ID   PEX3_PICAN              Reviewed;         457 AA.
AC   Q01497;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 56.
DE   RecName: Full=Peroxisomal biogenesis factor 3;
DE   AltName: Full=Peroxin-3;
DE   AltName: Full=Peroxisomal membrane protein PER9;
GN   Name=PEX3; Synonyms=PER9;
OS   Pichia angusta (Yeast) (Hansenula polymorpha).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Ogataea.
OX   NCBI_TaxID=870730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 34438 / CBS 4732 / DSM 70277 / JCM 3621 / NBRC 1476 / NRRL
RC   Y-5445;
RX   PubMed=8621531; DOI=10.1074/jbc.271.15.8887;
RA   Baerends R.J.S., Rasmussen S.W., Hilbrands R.E., van der Heide M.,
RA   Faber K.N., Reuvekamp P.T.W., Kiel J.A.K.W., Cregg J.M., van der Klei I.J.,
RA   Veenhuis M.;
RT   "The Hansenula polymorpha PER9 gene encodes a peroxisomal membrane protein
RT   essential for peroxisome assembly and integrity.";
RL   J. Biol. Chem. 271:8887-8894(1996).
CC   -!- FUNCTION: Involved in peroxisome proliferation and/or membrane
CC       biosynthesis. Plays a role in the maintenance of the peroxisomal
CC       membrane in vivo.
CC   -!- SUBCELLULAR LOCATION: Peroxisome membrane; Single-pass membrane
CC       protein.
CC   -!- DOMAIN: The first 16 AA of the protein contain topogenic information
CC       that is able to direct a reporter protein to the ER.
CC   -!- SIMILARITY: Belongs to the peroxin-3 family. {ECO:0000305}.
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DR   EMBL; U37763; AAC49471.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q01497; -.
DR   SMR; Q01497; -.
DR   PhylomeDB; Q01497; -.
DR   GO; GO:0005779; C:integral component of peroxisomal membrane; IEA:InterPro.
DR   GO; GO:0007031; P:peroxisome organization; IEA:UniProtKB-KW.
DR   InterPro; IPR006966; Peroxin-3.
DR   PANTHER; PTHR28080; PTHR28080; 1.
DR   Pfam; PF04882; Peroxin-3; 1.
PE   3: Inferred from homology;
KW   Membrane; Peroxisome; Peroxisome biogenesis; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..457
FT                   /note="Peroxisomal biogenesis factor 3"
FT                   /id="PRO_0000208744"
FT   TOPO_DOM        1..15
FT                   /note="Peroxisomal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        37..457
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   457 AA;  52070 MW;  BC47A9387E63F036 CRC64;
     MFQYCRDLVS RHKKKLLFGT GVIAVSYAVS SFVSNKLAEL NERLKEENFA KEQIKRRFKQ
     TQNDCYMTFL SLLPVLTEPI YEALKVEEIT RELQNKRFER QKAKNAPVGN STDPALSTVL
     SDDFSVHNEK ENPMHTGVQQ TKSKTQLWNE LRNQSITRFL TLLYCESLLI VFLHLQLNIL
     SRRSYLETAI KLASKTKGIK LENESNVDLD PANLFLENDE ELAMGSSRQD ENLAEQAFLS
     YSWWLLNKGW IDIKNQVESS VEDIFGDINP RQELSIEEFA TLINKTQQII DKQIYAEKES
     EPLTAPGHSS STVITSLLPP ANMELFLLQQ TNDMEFLTNF NNNIQNSENV SKLLNELKGY
     LMNDQVSAII SLLVTVGISK VLDNIVVNLM NKQKNPDQEE QVPTEIPKVK LASLLASITK
     QSNQLTNNSL DNEVLYTLNN LQELDDLSAS VYSNFDA