ID   PEX3_YARLI              Reviewed;         431 AA.
AC   Q874C0; Q6C0Q8;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Peroxisomal biogenesis factor 3;
DE   AltName: Full=Peroxin-3;
GN   Name=PEX3; OrderedLocusNames=YALI0F22539g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=12631715; DOI=10.1091/mbc.e02-10-0633;
RA   Bascom R.A., Chan H., Rachubinski R.A.;
RT   "Peroxisome biogenesis occurs in an unsynchronized manner in close
RT   association with the endoplasmic reticulum in temperature-sensitive
RT   Yarrowia lipolytica Pex3p mutants.";
RL   Mol. Biol. Cell 14:939-957(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Involved in peroxisome biosynthesis. Seems to directly or
CC       indirectly sequesters components of the peroxisome biogenesis
CC       machinery. {ECO:0000269|PubMed:12631715}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome membrane; Single-pass membrane
CC       protein.
CC   -!- SIMILARITY: Belongs to the peroxin-3 family. {ECO:0000305}.
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DR   EMBL; AF474003; AAO33094.1; -; Genomic_DNA.
DR   EMBL; CR382132; CAG78565.1; -; Genomic_DNA.
DR   RefSeq; XP_505754.1; XM_505754.1.
DR   AlphaFoldDB; Q874C0; -.
DR   SMR; Q874C0; -.
DR   STRING; 4952.CAG78565; -.
DR   EnsemblFungi; CAG78565; CAG78565; YALI0_F22539g.
DR   GeneID; 2908532; -.
DR   KEGG; yli:YALI0F22539g; -.
DR   VEuPathDB; FungiDB:YALI0_F22539g; -.
DR   HOGENOM; CLU_017002_3_0_1; -.
DR   InParanoid; Q874C0; -.
DR   OMA; WSLQMAI; -.
DR   Proteomes; UP000001300; Chromosome F.
DR   GO; GO:0005779; C:integral component of peroxisomal membrane; IBA:GO_Central.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
DR   GO; GO:0045046; P:protein import into peroxisome membrane; IBA:GO_Central.
DR   InterPro; IPR006966; Peroxin-3.
DR   PANTHER; PTHR28080; PTHR28080; 1.
DR   Pfam; PF04882; Peroxin-3; 2.
PE   3: Inferred from homology;
KW   Membrane; Peroxisome; Peroxisome biogenesis; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..431
FT                   /note="Peroxisomal biogenesis factor 3"
FT                   /id="PRO_0000208746"
FT   TOPO_DOM        1..10
FT                   /note="Peroxisomal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        11..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        29..431
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          95..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..126
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   431 AA;  47943 MW;  0159C4DDF00CFE83 CRC64;
     MDFFRRHQKK VLALVGVALS SYLFIDYVKK KFFEIQGRLS SERTAKQNLR RRFEQNQQDA
     DFTIMALLSS LTTPVMERYP VDQIKAELQS KRRPTDRVLA LESSTSSSAT AQTVPTMTSG
     ATEEGEKSKT QLWQDLKRTT ISRAFSLVYA DALLIFFTRL QLNILGRRNY VNSVVALAQQ
     GREGNAEGRV APSFGDLADM GYFGDLSGSS SFGETIVDPD LDEQYLTFSW WLLNEGWVSL
     SERVEEAVRR VWDPVSPKAE LGFDELSELI GRTQMLIDRP LNPSSPLNFL SQLLPPREQE
     EYVLAQNPSD TAAPIVGPTL RRLLDETADF IESPNAAEVI ERLVHSGLSV FMDKLAVTFG
     ATPADSGSPY PVVLPTAKVK LPSILANMAR QAGGMAQGSP GVENEYIDVM NQVQELTSFS
     AVVYSSFDWA L