ID   PXP2_YEAST              Reviewed;         283 AA.
AC   P47148; D6VWT0;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Peroxisomal protein 2 {ECO:0000303|PubMed:27392156};
GN   Name=PXP2 {ECO:0000303|PubMed:27392156}; OrderedLocusNames=YJR111C;
GN   ORFNames=J2009;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA   Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA   Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA   Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA   Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA   Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA   Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA   Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA   To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA   von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL   EMBO J. 15:2031-2049(1996).
RN   [2]
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   [3]
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   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [5]
RP   DOMAIN, SUBCELLULAR LOCATION, FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=27392156; DOI=10.1111/tra.12426;
RA   Noetzel C., Lingner T., Klingenberg H., Thoms S.;
RT   "Identification of new fungal peroxisomal matrix proteins and revision of
RT   the PTS1 consensus.";
RL   Traffic 17:1110-1124(2016).
CC   -!- FUNCTION: Probably involved in peroxisome formation or maintenance as
CC       well as in amino acid metabolism. {ECO:0000269|PubMed:27392156}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000269|PubMed:27392156}.
CC       Cytoplasm, cytosol {ECO:0000269|PubMed:27392156}.
CC   -!- DOMAIN: Peroxisomal targeting signal 1 (PTS1) is a tripeptide located
CC       at the C-terminus of more than 95% of all peroxisomal matrix proteins.
CC       The prototypical PTS1 is the terminal tripeptide SKL (serine-lysine-
CC       leucine) but the consensus of PTS1 is defined as [S/A/H/C/E/P/Q/V]
CC       [K/R/H/Q] [L/F]. However, this description of the PTS1 consensus must
CC       probably be expanded beyond the terminal tripeptide.
CC       {ECO:0000305|PubMed:27392156}.
CC   -!- DISRUPTION PHENOTYPE: Impairs growth on oleate as well as on the non-
CC       fermentable carbon sources ethanol and acetate (PubMed:27392156). Leads
CC       to increased level in threonine, serine, valine, isoleucine and
CC       histidine; as well as a reduction in citrulline, tyrosine and
CC       phenylalanine (PubMed:27392156). {ECO:0000269|PubMed:27392156}.
CC   -!- MISCELLANEOUS: Present with 1890 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the PXP2 family. {ECO:0000305}.
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DR   EMBL; Z49611; CAA89641.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08896.1; -; Genomic_DNA.
DR   PIR; S57134; S57134.
DR   RefSeq; NP_012645.1; NM_001181769.1.
DR   AlphaFoldDB; P47148; -.
DR   BioGRID; 33867; 38.
DR   IntAct; P47148; 2.
DR   STRING; 4932.YJR111C; -.
DR   MaxQB; P47148; -.
DR   PaxDb; P47148; -.
DR   PRIDE; P47148; -.
DR   EnsemblFungi; YJR111C_mRNA; YJR111C; YJR111C.
DR   GeneID; 853575; -.
DR   KEGG; sce:YJR111C; -.
DR   SGD; S000003872; PXP2.
DR   VEuPathDB; FungiDB:YJR111C; -.
DR   eggNOG; ENOG502RCP9; Eukaryota.
DR   HOGENOM; CLU_065389_3_0_1; -.
DR   InParanoid; P47148; -.
DR   OMA; VGFPRTI; -.
DR   BioCyc; YEAST:G3O-31734-MON; -.
DR   PRO; PR:P47148; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; P47148; protein.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0005782; C:peroxisomal matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005777; C:peroxisome; IDA:SGD.
DR   GO; GO:0051920; F:peroxiredoxin activity; IEA:InterPro.
DR   Gene3D; 1.20.1290.10; -; 1.
DR   InterPro; IPR029032; AhpD-like.
DR   InterPro; IPR003779; CMD-like.
DR   Pfam; PF02627; CMD; 1.
DR   SUPFAM; SSF69118; SSF69118; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Peroxisome; Reference proteome.
FT   CHAIN           1..283
FT                   /note="Peroxisomal protein 2"
FT                   /id="PRO_0000203112"
FT   MOTIF           281..283
FT                   /note="Peroxisomal target signal 1 (PTS1)"
FT                   /evidence="ECO:0000269|PubMed:27392156"
SQ   SEQUENCE   283 AA;  32208 MW;  CD49258DE05D3B4D CRC64;
     MNQILNAQRL IQLSQFHPKL KNIWYLVAAA TFSVCNEPQE IPKLYHYAML LSNDNAHMYR
     FTLASQTIDL LRSELPMRKT LINENYQQPT FFQKQLTAKF REVILKTGPL AGLPRAINGL
     TMLKETTPDI LVPHLDPIDP WEAAMGNSSP LSETSMRRKH DKTIQERDHT IQNGLRHWNS
     IYNKVSTRVV NNLNSSYPDL WYYTLVHVYG PLFAFDEILS AQETSLVIIA SLVPQDVNPQ
     LRGHLKGALN IGCDKETVEA VRGLAILISQ WCGVSWKSGV VKL