PEX13_PICPA
ID PEX13_PICPA Reviewed; 380 AA.
AC Q92266;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Peroxisomal membrane protein PEX13;
DE AltName: Full=Peroxin-13;
GN Name=PEX13;
OS Komagataella pastoris (Yeast) (Pichia pastoris).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Komagataella.
OX NCBI_TaxID=4922;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS.
RX PubMed=8858165; DOI=10.1083/jcb.135.1.85;
RA Gould S.J., Kalish J.E., Morrell J.C., Bjoerkman J., Urquhart A.J.,
RA Crane D.I.;
RT "Pex13p is an SH3 protein of the peroxisome membrane and a docking factor
RT for the predominantly cytoplasmic PTs1 receptor.";
RL J. Cell Biol. 135:85-95(1996).
CC -!- FUNCTION: Component of the peroxisomal translocation machinery with
CC PEX14 and PEX17. Interacts with the PTS1 receptor (PAS10/PEX5).
CC Involved in the import of PTS1 and PTS2 proteins.
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane; Single-pass membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=PEX13L;
CC IsoId=Q92266-1; Sequence=Displayed;
CC Name=PEX13S;
CC IsoId=Q92266-2; Sequence=VSP_018788;
CC -!- SIMILARITY: Belongs to the peroxin-13 family. {ECO:0000305}.
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DR EMBL; U70067; AAB09087.1; -; Genomic_DNA.
DR AlphaFoldDB; Q92266; -.
DR SMR; Q92266; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016560; P:protein import into peroxisome matrix, docking; IEA:InterPro.
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; PTHR19332; 1.
DR Pfam; PF04088; Peroxin-13_N; 1.
DR Pfam; PF14604; SH3_9; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Alternative initiation; Membrane; Peroxisome; Protein transport;
KW SH3 domain; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..380
FT /note="Peroxisomal membrane protein PEX13"
FT /id="PRO_0000022039"
FT TOPO_DOM 1..230
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 252..380
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 277..344
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..32
FT /note="Missing (in isoform PEX13S)"
FT /evidence="ECO:0000305"
FT /id="VSP_018788"
FT MUTAGEN 286
FT /note="Y->A: No effect on activity."
FT /evidence="ECO:0000269|PubMed:8858165"
FT MUTAGEN 287
FT /note="D->A: No effect on activity."
FT /evidence="ECO:0000269|PubMed:8858165"
FT MUTAGEN 288
FT /note="F->A: No effect on activity."
FT /evidence="ECO:0000269|PubMed:8858165"
FT MUTAGEN 291
FT /note="E->K: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:8858165"
FT MUTAGEN 296
FT /note="E->K: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:8858165"
SQ SEQUENCE 380 AA; 40695 MW; EEBABC39F93BA832 CRC64;
MSDSSAPDLP SKPSSLNAGQ SSSLQTTNTG IGMGSGMGSG MGMGTYGNSY GSSYGGGYGS
SMYGSGGYGM GGYGSSMYGG SRYGMGSYGM GGYGMGGYGM GMNTGMNGMG MAGSLAQGSE
ATFQLIESII GAVGGFAQVL EATYMATHSS FFTMISMADQ LSHLKTALGS MLGIYTVINW
LKRIMGKLMG VKNKLTPDEF RKFQEKQMKK LSNSNNTGGP NKNTNKLSLK PLLLFLAAVV
GFPYLLKKLI AHLAETSQMN GNFITSGGSL QGNLDPTKLE FARALYDFNP ENEEMELKLA
RGELMAILSK TEPNSNQEST WWKCRSRDGK VGFVPYNYVE IIERHQRPVP EAQEEPAAAV
LAERQQQPII DSTEFQKMKT