ID   PEX10_PICAN             Reviewed;         295 AA.
AC   Q00940;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Peroxisome biogenesis factor 10;
DE   AltName: Full=Peroxin-10;
DE   AltName: Full=Peroxisomal biogenesis factor 10;
DE   AltName: Full=Peroxisome assembly protein 10;
DE   AltName: Full=Peroxisome assembly protein PER8;
GN   Name=PEX10; Synonyms=PER8;
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=7844145; DOI=10.1083/jcb.128.3.307;
RA   Tan X., Waterham H.R., Veenhuis M., Cregg J.M.;
RT   "The Hansenula polymorpha PER8 gene encodes a novel peroxisomal integral
RT   membrane protein involved in proliferation.";
RL   J. Cell Biol. 128:307-319(1995).
CC   -!- FUNCTION: Somewhat implicated in the biogenesis of peroxisomes. It
CC       plays an important role in the regulation of peroxisome proliferation.
CC       May interact with PER1 (PEX8).
CC   -!- SUBCELLULAR LOCATION: Peroxisome membrane; Peripheral membrane protein.
CC   -!- SIMILARITY: Belongs to the pex2/pex10/pex12 family. {ECO:0000305}.
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DR   EMBL; Z38001; CAA86101.1; -; Genomic_DNA.
DR   PIR; A56488; A56488.
DR   AlphaFoldDB; Q00940; -.
DR   SMR; Q00940; -.
DR   GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007031; P:peroxisome organization; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR006845; Pex_N.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   Pfam; PF04757; Pex2_Pex12; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Membrane; Metal-binding; Peroxisome; Peroxisome biogenesis; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..295
FT                   /note="Peroxisome biogenesis factor 10"
FT                   /id="PRO_0000056378"
FT   ZN_FING         245..283
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
SQ   SEQUENCE   295 AA;  34002 MW;  5027E9CD5BC86D6D CRC64;
     MFKLLSFANA PAIVRANQKD SYFESRLHNQ LLDVVKAIKG SHFVHKYPEE LRTLATALYL
     CLTTLVGSKT LGEEYVDLVY VSRDGRKIPK FASRFGFVVA YVLFPYAVRQ LLQKLKAQQS
     RLAQLVSGVS YMNVMDLLNL HLALFYFTGK YYQFAKRLFG LRYAFGYRVD KNQQRARGNY
     ELLGLLIIFQ TVFKNVANLR KLWGATKTVQ DSGDLIYRFR DQTSDVIDLA DPKVLPYLPE
     ASRTCMLCLS PMKDPSCGEC GHVFCWKCVL DWVKERQECP LCRAKMRESQ LLPLR