ID PEX21_YEAST Reviewed; 288 AA. AC P50091; D6VV19; O11855; Q6Q597; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 24-JAN-2024, entry version 137. DE RecName: Full=Peroxisomal protein PEX21 {ECO:0000305}; DE AltName: Full=Peroxin-21 {ECO:0000305}; GN Name=PEX21; OrderedLocusNames=YGR239C; ORFNames=G8593; 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]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=8701610; RX DOI=10.1002/(sici)1097-0061(19960330)12:4<385::aid-yea910>3.0.co;2-g; RA van der Aart Q.J.M., Kleine K., Steensma H.Y.; RT "Sequence analysis of the 43 kb CRM1-YLM9-PET54-DIE2-SMI1-PHO81-YHB4-PFK1 RT region from the right arm of Saccharomyces cerevisiae chromosome VII."; RL Yeast 12:385-390(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169869; RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H., RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."; RL Nature 387:81-84(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=17322287; DOI=10.1101/gr.6037607; RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., RA LaBaer J.; RT "Approaching a complete repository of sequence-verified protein-encoding RT clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 123-288. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9090057; RX DOI=10.1002/(sici)1097-0061(19970315)13:3<275::aid-yea73>3.0.co;2-g; RA Guerreiro P., Azevedo D., Barreiros T., Rodrigues-Pousada C.; RT "Sequencing of a 9.9 kb segment on the right arm of yeast chromosome VII RT reveals four open reading frames, including PFK1, the gene coding for RT succinyl-CoA synthetase (beta-chain) and two ORFs sharing homology with RT ORFs of the yeast chromosome VIII."; RL Yeast 13:275-280(1997). RN [6] RP FUNCTION, AND INTERACTION WITH PEX7. RX PubMed=9864360; DOI=10.1083/jcb.143.7.1859; RA Purdue P.E., Yang X., Lazarow P.B.; RT "Pex18p and Pex21p, a novel pair of related peroxins essential for RT peroxisomal targeting by the PTS2 pathway."; RL J. Cell Biol. 143:1859-1869(1998). RN [7] RP INTERACTION WITH PEX7, AND MUTAGENESIS OF SER-234. RX PubMed=11606420; DOI=10.1093/embo-reports/kve228; RA Einwaechter H., Sowinski S., Kunau W.H., Schliebs W.; RT "Yarrowia lipolytica Pex20p, Saccharomyces cerevisiae Pex18p/Pex21p and RT mammalian Pex5pL fulfil a common function in the early steps of the RT peroxisomal PTS2 import pathway."; RL EMBO Rep. 2:1035-1039(2001). RN [8] RP FUNCTION, AND INTERACTION WITH SES1. RX PubMed=12204379; DOI=10.1111/j.1574-6968.2002.tb11331.x; RA Rocak S., Landeka I., Weygand-Durasevic I.; RT "Identifying Pex21p as a protein that specifically interacts with yeast RT seryl-tRNA synthetase."; RL FEMS Microbiol. Lett. 214:101-106(2002). RN [9] RP FUNCTION, AND INTERACTION WITH PEX7 AND PEX13. RX PubMed=12167700; DOI=10.1128/mcb.22.17.6056-6069.2002; RA Stein K., Schell-Steven A., Erdmann R., Rottensteiner H.; RT "Interactions of Pex7p and Pex18p/Pex21p with the peroxisomal docking RT machinery: implications for the first steps in PTS2 protein import."; RL Mol. Cell. Biol. 22:6056-6069(2002). RN [10] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=14562095; DOI=10.1038/nature02026; RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., RA Weissman J.S., O'Shea E.K.; RT "Global analysis of protein localization in budding yeast."; RL Nature 425:686-691(2003). RN [11] RP FUNCTION, AND INTERACTION WITH SES1. RX PubMed=17451428; DOI=10.1111/j.1742-4658.2007.05812.x; RA Godinic V., Mocibob M., Rocak S., Ibba M., Weygand-Durasevic I.; RT "Peroxin Pex21p interacts with the C-terminal noncatalytic domain of yeast RT seryl-tRNA synthetase and forms a specific ternary complex with RT tRNA(Ser)."; RL FEBS J. 274:2788-2799(2007). