ID PEX13_YEAST Reviewed; 386 AA. AC P80667; D6VYJ4; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 04-NOV-2026, entry version 195. DE RecName: Full=Peroxisomal membrane protein PEX13 {ECO:0000305}; DE AltName: Full=Peroxin-13 {ECO:0000305}; GN Name=PEX13 {ECO:0000303|PubMed:8858166, ECO:0000312|SGD:S000004181}; GN Synonyms=PAS20; OrderedLocusNames=YLR191W; ORFNames=L9470.1; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8858166; DOI=10.1083/jcb.135.1.97; RA Elgersma Y., Kwast L., Klein A., Voorn-Brouwer T., van den Berg M., RA Tabak H.F., Distel B.; RT "The SH3 domain of the Saccharomyces cerevisiae peroxisomal membrane RT protein Pex13p functions as a docking site for Pex5p, a mobile receptor for RT the import PTS1-containing proteins."; RL J. Cell Biol. 135:97-109(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169871; DOI=10.1038/387s087; RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J., RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., RA Zollner A., Hani J., Hoheisel J.D.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."; RL Nature 387:87-90(1997). RN [3] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [4] RP PARTIAL PROTEIN SEQUENCE, FUNCTION, AND SUBCELLULAR LOCATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=8858167; DOI=10.1083/jcb.135.1.111; RA Erdmann R., Blobel G.; RT "Identification of Pex13p a peroxisomal membrane receptor for the PTS1 RT recognition factor."; RL J. Cell Biol. 135:111-121(1996). RN [5] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [6] RP FUNCTION, AND INTERACTION WITH PEX13. RX PubMed=20154681; DOI=10.1038/ncb2027; RA Meinecke M., Cizmowski C., Schliebs W., Krueger V., Beck S., Wagner R., RA Erdmann R.; RT "The peroxisomal importomer constitutes a large and highly dynamic pore."; RL Nat. Cell Biol. 12:273-277(2010). RN [7] RP MUTAGENESIS OF 10-LYS--GLU-13. RX PubMed=40739340; DOI=10.1038/s41556-025-01711-z; RA Chen W.W., Rodrigues T.A., Wendscheck D., Pedrosa A.G., Yang C., RA Francisco T., Moecklinghoff T., Zografakis A., Nunes-Silva B., RA Avraham R.E., Silva A.R., Ferreira M.J., Das H., Koster J., Neuwirth S., RA Bender J., Oeljeklaus S., Sondhi V., Gatsogiannis C., Schuldiner M., RA Zalckvar E., Hofmann K., Waterham H.R., DeBerardinis R.J., Azevedo J.E., RA Warscheid B.; RT "PEX39 facilitates the peroxisomal import of PTS2-containing proteins."; RL Nat. Cell Biol. 27:1256-1271(2025). RN [8] {ECO:0007744|PDB:1N5Z} RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH PEX14 SH3 DOMAIN. RX PubMed=12453410; DOI=10.1016/s1097-2765(02)00749-9; RA Douangamath A., Filipp F.V., Klein A.T., Barnett P., Zou P., RA Voorn-Brouwer T., Vega M.C., Mayans O.M., Sattler M., Distel B., RA Wilmanns M.; RT "Topography for independent binding of alpha-helical and PPII-helical RT ligands to a peroxisomal SH3 domain."; RL Mol. Cell 10:1007-1017(2002). 