PEX1_ARTOA
ID PEX1_ARTOA Reviewed; 1194 AA.
AC G1X7C7;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Peroxisomal biogenesis factor 1 {ECO:0000303|PubMed:35323036};
DE AltName: Full=Peroxin-1 {ECO:0000250|UniProtKB:P24004};
GN Name=PEX1 {ECO:0000303|PubMed:35323036}; ORFNames=AOL_s00054g771;
OS Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX NCBI_TaxID=756982;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491;
RX PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT provide insights into nematode-trap formation.";
RL PLoS Pathog. 7:E1002179-E1002179(2011).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=35323036; DOI=10.1128/spectrum.00275-22;
RA Liu Q., Li D., Jiang K., Zhang K.Q., Yang J.;
RT "AoPEX1 and AoPEX6 are required for mycelial growth, conidiation, stress
RT Response, fatty acid utilization, and trap formation in Arthrobotrys
RT oligospora.";
RL Microbiol. Spectr. 10:e0027522-e0027522(2022).
CC -!- FUNCTION: Peroxisomal biogenesis factor that has pleiotropic roles in
CC various cellular processes (PubMed:35323036). Regulates autophagy and
CC biogenesis of peroxisomes and Woronin bodies (PubMed:35323036). Plays
CC important roles in mycelial growth and development and stress response
CC (PubMed:35323036). Is also essential for conidiation and fatty acid
CC utilization (PubMed:35323036). Required for nematode predation via trap
CC formation (PubMed:35323036). {ECO:0000269|PubMed:35323036}.
CC -!- SUBUNIT: Interacts with PEX6 to form a high-molecular-mass
CC heterooligomer in the cytosol (By similarity). The PEX1-PEX6
CC heterooligomers associate with the peroxisomal importomer via
CC interaction of PEX6 with the peroxisomal membrane anchor PEX15 (By
CC similarity). {ECO:0000250|UniProtKB:P24004}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P24004}.
CC Peroxisome membrane {ECO:0000250|UniProtKB:P24004}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:P24004}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P24004}. Note=Shuttles between the cytoplasm and
CC the peroxisomal membrane. {ECO:0000250|UniProtKB:P24004}.
CC -!- DOMAIN: AAA-cassette D1 is required for interaction with PEX6 (By
CC similarity). ATP-binding in AAA-cassette D2 is required for interaction
CC with PEX6 (By similarity). ATP-binding and hydrolysis in AAA-cassette
CC D2 is required for proper function in PEX5 dislocation (By similarity).
CC {ECO:0000250|UniProtKB:P24004}.
CC -!- DISRUPTION PHENOTYPE: Leads to growth defects with sparse aerial
CC hyphae, and reduced number of nuclei in hyphal cells (PubMed:35323036).
CC Results also in complete elimination of sporulation and trap formation
CC and a remarkable decrease in the ability to trap nematodes
CC (PubMed:35323036). Leads to defective cell wall biosynthesis and
CC increased stress susceptibility (PubMed:35323036). Results in the up-
CC regulation of the proteasome, membranes, ribosomes, DNA replication,
CC and cell cycle functions, and the down-regulation of MAPK signaling and
CC nitrogen metabolism (PubMed:35323036). {ECO:0000269|PubMed:35323036}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; ADOT01000092; EGX51035.1; -; Genomic_DNA.
DR RefSeq; XP_011120389.1; XM_011122087.1.
DR STRING; 13349.G1X7C7; -.
DR EnsemblFungi; EGX51035; EGX51035; AOL_s00054g771.
DR GeneID; 22891350; -.
DR eggNOG; KOG0735; Eukaryota.
DR HOGENOM; CLU_000688_1_0_1; -.
DR InParanoid; G1X7C7; -.
DR OMA; LSASWCA; -.
DR OrthoDB; 1171861at2759; -.
DR Proteomes; UP000008784; Unassembled WGS sequence.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0006625; P:protein targeting to peroxisome; IEA:InterPro.
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 InterPro; IPR025653; Pex1.
DR PANTHER; PTHR23077:SF12; PTHR23077:SF12; 1.
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 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Membrane; Nucleotide-binding; Peroxisome;
KW Peroxisome biogenesis; Reference proteome; Virulence.
FT CHAIN 1..1194
FT /note="Peroxisomal biogenesis factor 1"
FT /id="PRO_0000456237"
FT REGION 538..730
FT /note="AAA-cassette D1"
FT /evidence="ECO:0000250|UniProtKB:P24004"
FT REGION 844..1028
FT /note="AAA-cassette D2"
FT /evidence="ECO:0000250|UniProtKB:P24004"
FT BINDING 546..553
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 849..856
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1194 AA; 127861 MW; E1A62177D1AC3999 CRC64;
MASSQRRGPT TKTPAVVGLT ALRNCLVNLP SGLVSVLVSS NTPAQNVVVE LSWRVKAPPQ
AGPLTGPATI TRQAFAGWTG MPSKRQPLQP QGAGSFPGSQ RSNSLEGCVE IDSAFARNVG
LTEGSKVNIL LHVDPPTTHT IHIEPLTASD WEIIELHATF LELNLLSQIR AITFAHPLTV
YLSPTSTASI KVARIEPEDA ASAFGFAKIA PNAEVIVAPK TRQRRMSHQG KSVKAKSLAS
TRHGKRRDDG SGPSGGGPVF FRAISLPHES FDAAEEQKGA YCVYLDPEVL AIPALRGCAF
VGVVVVRPPG LAPPPDANQA NNDVGGSTSP DAPEVIKPSL KIVAKLLPWK NAPDLKHIAI
SNLLADALDI KNVVGCVIRI EAAHQQLPKG STTKVIIRPY SAGTLSSSAA SEQSSLRWSG
KDWKSDLAVR RVKEVLSQKT VWGEDILGGP LSDRLVLPAI PDSPLFAGGI LLLDGSEVKH
GWILGGDRKY ILELGSEITT SRPHVPLSIS ETALPVLPPG RIVGVDKAIN TASNILTRSA
SVLLTGARGS GKTSLVSVIT SILKKKHFFH VLPISCAKFA DERLQTIKDT FSRAIAEAKW
FSPTVIVFDD LDRLIPAEVE HADSTRSRYI AEAFGKAIRD LKSSVLGPGN VVILATVQAK
ESVNSLIVGG HIFREIITLK APNKAGRRQV LEQAVGGLSD EKSSPDTSSI RVKNPAALTN
GPEPTLKIEK GLELLDIAGM TDGYMPADLQ LLVGRARHEA IVRAVESGSD DAEADLVLGK
KDFDKAIKGF VPAGLRGVKL QTSGAAWKDI GGLTETRKIL LETLEWPTRY APIFANCPLR
LRSGLLLYGY PGCGKTLLAS AVAGECGLNF ISVKGPEILN KYIGASEKSV RDLFERASAA
KPCVLFFDEF DSIAPKRGHD STGVTDRVVN QMLTQMDGAE GLDGVYVLAA TSRPDLIDPA
LLRPGRLDKS LLCDLPNLED RVDILRALSL KLKIEESIGL EDIANLTEGY SGADLQAVLY
NAHLEAIHDV IASQDEEVER FGNGGKGKGK VDAGSGNDSI DYISFSMGNK DSTGEPSTQP
LTNGTQAART KFAERAAVMA KLDKLKKIVQ GDAAKQVQQQ QSQTNQAQEE EKGDDEPVIN
WKHLQSSLKS TRPSIAPDER KRLFRIYNEF IVGRSGEMPS GQSSTEIGGR SSLM