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200; RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; RT "A multidimensional chromatography technology for in-depth phosphoproteome RT analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [13] {ECO:0007744|PDB:3W15} RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 190-288 IN COMPLEX WITH PEX7 AND RP PTS2-TYPE PEROXISOMAL TARGETING SIGNAL, FUNCTION, INTERACTION WITH PEX7, RP AND MUTAGENESIS OF ILE-202; LYS-230 AND PHE-236. RX PubMed=23812376; DOI=10.1038/nsmb.2618; RA Pan D., Nakatsu T., Kato H.; RT "Crystal structure of peroxisomal targeting signal-2 bound to its receptor RT complex Pex7p-Pex21p."; RL Nat. Struct. Mol. Biol. 20:987-993(2013). CC -!- FUNCTION: Receptor that mediates peroxisomal import of proteins CC containing a C-terminal PTS2-type peroxisomal targeting signal via its CC interaction with PEX7 (PubMed:12167700, PubMed:9864360, CC PubMed:23812376). Interaction with PEX7 only takes place when PEX7 is CC associated with cargo proteins containing a PTS2 peroxisomal targeting CC signal (By similarity). PEX7 along with PTS2-containing cargo proteins CC are then translocated through the PEX13-PEX14 docking complex together CC with PEX21 (PubMed:23812376). Acts as an activator of the seryl-tRNA CC synthetase SES1 by increasing its binding to tRNA (PubMed:12204379, CC PubMed:17451428). {ECO:0000250|UniProtKB:P50542, CC ECO:0000269|PubMed:12167700, ECO:0000269|PubMed:12204379, CC ECO:0000269|PubMed:17451428, ECO:0000269|PubMed:23812376, CC ECO:0000269|PubMed:9864360}. CC -!- SUBUNIT: Interacts with PEX7 (PubMed:12167700, PubMed:9864360, CC PubMed:23812376, PubMed:11606420). Interacts with PEX13 CC (PubMed:12167700). Interacts with SES1 (PubMed:12204379, CC PubMed:17451428). {ECO:0000269|PubMed:11606420, CC ECO:0000269|PubMed:12167700, ECO:0000269|PubMed:12204379, CC ECO:0000269|PubMed:17451428, ECO:0000269|PubMed:23812376, CC ECO:0000269|PubMed:9864360}. CC -!- INTERACTION: CC P50091; P39108: PEX7; NbExp=13; IntAct=EBI-23549, EBI-13183; CC P50091; P27796: POT1; NbExp=5; IntAct=EBI-23549, EBI-19236; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:14562095, CC ECO:0000269|PubMed:9864360}. Peroxisome {ECO:0000269|PubMed:14562095, CC ECO:0000269|PubMed:9864360}. Note=Cycles between the cytosol and the CC peroxisome. {ECO:0000269|PubMed:9864360}. CC -!- PTM: Monoubiquitinated at Cys-5; acts as a signal for PEX21 extraction CC and is required for proper export from peroxisomes and recycling. CC {ECO:0000250|UniProtKB:P35056}. CC -!