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 or the PEX7-PEX21 or PEX7-PEX18 CC receptor complex (PubMed:20154681, PubMed:8858167). The PEX13-PEX14 CC docking complex forms a large import pore which can be opened to a CC diameter of about 9 nm (PubMed:20154681). Mechanistically, PEX5 (or CC PEX7-PEX21) receptor along with cargo proteins associates with the CC PEX14 subunit of the PEX13-PEX14 docking complex in the cytosol, CC leading to the insertion of the receptor into the organelle membrane CC with the concomitant translocation of the cargo into the peroxisome CC matrix (PubMed:20154681). {ECO:0000269|PubMed:20154681, CC ECO:0000269|PubMed:8858167}. CC -!- SUBUNIT: Component of the PEX13-PEX14 docking complex, composed of CC PEX13, PEX14 and PEX17 (PubMed:12453410, PubMed:20154681). Interacts CC (via SH3 domain) with PEX14 (via SH3-binding motif) (PubMed:12453410, CC PubMed:20154681). {ECO:0000269|PubMed:12453410, CC ECO:0000269|PubMed:20154681}. CC -!- INTERACTION: CC P80667; P53933: APP1; NbExp=2; IntAct=EBI-13206, EBI-28798; CC P80667; P53901: INN1; NbExp=2; IntAct=EBI-13206, EBI-28955; CC P80667; Q12446: LAS17; NbExp=2; IntAct=EBI-13206, EBI-10022; CC P80667; Q05568: PEX10; NbExp=8; IntAct=EBI-13206, EBI-13194; CC P80667; Q04370: PEX12; NbExp=7; IntAct=EBI-13206, EBI-2077297; CC P80667; P53112: PEX14; NbExp=18; IntAct=EBI-13206, EBI-13212; CC P80667; P32800: PEX2; NbExp=10; IntAct=EBI-13206, EBI-13160; CC P80667; P35056: PEX5; NbExp=6; IntAct=EBI-13206, EBI-13170; CC P80667; P40494: PRK1; NbExp=2; IntAct=EBI-13206, EBI-9703; CC P80667; Q03497: STE20; NbExp=3; IntAct=EBI-13206, EBI-18285; CC P80667; P25604: STP22; NbExp=2; IntAct=EBI-13206, EBI-411625; CC P80667; P40453: UBP7; NbExp=2; IntAct=EBI-13206, EBI-19857; CC -!- SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|PubMed:8858167}; CC Single-pass membrane protein {ECO:0000305}. CC -!- MISCELLANEOUS: Present with 7900 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the peroxin-13 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; S82971; AAB46885.1; -; Genomic_DNA. DR EMBL; U37420; AAA79308.1; -; Genomic_DNA. DR EMBL; U17246; AAB67453.1; -; Genomic_DNA. DR EMBL; U14913; AAB67448.1; -; Genomic_DNA. DR EMBL; BK006945; DAA09510.1; -; Genomic_DNA. DR PIR; S51436; S51436. DR RefSeq; NP_013292.1; NM_001182078.1. DR PDB; 1JQQ; X-ray; 2.65 A; A/B/C/D=299-386. DR PDB; 1N5Z; X-ray; 2.70 A; A/B=299-386. DR PDB; 1NM7; NMR; -; A=310-370. DR PDB; 2V1R; X-ray; 2.10 A; A/B=299-374. DR SMR; P80667; -. DR BioGRID; 31461; 283. DR ComplexPortal; CPX-1904; Peroxisomal PEX13-PEX14-PEX17 docking complex. DR DIP; DIP-2473N; -. DR ELM; P80667; -. DR IntAct; P80667; 80. DR STRING; 4932.YLR191W; -. DR TCDB; 3.A.20.1.5; the peroxisomal protein importer (ppi) family. DR iPTMnet; P80667; -. DR PaxDb; 4932-YLR191W; -. DR PeptideAtlas; P80667; -. DR EnsemblFungi; YLR191W_mRNA; YLR191W; YLR191W. DR GeneID; 850888; -. DR KEGG; sce:YLR191W; -. DR VEuPathDB; FungiDB:YLR191W; -. DR AGR; SGD:S000004181; -. DR SGD; S000004181; PEX13. DR eggNOG; KOG3875; Eukaryota. DR HOGENOM; CLU_034386_2_0_1; -. DR InParanoid; P80667; -. DR OMA; AAFMHGR; -. DR OrthoDB; 10037838at2759; -. DR BioCyc; YEAST:G3O-32313-MONOMER; -. DR Reactome; R-SCE-9033241; Peroxisomal protein import. DR Reactome; R-SCE-9603798; Class I peroxisomal membrane protein import. DR EvolutionaryTrace; P80667; -. DR PRO; PR:P80667; -. 