ID   PEX2_PODAS              Reviewed;         554 AA.
AC   P51021;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Peroxisomal biogenesis factor 2;
DE   AltName: Full=Peroxin-2;
DE   AltName: Full=Peroxisomal protein CAR1;
GN   Name=PEX2; Synonyms=CAR1;
OS   Podospora anserina (Pleurage anserina).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Podosporaceae; Podospora.
OX   NCBI_TaxID=2587412;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=s;
RX   PubMed=7600573; DOI=10.1016/s0092-8674(05)80009-1;
RA   Berteaux-Lecellier V., Picard M., Thomson-Coffe C., Zickler D.,
RA   Panvier-Adoutte A., Simonet J.-M.;
RT   "A nonmammalian homolog of the PAF1 gene (Zellweger syndrome) discovered as
RT   a gene involved in caryogamy in the fungus Podospora anserina.";
RL   Cell 81:1043-1051(1995).
CC   -!- FUNCTION: Involved in caryogamy (nuclear fusion), a process required
CC       for sexual sporulation.
CC   -!- SUBCELLULAR LOCATION: Peroxisome membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the pex2/pex10/pex12 family. {ECO:0000305}.
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DR   EMBL; X87329; CAA60739.1; -; Genomic_DNA.
DR   PIR; A56730; A56730.
DR   AlphaFoldDB; P51021; -.
DR   VEuPathDB; FungiDB:PODANS_1_2750; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR006845; Pex_N.
DR   Pfam; PF04757; Pex2_Pex12; 1.
PE   3: Inferred from homology;
KW   Membrane; Metal-binding; Peroxisome; Transmembrane; Transmembrane helix;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..554
FT                   /note="Peroxisomal biogenesis factor 2"
FT                   /id="PRO_0000056373"
FT   TRANSMEM        256..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        307..325
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         366..435
FT                   /note="RING-type; atypical"
FT   REGION          1..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          470..554
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..58
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        480..510
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        525..554
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   554 AA;  61534 MW;  8B78AA52D5E4BFBB CRC64;
     MSDSKPPKDS SSPSAAVPDV AAAAASSTPT PAPVAITPPS NPQSAHSFAQ AQQRLIARRQ
     TRDAQEAARV AAQQSESQLR ARIAASQSPL LRRLGASTLS LWDTISSREG TRPAFRVGQV
     DAELLDEELV ELMKGQVGEA VRYYGGGGGG DNNIKHEWDA EISLALRAVI FKLTIWDHDA
     TYGAALQNLK YTDARHTGSV LVPPSKWQKG LYGLMTVGGR YMWSKWENWL REQDGGYDEP
     SPTVQRLSSM TDRLSTLHAA ASFASFLVFL LQGRYRTLLD RVLRMRLAPP TSQVSREVSF
     EYLNRQLVWH AFTEFLLFVL PLVGINRWRR WLARTWRKTK KIMSTTGGEG AEEKKGEFAF
     LPERTCAICY QDQNQATNEN ELMAAATSKT GVVGSAQTDV TNPYETIPCG CVYCFVCLAT
     RIEREEGEGW NCLRCGELVK ECKPWSGDVL EHESKSPAQK TVVFADDVKD ASDDEQENSQ
     VLVQQEDDDE YPEEEGEEGG EEEEEEEEGS RSLEDLRTES ASEESSEQEA DSEGDESEDY
     EAEEEELGAD LDED