PEX1_YEAST
ID PEX1_YEAST Reviewed; 1043 AA.
AC P24004; D6VX03;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Peroxisomal ATPase PEX1;
DE AltName: Full=Peroxin-1;
DE AltName: Full=Peroxisomal assembly protein 1;
DE AltName: Full=Peroxisome biogenesis protein PAS1;
GN Name=PEX1; Synonyms=PAS1; OrderedLocusNames=YKL197C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1825027; DOI=10.1016/0092-8674(91)90234-p;
RA Erdmann R., Wiebel F.F., Flessau A., Rytka J., Beyer A., Froehlich K.-U.,
RA Kunau W.-H.;
RT "PAS1, a yeast gene required for peroxisome biogenesis, encodes a member of
RT a novel family of putative ATPases.";
RL Cell 64:499-510(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP MUTAGENESIS OF LYS-467 AND LYS-744.
RX PubMed=7725796; DOI=10.1002/yea.320101210;
RA Krause T., Kunau W.-H., Erdmann R.;
RT "Effect of site-directed mutagenesis of conserved lysine residues upon Pas1
RT protein function in peroxisome biogenesis.";
RL Yeast 10:1613-1620(1994).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP FUNCTION, INTERACTION WITH PEX6, AND MUTAGENESIS OF LYS-467; ASP-525;
RP LYS-744 AND ASP-797.
RX PubMed=15634331; DOI=10.1111/j.1432-1033.2004.04393.x;
RA Birschmann I., Rosenkranz K., Erdmann R., Kunau W.-H.;
RT "Structural and functional analysis of the interaction of the AAA-peroxins
RT Pex1p and Pex6p.";
RL FEBS J. 272:47-58(2005).
RN [8]
RP FUNCTION, INTERACTION WITH PEX6, AND MUTAGENESIS OF LYS-467; ASP-525;
RP LYS-744 AND ASP-797.
RX PubMed=16007078; DOI=10.1038/ncb1281;
RA Platta H.W., Grunau S., Rosenkranz K., Girzalsky W., Erdmann R.;
RT "Functional role of the AAA peroxins in dislocation of the cycling PTS1
RT receptor back to the cytosol.";
RL Nat. Cell Biol. 7:817-822(2005).
RN [9]
RP FUNCTION, AND INTERACTION WITH PEX6.
RX PubMed=16911527; DOI=10.1111/j.1742-4658.2006.05388.x;
RA Rosenkranz K., Birschmann I., Grunau S., Girzalsky W., Kunau W.-H.,
RA Erdmann R.;
RT "Functional association of the AAA complex and the peroxisomal
RT importomer.";
RL FEBS J. 273:3804-3815(2006).
CC -!- FUNCTION: Component of the peroxisomal protein import machinery.
CC Together with PEX6, mediates the ATP-dependent relocation and recycling
CC of the peroxisomal targeting signal-1 (PTS1) import receptor PEX5 from
CC the peroxisomal membrane to the cytosol, where it is then available for
CC another round of protein import into the organelle.
CC {ECO:0000269|PubMed:15634331, ECO:0000269|PubMed:16007078,
CC ECO:0000269|PubMed:16911527}.
CC -!- SUBUNIT: Interacts with PEX6; forms a high-molecular-mass
CC heterooligomer in the cytosol. The PEX1-PEX6 heterooligomers associate
CC with the peroxisomal importomer via interaction of PEX6 with the
CC peroxisomal membrane anchor PEX15. {ECO:0000269|PubMed:15634331,
CC ECO:0000269|PubMed:16007078, ECO:0000269|PubMed:16911527}.
CC -!- INTERACTION:
CC P24004; P33760: PEX6; NbExp=16; IntAct=EBI-13155, EBI-13178;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC Peroxisome membrane {ECO:0000269|PubMed:14562095}; Peripheral membrane
CC protein {ECO:0000269|PubMed:14562095}; Cytoplasmic side
CC {ECO:0000269|PubMed:14562095}. Note=Shuttles between the cytoplasm and
CC the peroxisomal membrane.
CC -!- INDUCTION: By oleate.
CC -!- DOMAIN: AAA-cassette D1 is required for interaction with PEX6. ATP-
CC binding in AAA-cassette D2 is required for interaction with PEX6. ATP-
CC binding and hydrolysis in AAA-cassette D2 is required for proper
CC function in PEX5 dislocation.
CC -!- MISCELLANEOUS: Present with 2100 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; M58676; AAA34842.1; -; Genomic_DNA.
DR EMBL; Z28197; CAA82041.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA08969.1; -; Genomic_DNA.
DR PIR; S38034; S38034.
DR RefSeq; NP_012724.1; NM_001179763.1.
DR AlphaFoldDB; P24004; -.
DR SMR; P24004; -.
DR BioGRID; 33923; 153.
DR ComplexPortal; CPX-1901; Peroxisomal receptor export module complex.
DR DIP; DIP-4266N; -.
DR IntAct; P24004; 9.
DR STRING; 4932.YKL197C; -.
DR TCDB; 3.A.20.1.5; the peroxisomal protein importer (ppi) family.
DR MaxQB; P24004; -.
DR PaxDb; P24004; -.
DR PRIDE; P24004; -.
