PEX21_YEAST
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 03-AUG-2022, entry version 132.
DE RecName: Full=Peroxisomal membrane protein PEX21;
DE AltName: Full=Peroxin-21;
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 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 [8]
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 [9]
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 [10]
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 [11]
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).
CC -!- FUNCTION: Involved in peroxisome biogenesis and the import of
CC peroxisomal matrix proteins that contain the peroxisomal targeting
CC sequence PTS2. Required for peroxisomal targeting of PEX7 and growth on
CC oleate. Acts as an activator of the seryl-tRNA synthetase SES1 by
CC increasing its binding to tRNA. {ECO:0000269|PubMed:12167700,
CC ECO:0000269|PubMed:12204379, ECO:0000269|PubMed:17451428,
CC ECO:0000269|PubMed:9864360}.
CC -!- SUBUNIT: Interacts with PEX7, PEX13 and SES1.
CC {ECO:0000269|PubMed:12167700, ECO:0000269|PubMed:12204379,
CC ECO:0000269|PubMed:17451428, 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 {ECO:0000269|PubMed:14562095}.
CC Peroxisome membrane {ECO:0000269|PubMed:14562095}; Peripheral membrane
CC protein {ECO:0000269|PubMed:14562095}; Cytoplasmic side
CC {ECO:0000269|PubMed:14562095}.
CC -!- SIMILARITY: Belongs to the peroxin-21 family. {ECO:0000305}.
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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; 99.
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; P50091; -.
DR PRIDE; P50091; -.
DR EnsemblFungi; YGR239C_mRNA; YGR239C; YGR239C.
DR GeneID; 853154; -.
DR KEGG; sce:YGR239C; -.
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 BioCyc; YEAST:G3O-30917-MON; -.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; IDA:SGD.
DR GO; GO:0051099; P:positive regulation of binding; IDA:SGD.
DR GO; GO:0016558; P:protein import into peroxisome matrix; IMP:SGD.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Membrane; Peroxisome; Reference proteome.
FT CHAIN 1..288
FT /note="Peroxisomal membrane protein PEX21"
FT /id="PRO_0000202855"
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
