIFTWR
AIRTPGEQRQ RRQPKRRIHN AETSSAAAAA SQSNLASSVA PEVSSPREDN AVQDVVDQFF
QPVKPTLGQI VRQKLSEGRK VTCRLLGVIL EETSPEELQK QATVRSSVLE VLLEITKYSD
LYLMERVLDD ESEAKVLQAL ENAGVFTSGG LVKDKVLFCS TEIGRTSFVR QLEPDWHIDT
NPEISTQLAR FIKYQLHVAT VKPERTAPNV FTSQSIEQFF GSV