- SIMILARITY: Belongs to the peroxin-21 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; X87941; CAA61191.1; -; Genomic_DNA. DR EMBL; Z73024; CAA97267.1; -; Genomic_DNA. DR EMBL; Z73025; CAA97269.1; -; Genomic_DNA. DR EMBL; AY558277; AAS56603.1; -; Genomic_DNA. DR EMBL; BK006941; DAA08330.1; -; Genomic_DNA. DR PIR; S57706; S57706. DR RefSeq; NP_011755.3; NM_001181368.3. DR PDB; 3W15; X-ray; 1.80 A; B=190-288. DR PDBsum; 3W15; -. DR AlphaFoldDB; P50091; -. DR SMR; P50091; -. DR BioGRID; 33491; 100. DR ComplexPortal; CPX-1906; Peroxisomal PEX7-PEX21 receptor complex. DR DIP; DIP-1503N; -. DR IntAct; P50091; 7. DR MINT; P50091; -. DR STRING; 4932.YGR239C; -. DR TCDB; 3.A.20.1.5; the peroxisomal protein importer (ppi) family. DR iPTMnet; P50091; -. DR PaxDb; 4932-YGR239C; -. DR PeptideAtlas; P50091; -. DR EnsemblFungi; YGR239C_mRNA; YGR239C; YGR239C. DR GeneID; 853154; -. DR KEGG; sce:YGR239C; -. DR AGR; SGD:S000003471; -. DR SGD; S000003471; PEX21. DR VEuPathDB; FungiDB:YGR239C; -. DR eggNOG; ENOG502S8JP; Eukaryota. DR HOGENOM; CLU_078821_0_0_1; -. DR InParanoid; P50091; -. DR OMA; NENSTIM; -. DR OrthoDB; 2036193at2759; -. DR BioCyc; YEAST:G3O-30917-MONOMER; -. DR BioGRID-ORCS; 853154; 0 hits in 10 CRISPR screens. DR PRO; PR:P50091; -. DR Proteomes; UP000002311; Chromosome VII. DR RNAct; P50091; Protein. DR GO; GO:0062137; C:cargo receptor complex; IPI:ComplexPortal. DR GO; GO:0005737; C:cytoplasm; HDA:SGD. DR GO; GO:0005829; C:cytosol; IDA:SGD. DR GO; GO:0005778; C:peroxisomal membrane; ISS:ComplexPortal. DR GO; GO:0005777; C:peroxisome; IDA:SGD. DR GO; GO:0140597; F:protein carrier chaperone; IDA:UniProtKB. DR GO; GO:0051099; P:positive regulation of binding; IDA:SGD. DR GO; GO:0016558; P:protein import into peroxisome matrix; IDA:UniProtKB. DR Gene3D; 6.10.280.230; -; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Peroxisome; Protein transport; Reference proteome; KW Thioester bond; Transport; Ubl conjugation. FT CHAIN 1..288 FT /note="Peroxisomal protein PEX21" FT /id="PRO_0000202855" FT CROSSLNK 5 FT /note="Glycyl cysteine thioester (Cys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:P35056" FT MUTAGEN 202 FT /note="I->D: Does not affect formation of a ternary complex FT composed of PEX21 and PEX7 along with PTS2-containing cargo FT proteins." FT /evidence="ECO:0000269|PubMed:23812376" FT MUTAGEN 230 FT /note="K->E: Does not affect formation of a ternary complex FT composed of PEX21 and PEX7 along with PTS2-containing cargo FT proteins." FT /evidence="ECO:0000269|PubMed:23812376" FT MUTAGEN 234 FT /note="S->F: Abolished interaction with PEX7." FT /evidence="ECO:0000269|PubMed:11606420" FT MUTAGEN 236 FT /note="F->A: Decreased formation of a ternary complex FT composed of PEX21 and PEX7 along with PTS2-containing cargo FT proteins." FT /evidence="ECO:0000269|PubMed:23812376" FT HELIX 198..209 FT /evidence="ECO:0007829|PDB:3W15" FT HELIX 225..232 FT /evidence="ECO:0007829|PDB:3W15" FT HELIX 235..244 FT /evidence="ECO:0007829|PDB:3W15" FT STRAND 247..250 FT /evidence="ECO:0007829|PDB:3W15" FT STRAND 262..264 FT /evidence="ECO:0007829|PDB:3W15" FT TURN 265..267 FT /evidence="ECO:0007829|PDB:3W15" FT STRAND 269..272 FT /evidence="ECO:0007829|PDB:3W15" SQ SEQUENCE 288 AA; 33050 MW; 0197257317ADE4FF CRC64; MPSVCHTSPI EKIIQQGHRI QNDSLIPSKR TKLAHTELTA HYATEDSHVE KHFLHNGSNF DGIDNVRYQN QPSPLTFITP NNTVDSSDWV PQFSSMKIDD SLEFSSEYKR LYSNYESQQR LNSSRQHLPF KNCMIRKTSC TYPPQKTLRQ QRQGNRDNPT DAFQFDAEFQ VLEREIQKER YEPITRRDEK WFDQDQSELQ RIATDIVKCC TPPPSSASSS STLSSSVESK LSESKFIQLM RNISSGDVTL KKNADGNSAS ELFSSNNGEL VGNRHIFVKD EIHKDILD //