DR EnsemblFungi; YKL197C_mRNA; YKL197C; YKL197C.
DR GeneID; 853636; -.
DR KEGG; sce:YKL197C; -.
DR SGD; S000001680; PEX1.
DR VEuPathDB; FungiDB:YKL197C; -.
DR eggNOG; KOG0735; Eukaryota.
DR GeneTree; ENSGT00550000075032; -.
DR HOGENOM; CLU_000688_1_1_1; -.
DR InParanoid; P24004; -.
DR OMA; LCYNAYL; -.
DR BioCyc; YEAST:G3O-31959-MON; -.
DR BRENDA; 3.6.4.7; 984.
DR PRO; PR:P24004; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P24004; protein.
DR GO; GO:1904949; C:ATPase complex; IPI:ComplexPortal.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005778; C:peroxisomal membrane; IDA:SGD.
DR GO; GO:0005777; C:peroxisome; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IMP:SGD.
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; IDA:SGD.
DR GO; GO:0043335; P:protein unfolding; IDA:SGD.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
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; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54585; SSF54585; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Membrane; Nucleotide-binding; Peroxisome;
KW Peroxisome biogenesis; Reference proteome; Repeat.
FT CHAIN 1..1043
FT /note="Peroxisomal ATPase PEX1"
FT /id="PRO_0000084606"
FT REGION 453..626
FT /note="AAA-cassette D1"
FT REGION 733..926
FT /note="AAA-cassette D2"
FT BINDING 461..468
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 738..745
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 467
FT /note="K->E: In PEX1pA1; no effect."
FT /evidence="ECO:0000269|PubMed:15634331,
FT ECO:0000269|PubMed:16007078, ECO:0000269|PubMed:7725796"
FT MUTAGEN 525
FT /note="D->Q: In PEX1pB1; no effect."
FT /evidence="ECO:0000269|PubMed:15634331,
FT ECO:0000269|PubMed:16007078"
FT MUTAGEN 744
FT /note="K->E: In PEX1pA2; decreased binding to PEX6. Results
FT in accumulation of PEX5 on peroxisomal membranes."
FT /evidence="ECO:0000269|PubMed:15634331,
FT ECO:0000269|PubMed:16007078, ECO:0000269|PubMed:7725796"
FT MUTAGEN 797
FT /note="D->Q: In PEX1pB2; results in accumulation of PEX5 on
FT peroxisomal membranes."
FT /evidence="ECO:0000269|PubMed:15634331,
FT ECO:0000269|PubMed:16007078"
FT CONFLICT 354
FT /note="S -> T (in Ref. 1; AAA34842)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1043 AA; 117276 MW; EB13C080FB8189DB CRC64;
MTTTKRLKFE NLRIQFSNAI VGNFLRLPHS IINVLESTNY AIQEFGIAVH SHNSDIPIVH
LGWDGHDSGS SENVVLINPV LATVYDLNQK SPLVDLYIQR YDHTHLATEV YVTPETSDDW
EIIDANAMRF QNGEILHQTR IVTPGETLIC YLEGIVTKFK IDRVEPSMKS ARITDGSLVV
VAPKVNKTRL VKAEYGHSNK TILKNGAIQL LKKVILRSTV CKMDFPKDNL FVVYISDGAQ
LPSQKGYASI VKCSLRQSKK SDSDNKSVGI PSKKIGVFIK CDSQIPENHI ALSSHLWDAF
FTHPMNGAKI KLEFLQMNQA NIISGRNATV NIKYFGKDVP TKSGDQYSKL LGGSLLTNNL
ILPTEQIIIE IKKGESEQQL CNLNEISNES VQWKVTQMGK EEVKDIIERH LPKHYHVKET
GEVSRTSKDE DDFITVNSIK KEMVNYLTSP IIATPAIILD GKQGIGKTRL LKELINEVEK
DHHIFVKYAD CETLHETSNL DKTQKLIMEW CSFCYWYGPS LIVLDNVEAL FGKPQANDGD
PSNNGQWDNA SKLLNFFINQ VTKIFNKDNK RIRVLFSGKQ KTQINPLLFD KHFVSETWSL
RAPDKHARAK LLEYFFSKNQ IMKLNRDLQF SDLSLETEGF SPLDLEIFTE KIFYDLQLER
DCDNVVTREL FSKSLSAFTP SALRGVKLTK ETNIKWGDIG ALANAKDVLL ETLEWPTKYE
PIFVNCPLRL RSGILLYGYP GCGKTLLASA VAQQCGLNFI SVKGPEILNK FIGASEQNIR
ELFERAQSVK PCILFFDEFD SIAPKRGHDS TGVTDRVVNQ LLTQMDGAEG LDGVYILAAT
SRPDLIDSAL LRPGRLDKSV ICNIPTESER LDILQAIVNS KDKDTGQKKF ALEKNADLKL
IAEKTAGFSG ADLQGLCYNA YLKSVHRWLS AADQSEVVPG NDNIEYFSIN EHGRREENRL
RLKTLLQQDV VHETKTSTSA ASELTAVVTI NDLLEACQET KPSISTSELV KLRGIYDRFQ
KDRNGEMPNG ENSIDIGSRL SLM
