PEX1_ARATH
ID PEX1_ARATH Reviewed; 1130 AA.
AC Q9FNP1; Q9FQ60;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Peroxisome biogenesis protein 1;
DE AltName: Full=Peroxin-1;
DE Short=AtPEX1;
GN Name=PEX1; OrderedLocusNames=At5g08470; ORFNames=F8L15.15;
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=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
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 [MRNA] OF 12-1130, INDUCTION BY HYDROGEN PEROXIDE;
RP WOUNDING AND PATHOGEN INFECTION, DEVELOPMENTAL STAGE, AND TISSUE
RP SPECIFICITY.
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 [4]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15449020; DOI=10.1007/s00299-004-0879-7;
RA Charlton W.L., Johnson B., Graham I.A., Baker A.;
RT "Non-coordinate expression of peroxisome biogenesis, beta-oxidation and
RT glyoxylate cycle genes in mature Arabidopsis plants.";
RL Plant Cell Rep. 23:647-653(2005).
RN [5]
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 [6]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH PEX6.
RX PubMed=21487094; DOI=10.1105/tpc.110.080770;
RA Goto S., Mano S., Nakamori C., Nishimura M.;
RT "Arabidopsis ABERRANT PEROXISOME MORPHOLOGY9 is a peroxin that recruits the
RT PEX1-PEX6 complex to peroxisomes.";
RL Plant Cell 23:1573-1587(2011).
CC -!- FUNCTION: Involved in PTS1- and PTS2-dependent protein import into
CC peroxisomes. May form heteromeric AAA ATPase complexes required for the
CC import of proteins. {ECO:0000269|PubMed:17478547}.
CC -!- SUBUNIT: Forms a AAA ATPase complex in the cytoplasm with PEX6.
CC {ECO:0000269|PubMed:21487094}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21487094}.
CC Note=Localizes to the peroxisome when interacting with the PEX6/APEM9
CC complex. {ECO:0000269|PubMed:21487094}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in meristems and young developing
CC leaves. Expressed in seedlings, roots, leaves, flowers, siliques and
CC stems. Not detected in root tips. {ECO:0000269|PubMed:11118212,
CC ECO:0000269|PubMed:15449020}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed during the first two days post-
CC germinative growth. Strongly up-regulated in senescence.
CC {ECO:0000269|PubMed:11118212, ECO:0000269|PubMed:15449020}.
CC -!- INDUCTION: By wounding and avirulent pathogen infection. Systemic
CC induction by hydrogen peroxide. {ECO:0000269|PubMed:11118212}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09996.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB006697; BAB09996.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91307.1; -; Genomic_DNA.
DR EMBL; AF275382; AAG44817.1; -; mRNA.
DR RefSeq; NP_196464.2; NM_120932.3.
DR AlphaFoldDB; Q9FNP1; -.
DR SMR; Q9FNP1; -.
DR STRING; 3702.AT5G08470.1; -.
DR PaxDb; Q9FNP1; -.
DR PRIDE; Q9FNP1; -.
DR ProteomicsDB; 236461; -.
DR EnsemblPlants; AT5G08470.1; AT5G08470.1; AT5G08470.
DR GeneID; 830746; -.
DR Gramene; AT5G08470.1; AT5G08470.1; AT5G08470.
DR KEGG; ath:AT5G08470; -.
DR Araport; AT5G08470; -.
DR TAIR; locus:2159557; AT5G08470.
DR eggNOG; KOG0735; Eukaryota.
DR HOGENOM; CLU_000688_1_1_1; -.
DR InParanoid; Q9FNP1; -.
DR OrthoDB; 1171861at2759; -.
DR PhylomeDB; Q9FNP1; -.
DR BRENDA; 3.6.4.7; 399.
DR PRO; PR:Q9FNP1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FNP1; baseline and differential.
DR Genevisible; Q9FNP1; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005778; C:peroxisomal membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IMP:TAIR.
DR GO; GO:0016558; P:protein import into peroxisome matrix; IMP:TAIR.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR029067; CDC48_domain_2-like_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015342; PEX-N_psi_beta-barrel.
DR Pfam; PF00004; AAA; 2.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF09262; PEX-1N; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF50692; SSF50692; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54585; SSF54585; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Nucleotide-binding; Peroxisome biogenesis;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..1130
FT /note="Peroxisome biogenesis protein 1"
FT /id="PRO_0000404526"
FT BINDING 600..607
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 885..892
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1130 AA; 123844 MW; D62F682D944BDDEC CRC64;
MSRNRQIIIP DDVMETEAVV NTVAGVDCFV SLPRQLLHAL QSTSSSPLPP LLPVELRSGD
RRWSVAWSGS SSSSSAIEIA RVFAESISLP DGTVVKVRVL PNVPKATLVT VEPETEDDWE
VLELNAELAE AAILSQVRIL HETMKFPLWL HDRTVIRFSV VSTFPSKGVV QLVPGTEVAV
APKRRDRNLK AKKSQEKECN NVKALLRVQE TDRSAFHEAD VKGFELRVAL TSIAYIHPET
AKKHSLESLQ LISVSPRIPL KGSAKKDEAL NMKNSEASKV AENGTSSAKK EPRQAILRLV
FSDLAAKGHL MMVESLRLYL GAGLHSWVYL RGCNVNEDKE IPALSLSPCV FKISENEKVL
DKGTDRLGNN NSVRKSSHPP SGLSTYVDVV DWSVHDKVVT ALSSEGLHDE GNHDKNKKGL
EYLTRLWSLA QLDAMASVTG VDVSSLIVGR ETFFHFEVRG LESYKSIDGQ PSVNDRWESG
KKDKHTPLEI LYVMTVSDES LLGDKFAGYD LSLDRSEKSD NVVHIEPVLE KMNLGEPIYL
KSAKETHCNK GVSPDISSLT WMGPIVSDVI KRMTVLLSPA AGMWFSKFKI PSPGHILIYG
PPGSGKTILA RAAAKYFEEQ KDLLAHVILV SCSTLALEKV QHIHHVLSSV IAEGLEHAPS
VIILDDLDSI ISSSSDTEGT QASVGVTMLT KFLTDVIDDY GEYRNSSCGI GPLAFVASVQ
SLEQIPQTLS SSGRFDFHVQ LAAPATSERG AILKHEIQKR LLDCSEDILL NLAAKCEGYD
AYDLEILVDR AVHAAIGRHL PLESNISKYN LVKEDFTRAM HDFVPVAMRD ITKSASEGGR
LGWEDVGGVT DIKNAIKEMI ELPSKFPKIF AKSPLRLRSN VLLYGPPGCG KTHIVGAAAA
ACSLRFISVK GPELLNKYIG ASEQAVRDIF SKAAAAAPCI LFFDEFDSIA PKRGHDNTGV
TDRVVNQFLT ELDGVEVLTG VFVFAATSRP DLLDPALLRP GRLDRLLLCD FPSPPERLEI
LTVLSRKLLM ADDIDLEPIA LMTEGFSGAD LQALLSDAQL AAVHEYLNRE DKPETGTTPI
ITDPLLKSIA SKTKPSVSET EKQKLYDIYS QFLDSRKSSR EAKGKRATLA