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; PF00018; SH3_1; 1. DR PRINTS; PR00452; SH3DOMAIN. DR SMART; SM00326; SH3; 1. DR SUPFAM; SSF50044; SH3-domain; 1. DR PROSITE; PS50002; SH3; 1. DR GO; GO:1990429; C:peroxisomal importomer complex; IDA:SGD. DR GO; GO:0005778; C:peroxisomal membrane; IDA:ComplexPortal. DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IPI:SGD. DR GO; GO:0008320; F:transmembrane protein transporter activity; IDA:UniProtKB. DR GO; GO:0016560; P:protein import into peroxisome matrix, docking; IDA:UniProtKB. DR GO; GO:0016561; P:protein import into peroxisome matrix, translocation; IDA:UniProt. DR Proteomes; UP000002311; Chromosome XII. DR RNAct; P80667; protein. DR BioGRID-ORCS; 850888; 0 hits in 10 CRISPR screens. DR AlphaFoldDB; P80667; -. DR MDposit; P80667; -. DR FunCoup; P80667; 234. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Membrane; Peroxisome; KW Protein transport; Reference proteome; SH3 domain; Translocation; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..386 FT /note="Peroxisomal membrane protein PEX13" FT /id="PRO_0000058324" FT TOPO_DOM 1..263 FT /note="Peroxisomal matrix" FT /evidence="ECO:0000305" FT TRANSMEM 264..280 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 281..386 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:Q92266" FT DOMAIN 306..372 FT /note="SH3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT REGION 1..76 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 10..13 FT /note="Required for binding to PEX7" FT /evidence="ECO:0000250|UniProtKB:Q92968" FT COMPBIAS 23..39 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 44..55 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 65..76 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MUTAGEN 10..13 FT /note="KPWE->AAAA: Leads to PEX7 being stalled at the FT peroxisomal membrane. Decreases growth on oleic acid carbon FT source." FT /evidence="ECO:0000269|PubMed:40739340" FT HELIX 305..307 FT /evidence="ECO:0007829|PDB:2V1R" FT STRAND 309..315 FT /evidence="ECO:0007829|PDB:2V1R" FT TURN 322..324 FT /evidence="ECO:0007829|PDB:2V1R" FT STRAND 333..340 FT /evidence="ECO:0007829|PDB:2V1R" FT STRAND 346..353 FT /evidence="ECO:0007829|PDB:2V1R" FT TURN 355..357 FT /evidence="ECO:0007829|PDB:1NM7" FT STRAND 359..363 FT /evidence="ECO:0007829|PDB:2V1R" FT HELIX 364..366 FT /evidence="ECO:0007829|PDB:2V1R" FT STRAND 367..369 FT /evidence="ECO:0007829|PDB:2V1R" SQ SEQUENCE 386 AA; 42706 MW; DBEA9A2372185860 CRC64; MSSTAVPRPK PWETSASLEE PQRNAQSLSA MMTSNQQDSR PTEESNNSNS ASESAPEVLP RPAALNSSGT YGESNTIPGI YGNSNYGIPY DNNPYSMNSI YGNSIGRYGY GGSYYGNNYG SFYGGGYGAG AGYGMNNGSG LGESTKATFQ LIESLIGAVT GFAQMLESTY MATHNSFFTM ISVAEQFGNL KEMLGSFFGI FAIMKFLKKI LYRATKGRLG IPPKNFAESE GSKNKLIEDF QKFNDSGTIN SNEKATRRKI SWKPLLFFLM AVFGFPYLLN KFITKLQTSG TIRASQGNGS EPIDPSKLEF ARALYDFVPE NPEMEVALKK GDLMAILSKK DPLGRDSDWW KVRTKNGNIG YIPYNYIEII KRRKKIEHVD DETRTH //