PEX6_YEAST
ID PEX6_YEAST Reviewed; 1030 AA.
AC P33760; D6W0L8;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Peroxisomal ATPase PEX6;
DE AltName: Full=Peroxin-6;
DE AltName: Full=Peroxisomal assembly protein 8;
DE AltName: Full=Peroxisome biosynthesis protein PAS8;
GN Name=PEX6; Synonyms=PAS8; OrderedLocusNames=YNL329C; ORFNames=N0310;
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.
RX PubMed=8241279; DOI=10.1016/0167-4781(93)90166-b;
RA Voorn-Brouwer T., van der Leij I., Hemrika W., Distel B., Tabak H.F.;
RT "Sequence of the PAS8 gene, the product of which is essential for
RT biogenesis of peroxisomes in Saccharomyces cerevisiae.";
RL Biochim. Biophys. Acta 1216:325-328(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S288c / FY1676;
RX PubMed=7645347; DOI=10.1002/yea.320110606;
RA Maftahi M., Nicaud J.-M., Levesque H., Gaillardin C.;
RT "Sequencing analysis of a 15.4 kb fragment of yeast chromosome XIV
RT identifies the RPD3, PAS8 and KRE1 loci, five new open reading frames.";
RL Yeast 11:567-572(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 142-1030.
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8533474; DOI=10.1002/yea.320111010;
RA van Dyck L., Pascual-Ahuir A., Purnelle B., Goffeau A.;
RT "An 8.2 kb DNA segment from chromosome XIV carries the RPD3 and PAS8 genes
RT as well as the Saccharomyces cerevisiae homologue of the thiamine-repressed
RT nmt1 gene and a chromosome III-duplicated gene for a putative aryl-alcohol
RT dehydrogenase.";
RL Yeast 11:987-991(1995).
RN [6]
RP INTERACTION WITH PEX15, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-489;
RP LYS-778 AND ASP-831.
RX PubMed=12808025; DOI=10.1091/mbc.e02-11-0752;
RA Birschmann I., Stroobants A.K., van den Berg M., Schaefer A.,
RA Rosenkranz K., Kunau W.-H., Tabak H.F.;
RT "Pex15p of Saccharomyces cerevisiae provides a molecular basis for
RT recruitment of the AAA peroxin Pex6p to peroxisomal membranes.";
RL Mol. Biol. Cell 14:2226-2236(2003).
RN [7]
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 [8]
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 [9]
RP FUNCTION, INTERACTION WITH PEX1, AND MUTAGENESIS OF LYS-489; LYS-778 AND
RP ASP-831.
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 [10]
RP FUNCTION, INTERACTION WITH PEX1, AND MUTAGENESIS OF LYS-489; LYS-778 AND
RP ASP-831.
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 [11]
RP FUNCTION.
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 PEX1, 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 PEX1; forms a high-molecular-mass
CC heterooligomer in the cytosol. Interacts with PEX15; anchors PEX1-PEX6
CC heterooligomers to the peroxisomal membrane and mediates their
CC association with the peroxisomal importomer.
CC {ECO:0000269|PubMed:12808025, ECO:0000269|PubMed:15634331,
CC ECO:0000269|PubMed:16007078}.
CC -!- INTERACTION:
CC P33760; P24004: PEX1; NbExp=16; IntAct=EBI-13178, EBI-13155;
CC P33760; P53112: PEX14; NbExp=6; IntAct=EBI-13178, EBI-13212;
CC P33760; Q08215: PEX15; NbExp=14; IntAct=EBI-13178, EBI-31849;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12808025}.
CC Peroxisome membrane {ECO:0000269|PubMed:12808025,
CC ECO:0000269|PubMed:14562095}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12808025}; Cytoplasmic side
CC {ECO:0000269|PubMed:12808025}. Note=Shuttles between the cytoplasm and
CC the peroxisomal membrane (PubMed:12808025).
CC {ECO:0000269|PubMed:12808025}.
CC -!- DOMAIN: AAA-cassette D1 is required for interaction with PEX1. ATP-
CC binding in AAA-cassette D1 is required for attachment to PEX15. ATP-
CC binding and hydrolysis in AAA-cassette D2 is required for release from
CC PEX15 and proper function in PEX5 dislocation.
CC -!- MISCELLANEOUS: Present with 1630 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; L20789; AAA16574.1; -; Unassigned_DNA.
DR EMBL; Z46259; CAA86369.1; -; Genomic_DNA.
DR EMBL; Z71605; CAA96261.1; -; Genomic_DNA.
DR EMBL; X83226; CAA58229.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10234.1; -; Genomic_DNA.
DR PIR; S43211; S43211.
DR RefSeq; NP_014070.1; NM_001183167.1.
DR AlphaFoldDB; P33760; -.
DR SMR; P33760; -.
DR BioGRID; 35512; 85.
DR ComplexPortal; CPX-1901; Peroxisomal receptor export module complex.
DR DIP; DIP-2621N; -.
DR IntAct; P33760; 15.
DR MINT; P33760; -.
