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Database: UniProt
Entry: E1BPU3_BOVIN
LinkDB: E1BPU3_BOVIN
Original site: E1BPU3_BOVIN 
ID   E1BPU3_BOVIN            Unreviewed;      1281 AA.
AC   E1BPU3;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 2.
DT   24-JAN-2024, entry version 85.
DE   RecName: Full=Peroxisomal ATPase PEX1 {ECO:0000256|ARBA:ARBA00034532};
DE   AltName: Full=Peroxin-1 {ECO:0000256|ARBA:ARBA00032509};
GN   Name=PEX1 {ECO:0000313|Ensembl:ENSBTAP00000033778.4,
GN   ECO:0000313|VGNC:VGNC:32751};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000033778.4, ECO:0000313|Proteomes:UP000009136};
RN   [1] {ECO:0000313|Ensembl:ENSBTAP00000033778.4, ECO:0000313|Proteomes:UP000009136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000033778.4,
RC   ECO:0000313|Proteomes:UP000009136};
RA   Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA   Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA   Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT   "ARS-UCD1.2.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSBTAP00000033778.4}
RP   IDENTIFICATION.
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000033778.4};
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|ARBA:ARBA00034440};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC         Evidence={ECO:0000256|ARBA:ARBA00034440};
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
CC       {ECO:0000256|ARBA:ARBA00006914}.
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DR   SMR; E1BPU3; -.
DR   STRING; 9913.ENSBTAP00000033778; -.
DR   PaxDb; 9913-ENSBTAP00000033778; -.
DR   Ensembl; ENSBTAT00000033872.5; ENSBTAP00000033778.4; ENSBTAG00000024431.5.
DR   VEuPathDB; HostDB:ENSBTAG00000024431; -.
DR   VGNC; VGNC:32751; PEX1.
DR   eggNOG; KOG0735; Eukaryota.
DR   GeneTree; ENSGT00550000075032; -.
DR   HOGENOM; CLU_000688_1_1_1; -.
DR   InParanoid; E1BPU3; -.
DR   OMA; QGFVNIQ; -.
DR   TreeFam; TF106447; -.
DR   Reactome; R-BTA-9033241; Peroxisomal protein import.
DR   Proteomes; UP000009136; Chromosome 4.
DR   Bgee; ENSBTAG00000024431; Expressed in liver and 105 other cell types or tissues.
DR   ExpressionAtlas; E1BPU3; baseline and differential.
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:Ensembl.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0140318; F:protein transporter activity; IEA:Ensembl.
DR   GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR   GO; GO:0140036; F:ubiquitin-dependent protein binding; IEA:Ensembl.
DR   GO; GO:0060152; P:microtubule-based peroxisome localization; IEA:Ensembl.
DR   GO; GO:0016558; P:protein import into peroxisome matrix; IBA:GO_Central.
DR   GO; GO:0016562; P:protein import into peroxisome matrix, receptor recycling; IEA:Ensembl.
DR   GO; GO:0043335; P:protein unfolding; IEA:Ensembl.
DR   CDD; cd19526; RecA-like_PEX1_r2; 1.
DR   Gene3D; 1.10.8.60; -; 2.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.10.330.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR015343; PEX1-N-lobe.
DR   InterPro; IPR015342; PEX1-N_C-lobe.
DR   PANTHER; PTHR23077; AAA-FAMILY ATPASE; 1.
DR   PANTHER; PTHR23077:SF12; PEROXISOME BIOGENESIS FACTOR 1; 1.
DR   Pfam; PF00004; AAA; 2.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   Pfam; PF09262; PEX-1N; 1.
DR   Pfam; PF09263; PEX-2N; 1.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF54585; Cdc48 domain 2-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00674; AAA; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          590..740
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          872..1008
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          345..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1140..1173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1259..1281
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        351..373
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1140..1162
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1281 AA;  142149 MW;  31109096D2256D96 CRC64;
     MWGSGRLAGS GGGAAVTVAF TNARDCFLHL PRRLVAQLHL LQNQAIEVAW GHQPAFLSWV
     EGRHFSDEGE NVAEINRQVG QKLGLSNGAQ VFLKPCSHVV SCQQVEVEPL SADDWEILEL
     HAASLEQHLL DQIRIVFPKA IFPVWVDQQT YIFIQIAALI PDAPYGRLET DSRLLIQPKT
     RQAKESTFSE AEDIPGKFHH YGRDQKGLTK ELQTKQLQSN TVGVAGSKER ESEGRIDSSF
     IPSLWTMIGS IFSSGSEKKR DTSWGLTEVN AFKNMQSAVV PLDNIFRVCK SQPPSMCKAS
     ATSVFHKHYA IHVFPWDQEY FDVEPSFTVT YGKLVKLLSP KQQQSRTKQN VLSPEKEKQM
     SEPLDQKQVS PDHSHKAGKA CVLKVVWNGL EELKNAIKYT KNLDVLHLGK VWIPHDLRKR
     LNIEMHAVVR ITPVEITPNI PRSLKLQPTE NLSEDVSEED IKTVFYSWLQ QSATTAVPLI
     VSEEEYIKLE MKDGVKEFSL NIVHSWEKEK EENIFLLSTN LLQKMTIQVL LDPMVKEENS
     EEIDFILPFL KLNCLGGVNS LGVSSMEHIT HSLLGRPLSR QLVSLVAGLR NGALLLTGGK
     GSGKSTLAKA ICKEAFDILD AHVEIIDCKA LRGKRLENIQ KTLAAAFSEA LWRQPSVVLL
     DDLDLVVGRS ALPEHEHSPE AIQSQRLAHA LNDLVKEFIS MGSLVALIAT SQSQHSLHPL
     LVSAQGIHIF QCVQHIQPPD QDQRCEILHA IIKNKLDCDM KRFTGLDLQR IAKETEGFVA
     RDFTMLVDRA IHSHLSHQNV YTREELVLTT LDFQKALRGF TPVSLRNVNL HKPRDLGWDR
     IGGLHDVRQI LVDTIQLPAK YPELFANLPI RQRTGVLLYG PPGTGKTLLA GVIARESGMN
     FISVKGPELL SKYIGASEQA VRDVFVRAQA AKPCILFFDE FESIAPRRGH DNTGVTDRVV
     NQLLTQLDGV EGLQGVYVLA ATSRPDLIDP ALLRPGRLDK CVYCPPPDQA SRLEILNVLS
     ESLPLADDVD LQHVASLTDS FTGADLKALL YGAQLEALHG RLLTGGLQDG GSSSDSDLSL
     SSMVFLNHSS GSDDSAGDGE CGLEQSLVSL EMSEVLQDES KFNMYRLYFG SSYESELGNG
     TSSDLSSQCL SAPSSMTQEF PGAPGKDQSL RPPLFRTASQ EGYQELTQEQ RDQLRADISI
     IKGRYRSQTG EDDALNPPGP SKTSLAISQS HLMTALSHTR PSISEDDWKT FAELYESFQN
     PKKRKNQSGT VFRPGQKVTL A
//
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