ID W6MF92_9ASCO Unreviewed; 367 AA.
AC W6MF92;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=KUCA_T00000091001 {ECO:0000313|EMBL:CDK24131.1};
OS Kuraishia capsulata CBS 1993.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetales incertae sedis; Kuraishia.
OX NCBI_TaxID=1382522 {ECO:0000313|EMBL:CDK24131.1};
RN [1] {ECO:0000313|EMBL:CDK24131.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK24131.1};
RA Genoscope - CEA;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDK24131.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK24131.1};
RA Morales L., Noel B., Porcel B., Marcet-Houben M., Hullo M-F., Sacerdot C.,
RA Tekaia F., Leh-Louis V., Despons L., Khanna V., Aury J-M., Barbe V.,
RA Couloux A., Labadie K., Pelletier E., Souciet J-L., Boekhout T.,
RA Gabaldon T., Wincker P., Dujon B.;
RT "Complete DNA sequence of /Kuraishia capsulata/ illustrates novel genomic
RT features among budding yeasts (/Saccharomycotina/).";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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; HG793125; CDK24131.1; -; Genomic_DNA.
DR AlphaFoldDB; W6MF92; -.
DR STRING; 1382522.W6MF92; -.
DR HOGENOM; CLU_031067_0_0_1; -.
DR OrthoDB; 65730at2759; -.
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; IPR001841; Znf_RING.
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.
DR PROSITE; PS50089; ZF_RING_2; 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 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, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 304..342
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 367 AA; 42955 MW; AF955B2DEDD15DF9 CRC64;
MDYYSNLSGT FDSTPTLFEI ISSNELQDLL SPSLRYVLIY YTHRYPHLLL KFTNRFDELN
LLLRGLIEYR FLKKWNSTFT EKFYGLKRQN SNGIKLSFDP GQRLTKKQIY ASWIELMLAP
YLKEKLDVLH EYLYPQALMS RIKNDSWQNW LRLKFIKLYP IVKAAVKLVN LVLQLLYLSG
DVKSPSLIMW LLKINYSRFN SLDYERAESG SDSGKLSSPS HRIRPVTLNE SLYNFTARSS
TTLRRSLMMA GNSIFPAMIF SLKIMEWWNS SDFAKLLQND QNLMGLKLAP PMLNTEYRTT
EKECPLCKKE LTNPSIIETG YVFCHSCIFP YLQEHGKCPI TEKHLHGCKW NESSKNWDVL
GVRKLIL
//
