ID A7F816_SCLS1 Unreviewed; 447 AA.
AC A7F816;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Peroxisome assembly protein 12 {ECO:0000256|ARBA:ARBA00018980};
DE AltName: Full=Peroxin-12 {ECO:0000256|ARBA:ARBA00029692};
GN ORFNames=SS1G_13746 {ECO:0000313|EMBL:EDN98887.1};
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079 {ECO:0000313|EMBL:EDN98887.1, ECO:0000313|Proteomes:UP000001312};
RN [1] {ECO:0000313|Proteomes:UP000001312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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}.
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DR EMBL; CH476647; EDN98887.1; -; Genomic_DNA.
DR RefSeq; XP_001585178.1; XM_001585128.1.
DR AlphaFoldDB; A7F816; -.
DR STRING; 665079.A7F816; -.
DR EnsemblFungi; EDN98887; EDN98887; SS1G_13746.
DR GeneID; 5481382; -.
DR KEGG; ssl:SS1G_13746; -.
DR VEuPathDB; FungiDB:sscle_10g079840; -.
DR eggNOG; KOG0826; Eukaryota.
DR HOGENOM; CLU_031067_2_1_1; -.
DR InParanoid; A7F816; -.
DR OMA; RCPITGY; -.
DR OrthoDB; 65730at2759; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:1990429; C:peroxisomal importomer complex; IBA:GO_Central.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016558; P:protein import into peroxisome matrix; IBA:GO_Central.
DR GO; GO:0016562; P:protein import into peroxisome matrix, receptor recycling; IEA:UniProt.
DR GO; GO:0006513; P:protein monoubiquitination; IBA:GO_Central.
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 SUPFAM; SSF57850; RING/U-box; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000001312};
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 21..284
FT /note="Pex N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04757"
FT REGION 306..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 447 AA; 49892 MW; BD98FF536280B3C0 CRC64;
MSSEPPLDPY KPSLFELLSS TQLSSLLPPS LHYLLTIATH RHPRHLLPIL NSFHEIHALL
FLAIEHHYLT TYSSSFVENF YSLKRERALP AAVGDLRLTA EAANASLRET TKLTRGDVWK
NLAVLVGIPY LKRRLDESQE INAPRALLGA NYTRMPPNPT LKQRFLHYYR WFLTNVYPSV
NAAYYFSILA FNLRYLFSGS KSGSGVYSDP FLWLIGTRIR RLSQADFQAF EAIKNAASSI
PGSNLGIRSL LDPRLAMGRI GSGLKLLLPT SIFALKFLEW WHASDFARQL SRKAIEGLEL
PPPIISYTPS PVTKPETTSK SSSEEKQPSE VEEPTNPPIS TITQLPIYVV PAPSTSTSLE
NCPICLEEIT TPTACQTGYV YCYTCIHRWI EGLHDLQEKF MKGDVKVDGE GKGEKGREGK
WESGAGRCAV SGRRVLGGVG GLRRVLV
//
