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PEX30_YEAST
ID   PEX30_YEAST             Reviewed;         523 AA.
AC   Q06169; D6VYW6; Q66R43;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=Peroxisomal membrane protein PEX30;
DE   AltName: Full=Peroxin-30;
GN   Name=PEX30; OrderedLocusNames=YLR324W;
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=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   [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   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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-420 AND SER-424, AND
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-420 AND SER-424, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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).
CC   -!- INTERACTION:
CC       Q06169; Q06169: PEX30; NbExp=3; IntAct=EBI-31008, EBI-31008;
CC   -!- SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PEX28-32 family. PEX30/31 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; U20618; AAB64522.1; -; Genomic_DNA.
DR   EMBL; AY723849; AAU09766.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09632.1; -; Genomic_DNA.
DR   PIR; S53401; S53401.
DR   RefSeq; NP_013428.1; NM_001182213.1.
DR   AlphaFoldDB; Q06169; -.
DR   BioGRID; 31587; 114.
DR   DIP; DIP-1800N; -.
DR   IntAct; Q06169; 8.
DR   MINT; Q06169; -.
DR   STRING; 4932.YLR324W; -.
DR   TCDB; 3.A.20.1.5; the peroxisomal protein importer (ppi) family.
DR   iPTMnet; Q06169; -.
DR   MaxQB; Q06169; -.
DR   PaxDb; Q06169; -.
DR   PRIDE; Q06169; -.
DR   EnsemblFungi; YLR324W_mRNA; YLR324W; YLR324W.
DR   GeneID; 851034; -.
DR   KEGG; sce:YLR324W; -.
DR   SGD; S000004316; PEX30.
DR   VEuPathDB; FungiDB:YLR324W; -.
DR   eggNOG; ENOG502QT80; Eukaryota.
DR   GeneTree; ENSGT00940000176349; -.
DR   HOGENOM; CLU_016397_0_0_1; -.
DR   InParanoid; Q06169; -.
DR   OMA; YHSPWSK; -.
DR   BioCyc; YEAST:G3O-32407-MON; -.
DR   PRO; PR:Q06169; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; Q06169; protein.
DR   GO; GO:0071944; C:cell periphery; HDA:SGD.
DR   GO; GO:0005933; C:cellular bud; HDA:SGD.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR   GO; GO:0071782; C:endoplasmic reticulum tubular network; IDA:SGD.
DR   GO; GO:0005779; C:integral component of peroxisomal membrane; IDA:SGD.
DR   GO; GO:0005777; C:peroxisome; IDA:SGD.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0032581; P:ER-dependent peroxisome organization; IGI:SGD.
DR   GO; GO:0097749; P:membrane tubulation; IMP:SGD.
DR   GO; GO:0007031; P:peroxisome organization; IMP:SGD.
DR   GO; GO:1900063; P:regulation of peroxisome organization; IGI:SGD.
DR   InterPro; IPR010482; Peroxin.
DR   InterPro; IPR006614; Peroxin/Ferlin.
DR   Pfam; PF06398; Pex24p; 1.
DR   SMART; SM00694; DysFC; 1.
DR   SMART; SM00693; DysFN; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Membrane; Peroxisome; Phosphoprotein; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..523
FT                   /note="Peroxisomal membrane protein PEX30"
FT                   /id="PRO_0000252270"
FT   TRANSMEM        91..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        118..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        184..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        207..227
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          429..523
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        429..444
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        445..523
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         52
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         420
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         424
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   CONFLICT        257
FT                   /note="G -> S (in Ref. 3; AAU09766)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   523 AA;  59462 MW;  417DBE56B1C8B1D5 CRC64;
     MSGNTTNVHE TRAKFAETLQ PRIGGNTTKV IRAALEKNEA ESGVSEDNDN GSLEKVNVAT
     SPLLTSTPPT ISKALVKLYP YLILIDEFLN VVTWTGKNIW SSVLMLCLFI TTVEYFETLV
     KYFGHLAIIA ILWGYSLLDN YIEGTLSSSP TLEDIALLMN RVSLKSDILL SPMVNLGTQD
     IQRLLYTTVI LSPIYVMITW LLLPPRSLML MVGMFLLTYH SPWSKVARRL LWKFKIVRLL
     VFYVTGLDLG GINKDQGIFA TVQKQVKKLA STENSNGVLS DSKPIRFTYV LYENQRRWLG
     IGWKPSMLSY ERTPWTDEFL NEAPSPENFH LPEETNTMVW RWVDKTWRLD MTNDGAIQVP
     NSKARTSADP SPDEGFIYYD NTWKKPSKED SFSKYTRRRR WVRTAELVKT SDFDESVINS
     NRNSAIEQKV EENSTNGLTA EQELGSNKQE KDNAKKVGEP TTEETKEFAE ASNINEGEFE
     RISSTDEEVL KSRARDRLAK VLDDTEEKEQ SNPTIGRDSK KAV
 
 
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