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Database: UniProt
Entry: A0A2I4AHZ5_AUSLI
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ID   A0A2I4AHZ5_AUSLI        Unreviewed;       408 AA.
AC   A0A2I4AHZ5;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   28-JAN-2026, entry version 35.
DE   RecName: Full=Peroxisomal membrane protein PEX13 {ECO:0000256|ARBA:ARBA00034535};
DE   AltName: Full=Peroxin-13 {ECO:0000256|ARBA:ARBA00029693};
GN   Name=pex13 {ECO:0000313|RefSeq:XP_013855138.1};
OS   Austrofundulus limnaeus (Annual killifish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae;
OC   Austrofundulus.
OX   NCBI_TaxID=52670 {ECO:0000313|Proteomes:UP000192220, ECO:0000313|RefSeq:XP_013855138.1};
RN   [1] {ECO:0000313|RefSeq:XP_013855138.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (AUG-2025) to UniProtKB.
CC   -!- FUNCTION: Component of the PEX13-PEX14 docking complex, a translocon
CC       channel that specifically mediates the import of peroxisomal cargo
CC       proteins bound to PEX5 receptor. The PEX13-PEX14 docking complex forms
CC       a large import pore which can be opened to a diameter of about 9 nm.
CC       Mechanistically, PEX5 receptor along with cargo proteins associates
CC       with the PEX14 subunit of the PEX13-PEX14 docking complex in the
CC       cytosol, leading to the insertion of the receptor into the organelle
CC       membrane with the concomitant translocation of the cargo into the
CC       peroxisome matrix. Involved in the import of PTS1- and PTS2-type
CC       containing proteins. {ECO:0000256|ARBA:ARBA00056165}.
CC   -!- SUBUNIT: Interacts (via SH3 domain) with PEX14 (via SH3-binding motif);
CC       forming the PEX13-PEX14 docking complex. Interacts with PEX19.
CC       {ECO:0000256|ARBA:ARBA00063917}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC       {ECO:0000256|ARBA:ARBA00004585}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004585}.
CC   -!- SIMILARITY: Belongs to the peroxin-13 family.
CC       {ECO:0000256|ARBA:ARBA00006033}.
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DR   RefSeq; XP_013855138.1; XM_013999684.1.
DR   AlphaFoldDB; A0A2I4AHZ5; -.
DR   FunCoup; A0A2I4AHZ5; 773.
DR   STRING; 52670.A0A2I4AHZ5; -.
DR   GeneID; 106510947; -.
DR   KEGG; alim:106510947; -.
DR   CTD; 5194; -.
DR   InParanoid; A0A2I4AHZ5; -.
DR   OrthoDB; 10037838at2759; -.
DR   Proteomes; UP000192220; Unplaced.
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; cd11864; SH3_PEX13_eumet; 1.
DR   FunFam; 2.30.30.40:FF:000109; Peroxisomal biogenesis factor 13; 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; PF14604; SH3_9; 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   Reference proteome {ECO:0000313|Proteomes:UP000192220};
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          267..331
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          25..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          345..370
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          384..408
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        360..369
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        384..395
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   408 AA;  44262 MW;  AF13DDA9E946F7FB CRC64;
     MDSQPPPKPW EGRIPGALSP SISYRSAGFG PATGSPLTSV GHPVLTRMAP PVPPRPVQQS
     YRPSYSSLSS YSPYSSSFYG GGYSPYPYGS SYGLGAYRHF PHTEDVAPSR FVQQAEESSR
     GAFQSIESIV QAFASVSMML DATFSAVYNS FRAVLDVANH LSRLRADLTR VLSAFALVRT
     LRYLYRWLRR LLRSSGGDVE DLWADSMSDA VPAASSRPDG SKEQSVKSWP IFLFFAVVLG
     GPYLIWKLLS SSSGSEDHPS NWASGEDDHV VARAEYDFSA ASDEEISVRA GDVLNLAPKE
     QQPRVRGWLL ASVDGQTTGL VPANYVKVLG RRRGHKAADV QRLVQTTQPS EAAARDQIQD
     PPTASNTAPA EQLLESVYAG SPASFQVETS DSNRSCDAAL TLPEKTDL
//
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