ID A0A9P5G4N6_GEOCN Unreviewed; 387 AA.
AC A0A9P5G4N6;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 12.
DE RecName: Full=Peroxisomal membrane protein PEX13 {ECO:0000256|ARBA:ARBA00034535};
DE AltName: Full=Peroxin-13 {ECO:0000256|ARBA:ARBA00029693};
GN ORFNames=DV451_003336 {ECO:0000313|EMBL:KAF5098602.1};
OS Geotrichum candidum (Oospora lactis) (Dipodascus geotrichum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Dipodascomycetes;
OC Dipodascales; Dipodascaceae; Geotrichum.
OX NCBI_TaxID=1173061 {ECO:0000313|EMBL:KAF5098602.1, ECO:0000313|Proteomes:UP000750522};
RN [1] {ECO:0000313|EMBL:KAF5098602.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=LMA-70 {ECO:0000313|EMBL:KAF5098602.1};
RX PubMed=32457706;
RA Perkins V., Vignola S., Lessard M.H., Plante P.L., Corbeil J.,
RA Dugat-Bony E., Frenette M., Labrie S.;
RT "Phenotypic and Genetic Characterization of the Cheese Ripening Yeast
RT Geotrichum candidum.";
RL Front. Microbiol. 11:0-0(2020).
RN [2] {ECO:0000313|EMBL:KAF5098602.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=LMA-70 {ECO:0000313|EMBL:KAF5098602.1};
RA Perkins V., Lessard M.-H., Dugat-Bony E., Frenette M., Labrie S.;
RL Submitted (JAN-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Interacts (via SH3 domain) with PEX14 (via SH3-binding motif);
CC forming the PEX13-PEX14 docking complex.
CC {ECO:0000256|ARBA:ARBA00065871}.
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC {ECO:0000256|ARBA:ARBA00004549}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004549}.
CC -!- SIMILARITY: Belongs to the peroxin-13 family.
CC {ECO:0000256|ARBA:ARBA00006033}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAF5098602.1}.
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DR EMBL; QQZK01000071; KAF5098602.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9P5G4N6; -.
DR Proteomes; UP000750522; Unassembled WGS sequence.
DR GO; GO:1990429; C:peroxisomal importomer complex; IEA:TreeGrafter.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016560; P:protein import into peroxisome matrix, docking; IEA:InterPro.
DR CDD; cd11771; SH3_Pex13p_fungal; 1.
DR FunFam; 2.30.30.40:FF:000128; Peroxisomal membrane protein (Pex13); 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR007223; Peroxin-13_N.
DR InterPro; IPR035463; Pex13.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR19332; PEROXISOMAL MEMBRANE PROTEIN PEX13; 1.
DR PANTHER; PTHR19332:SF1; PEROXISOMAL MEMBRANE PROTEIN PEX13; 1.
DR Pfam; PF04088; Peroxin-13_N; 1.
DR Pfam; PF07653; SH3_2; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Translocation {ECO:0000256|ARBA:ARBA00023010};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 292..358
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 387 AA; 40894 MW; C16974D2E13BEE5C CRC64;
MSTTAARPTT AAPAAPADPV STTLSTADTA NSPSLPVRPT SLTSGVPNTT SYSPYGATNS
YSSPYGGYGG GSGMYGGTYG GGGMYGNSYG GGMYGNSYGG GMYGGGGMYG NQYAPGGMDP
NGSLHGNLQN STAATFQLIE SVVGAFGGFA QMLNSTYMAT HSSFFAMMSV AEQFAHLRNS
LGSILGVFAI LRWFKRLLAR ASGGKFGSGA SSINAQSFAK FQAKGASPMA AGPRPSFKPL
LFFLAAVFGM PYLLNKLIRA LASQQDQQQQ QFDANGNPLL TDSASGTTID PTKLEFCRAL
YDFVPENPQV ELEMKKGDLI AIIAKTDPLG KPSEWWRVRT RDGRTGYVPS TYVEVITRRI
EPVKAEEETP TEVDEIEVQK AKNRAQS
//