DR STRING; 4932.YNL329C; -.
DR TCDB; 3.A.20.1.5; the peroxisomal protein importer (ppi) family.
DR MaxQB; P33760; -.
DR PaxDb; P33760; -.
DR PRIDE; P33760; -.
DR EnsemblFungi; YNL329C_mRNA; YNL329C; YNL329C.
DR GeneID; 855387; -.
DR KEGG; sce:YNL329C; -.
DR SGD; S000005273; PEX6.
DR VEuPathDB; FungiDB:YNL329C; -.
DR eggNOG; KOG0736; Eukaryota.
DR GeneTree; ENSGT00550000074953; -.
DR HOGENOM; CLU_000688_0_4_1; -.
DR InParanoid; P33760; -.
DR OMA; DSMLNAM; -.
DR BioCyc; YEAST:G3O-33313-MON; -.
DR BRENDA; 3.6.4.7; 984.
DR PRO; PR:P33760; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P33760; protein.
DR GO; GO:1904949; C:ATPase complex; IPI:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005778; C:peroxisomal membrane; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; IDA: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; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00004; AAA; 2.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Membrane; Nucleotide-binding; Peroxisome;
KW Peroxisome biogenesis; Reference proteome.
FT CHAIN 1..1030
FT /note="Peroxisomal ATPase PEX6"
FT /id="PRO_0000084621"
FT REGION 478..683
FT /note="AAA-cassette D1"
FT REGION 767..956
FT /note="AAA-cassette D2"
FT BINDING 772..779
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 489
FT /note="K->A: In PEX6pA1; decreased binding to PEX15."
FT /evidence="ECO:0000269|PubMed:12808025,
FT ECO:0000269|PubMed:15634331, ECO:0000269|PubMed:16007078"
FT MUTAGEN 778
FT /note="K->A: In PEX6pA2; increased amount of peroxisome-
FT bound PEX6. Results in accumulation of PEX5 on peroxisomal
FT membranes."
FT /evidence="ECO:0000269|PubMed:12808025,
FT ECO:0000269|PubMed:15634331, ECO:0000269|PubMed:16007078"
FT MUTAGEN 831
FT /note="D->Q: In PEX6pB2; increased amount of peroxisome-
FT bound PEX6. Results in accumulation of PEX5 on peroxisomal
FT membranes."
FT /evidence="ECO:0000269|PubMed:12808025,
FT ECO:0000269|PubMed:15634331, ECO:0000269|PubMed:16007078"
SQ SEQUENCE 1030 AA; 115571 MW; 736FECB57BBFF8F8 CRC64;
MKASLTFSLS GIYAPCSISR DIYLEYGDKK AECLYGTIRL PQYGPGCTPG KIVHCVLDDS
LPFCSIVVPS KLFGFMPTQP TMDFCYFEPI LDNVVPVLDS VTFLINEQLY SKLMDLPQEM
QQIQFLHYKY NINSMETVVH SRDILTSGLC QILNCSPFPQ GLVDFTETQL ILVNDTEQKL
SALKYANEDE EYALPKIGTN SALSIDLESL PCTISRDLLR PAPHINDDNS IYAFTDAETL
LRLDVTSGSF ITVSNMGCVR LVKLFVLLLP NGFKKRTIYA PPKIIASFPD CSVVTISKSN
IGHTDIPIAN QVFISRVGGW LQSQKCFQNI ILTTLKKFFS ESKRILCQND LIPIAFDSSM
ADLNIAEEND ESDDEDELGQ YYKNDSLVWF FVTSAELDCF SKDNSHFIID PNRTKLITTN
ITNRRPLPLS RSNLQRYYGF AETFYYDLHI FPYVRQLVNI LETSFNCSQR GITLNASVLL
HSTTNNVGKA TMVRFASKYL GIHLLEIDCL SLTSNSRQLD STSKIIGYIR AKCENVLPYA
SPAVIFLAHL DSILLDVNAN QDPEAIKLQK SINFEMSKLL DDFTFKFPGT TFVGSVNNID
NVPSSFRSHM RFEILVPVPS EAQRLRIFQW YLSSHELNRD VQQKVPVSYM DNISFSSLSS
YSAGLTPLDI KSIVETARMT ATARFYQESK KCGWLPQSIL ITQEDLSKAT SKARNEFSVS
IGAPQIPNVT WDDIGGIDFV KGEILDTIDM PLKHPELFTS GMKKRSGILF YGPPGTGKTL
MAKAIATNFS LNFFSVKGPE LLNMYIGESE ANVRRVFQKA REAKPCVIFF DEIDSVAPKR
GNQGDSGGVM DRIVSQLLAE LDGMSTDADG VFVIGATNRP DLLDEALLRP GRFDKLLYLG
IPDTDTKQLN ILEALTRKFV LDNDVKLIEL AKLCPFNYTG ADFYALCSDA MLNAMSRIAR
MVEKKVSQHN ELTGENISTR RWFDKIATKE DTKVVVKMED FLKAQEQLTP SVSRAELNHY
EAVRANFEGA
