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
