PEX13_YEAST
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 03-AUG-2022, entry version 177.
DE RecName: Full=Peroxisomal membrane protein PAS20;
DE AltName: Full=Peroxin-13;
GN Name=PEX13; 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, AND CHARACTERIZATION.
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).
CC -!- FUNCTION: Component of the peroxisomal translocation machinery with
CC PEX14 and PEX17. Interacts with the PTS1 receptor (PAS10/PEX5).
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; Single-pass membrane
CC protein.
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; 274.
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; P80667; -.
DR PRIDE; P80667; -.
DR EnsemblFungi; YLR191W_mRNA; YLR191W; YLR191W.
DR GeneID; 850888; -.
DR KEGG; sce:YLR191W; -.
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; QPKIRGW; -.
DR BioCyc; YEAST:G3O-32313-MON; -.
DR Reactome; R-SCE-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
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 Proteomes; UP000002311; Chromosome XII.
DR RNAct; P80667; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:1990429; C:peroxisomal importomer complex; IDA:SGD.
DR GO; GO:0005778; C:peroxisomal membrane; IDA:SGD.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IPI:SGD.
DR GO; GO:0016560; P:protein import into peroxisome matrix, docking; IGI:SGD.
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; PF00018; SH3_1; 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 3D-structure; Direct protein sequencing; Membrane; Peroxisome;
KW Protein transport; Reference proteome; SH3 domain; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..386
FT /note="Peroxisomal membrane protein PAS20"
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
