ID   PEX31_YEAST             Reviewed;         462 AA.
AC   P53203; D6VUE1;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 144.
DE   RecName: Full=Peroxisomal membrane protein PEX31;
DE   AltName: Full=Peroxin-31;
GN   Name=PEX31; OrderedLocusNames=YGR004W;
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=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   [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   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   [4]
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   [5]
RP   TOPOLOGY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 208353 / W303-1A;
RX   PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA   Kim H., Melen K., Oesterberg M., von Heijne G.;
RT   "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432 AND THR-435, 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).
CC   -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC       {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 238 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the PEX28-32 family. PEX30/31 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; Z72789; CAA96987.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08102.1; -; Genomic_DNA.
DR   PIR; S64293; S64293.
DR   RefSeq; NP_011518.1; NM_001181133.1.
DR   AlphaFoldDB; P53203; -.
DR   BioGRID; 33248; 103.
DR   DIP; DIP-5455N; -.
DR   IntAct; P53203; 3.
DR   MINT; P53203; -.
DR   STRING; 4932.YGR004W; -.
DR   TCDB; 3.A.20.1.5; the peroxisomal protein importer (ppi) family.
DR   iPTMnet; P53203; -.
DR   MaxQB; P53203; -.
DR   PaxDb; 4932-YGR004W; -.
DR   PeptideAtlas; P53203; -.
DR   TopDownProteomics; P53203; -.
DR   EnsemblFungi; YGR004W_mRNA; YGR004W; YGR004W.
DR   GeneID; 852887; -.
DR   KEGG; sce:YGR004W; -.
DR   AGR; SGD:S000003236; -.
DR   SGD; S000003236; PEX31.
DR   VEuPathDB; FungiDB:YGR004W; -.
DR   eggNOG; ENOG502QT80; Eukaryota.
DR   GeneTree; ENSGT00940000176349; -.
DR   HOGENOM; CLU_016397_0_0_1; -.
DR   InParanoid; P53203; -.
DR   OMA; ASWTDEF; -.
DR   OrthoDB; 1449562at2759; -.
DR   BioCyc; YEAST:G3O-30735-MONOMER; -.
DR   BioGRID-ORCS; 852887; 1 hit in 10 CRISPR screens.
DR   PRO; PR:P53203; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P53203; Protein.
DR   GO; GO:0071944; C:cell periphery; HDA:SGD.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR   GO; GO:0071782; C:endoplasmic reticulum tubular network; ISS:SGD.
DR   GO; GO:0005778; C:peroxisomal membrane; IDA:SGD.
DR   GO; GO:0097749; P:membrane tubulation; ISS: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   PANTHER; PTHR31679; PEROXISOMAL MEMBRANE PROTEIN PEX30-RELATED; 1.
DR   PANTHER; PTHR31679:SF2; PEROXISOMAL MEMBRANE PROTEIN PEX30-RELATED; 1.
DR   Pfam; PF06398; Pex24p; 1.
DR   SMART; SM00694; DysFC; 1.
DR   SMART; SM00693; DysFN; 1.
PE   1: Evidence at protein level;
KW   Membrane; Peroxisome; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..462
FT                   /note="Peroxisomal membrane protein PEX31"
FT                   /id="PRO_0000202779"
FT   TOPO_DOM        1..90
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        91..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        112..175
FT                   /note="Peroxisomal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        176..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        197..462
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          406..425
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         432
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358,
FT                   ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198"
FT   MOD_RES         435
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   462 AA;  52943 MW;  3F875D40748AB6C3 CRC64;
     MSEINNENLE PTSSTVAEST ESKNKHIRSA LRKRRGKLSA QTYEEDQEAI LSSPLLTSTP
     KTVSRSLVRL YPYLIVVDNF LSIITWSNDN VSANLLGIFL FTVCVLYFGF ITRYFGHLMI
     VGIIWVYLLI DKHVQETMAS CPSLDDIIHV MDRVSMKSSA VLSPITILSA QDVRRLLFTI
     AFLSPVYIFL TVFVLSPNYL MLIGGLYVLT YHSKLIRRMR RYLWKFRVVR LLVFFITGLD
     LGGPDNNRRL FASVNKKIRS FVWNEVGNTS NTKKTVLFKV ALFENQRRWL GIGWTSTMLS
     YERASWTDEF LNTSPSPEVF TLPEEQSGMA WEWHDKDWML DLTNDGIIQL PASAAKTKVK
     PGADEGFIYY DNTWNNPSAT DTYKKYTRRR RWIRTATVTT TYDDEPTVEK ATPNSHALKS
     EENNRVRKRK VSFSTANEVH IIPSSDSSKL IQISDVSMSP SL
//