ID R7SZD2_DICSQ Unreviewed; 372 AA.
AC R7SZD2;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Peroxisome assembly protein 12 {ECO:0000256|ARBA:ARBA00018980, ECO:0000256|PIRNR:PIRNR038074};
DE AltName: Full=Peroxin-12 {ECO:0000256|ARBA:ARBA00029692, ECO:0000256|PIRNR:PIRNR038074};
GN ORFNames=DICSQDRAFT_60738 {ECO:0000313|EMBL:EJF61298.1};
OS Dichomitus squalens (strain LYAD-421) (Western red white-rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Dichomitus.
OX NCBI_TaxID=732165 {ECO:0000313|EMBL:EJF61298.1, ECO:0000313|Proteomes:UP000053319};
RN [1] {ECO:0000313|EMBL:EJF61298.1, ECO:0000313|Proteomes:UP000053319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LYAD-421 SS1 {ECO:0000313|EMBL:EJF61298.1,
RC ECO:0000313|Proteomes:UP000053319};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
CC -!- FUNCTION: Component of a retrotranslocation channel required for
CC peroxisome organization by mediating export of the PEX5 receptor from
CC peroxisomes to the cytosol, thereby promoting PEX5 recycling.
CC {ECO:0000256|PIRNR:PIRNR038074}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBUNIT: Component of the PEX2-PEX10-PEX12 retrotranslocation channel,
CC composed of PEX2, PEX10 and PEX12. {ECO:0000256|ARBA:ARBA00034505}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Peroxisome
CC membrane {ECO:0000256|ARBA:ARBA00004585}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004585}.
CC -!- SIMILARITY: Belongs to the pex2/pex10/pex12 family.
CC {ECO:0000256|ARBA:ARBA00008704, ECO:0000256|PIRNR:PIRNR038074}.
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DR EMBL; JH719411; EJF61298.1; -; Genomic_DNA.
DR RefSeq; XP_007366127.1; XM_007366065.1.
DR AlphaFoldDB; R7SZD2; -.
DR GeneID; 18842993; -.
DR KEGG; dsq:DICSQDRAFT_60738; -.
DR HOGENOM; CLU_031067_0_0_1; -.
DR OMA; RCPITGY; -.
DR OrthoDB; 65730at2759; -.
DR Proteomes; UP000053319; Unassembled WGS sequence.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016562; P:protein import into peroxisome matrix, receptor recycling; IEA:UniProt.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProt.
DR CDD; cd16451; mRING_PEX12; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR017375; PEX12.
DR InterPro; IPR006845; Pex_N.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12888:SF0; PEROXISOME ASSEMBLY PROTEIN 12; 1.
DR PANTHER; PTHR12888; PEROXISOME ASSEMBLY PROTEIN 12 PEROXIN-12; 1.
DR Pfam; PF04757; Pex2_Pex12; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR PIRSF; PIRSF038074; Peroxisome_assembly_p12; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR038074};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140, ECO:0000256|PIRNR:PIRNR038074};
KW Reference proteome {ECO:0000313|Proteomes:UP000053319};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Transport {ECO:0000256|ARBA:ARBA00022448};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 22..281
FT /note="Pex N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04757"
SQ SEQUENCE 372 AA; 43336 MW; 3D45FCE486A67E71 CRC64;
MEFFNDAGDD PLKPTLFELV AQEQLRDLLQ PALKYVLSVF AQSYPRYLLR IVNKHEEFYA
LLMFFVERHY LRAHGASFAE NFYGLKRRRV PLFKTERARS AVGGVFPEEK LRDRDIWRSL
LFLVGLPYVR AKAQDYYEEL GGGLQTDLIE DTRPIPVDEV RATQEQTWKG RLKRAYKAAY
PWLNTSFEVW LLVYNIAYLF ERTPYYRPWL SWVGVDLRRV SAEDLRAAQV AVRTPPAPKP
RGVLESLTRV LRRSPRLLLD SLKVLLPTAI FFIKFLEWWY SPSSPARSLS TSPLGPVVPP
PRLHPPHPQG IRVDDVEYGM CPLCRKQIAN ATAFPSGYVF CYRCAHDWVE KDGRCPVTLV
RTRMWQLRKI LV
//
