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   27-MAR-2024, entry version 184.
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;
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] {ECO:0007744|PDB:1N5Z}
RP   X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 299-386 IN COMPLEX WITH PEX14 SH3
RP   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 or PEX21 receptors (PubMed:8858167,
CC       PubMed:20154681). The PEX13-PEX14 docking complex forms a large import
CC       pore which can be opened to a diameter of about 9 nm (PubMed:20154681).
CC       Mechanistically, PEX5 (or PEX21) receptor along with cargo proteins
CC       associates with the PEX14 subunit of the PEX13-PEX14 docking complex in
CC       the cytosol, leading to the insertion of the receptor into the
CC       organelle membrane with the concomitant translocation of the cargo into
CC       the peroxisome matrix (PubMed:20154681). {ECO:0000269|PubMed:20154681,
CC       ECO:0000269|PubMed:8858167}.
CC   -!- SUBUNIT: Interacts (via SH3 domain) with PEX14 (via SH3-binding motif);
CC       forming the PEX13-PEX14 docking complex. {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=7; IntAct=EBI-13206, EBI-13194;
CC       P80667; Q04370: PEX12; NbExp=6; IntAct=EBI-13206, EBI-2077297;
CC       P80667; P53112: PEX14; NbExp=17; 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}.
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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   PDBsum; 1JQQ; -.
DR   PDBsum; 1N5Z; -.
DR   PDBsum; 1NM7; -.
DR   PDBsum; 2V1R; -.
DR   AlphaFoldDB; P80667; -.
DR   SMR; P80667; -.
DR   BioGRID; 31461; 280.
DR   ComplexPortal; CPX-1904; Peroxisomal PEX13-PEX14-PEX17 docking complex.
DR   DIP; DIP-2473N; -.
DR   ELM; P80667; -.
DR   IntAct; P80667; 80.
DR   MINT; P80667; -.
DR   STRING; 4932.YLR191W; -.
DR   TCDB; 3.A.20.1.5; the peroxisomal protein importer (ppi) family.
DR   iPTMnet; P80667; -.
DR   MaxQB; P80667; -.
DR   PaxDb; 4932-YLR191W; -.
DR   PeptideAtlas; P80667; -.
DR   EnsemblFungi; YLR191W_mRNA; YLR191W; YLR191W.
DR   GeneID; 850888; -.
DR   KEGG; sce:YLR191W; -.
DR   AGR; SGD:S000004181; -.
DR   SGD; S000004181; PEX13.
DR   VEuPathDB; FungiDB:YLR191W; -.
DR   eggNOG; KOG3875; Eukaryota.
DR   GeneTree; ENSGT00390000016883; -.
DR   HOGENOM; CLU_034386_2_0_1; -.
DR   InParanoid; P80667; -.
DR   OMA; EGWFPKK; -.
DR   OrthoDB; 8987at2759; -.
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   BioGRID-ORCS; 850888; 0 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; P80667; -.
DR   PRO; PR:P80667; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; P80667; Protein.
DR   GO; GO:1990429; C:peroxisomal importomer complex; IDA:SGD.
DR   GO; GO:0005778; C:peroxisomal membrane; IDA:SGD.
DR   GO; GO:0008320; F:protein transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; IPI:SGD.
DR   GO; GO:0016560; P:protein import into peroxisome matrix, docking; IDA:UniProtKB.
DR   CDD; cd11771; SH3_Pex13p_fungal; 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.
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="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        264..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        281..386
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
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   COMPBIAS        17..55
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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
//