PEX14_YEAST
ID PEX14_YEAST Reviewed; 341 AA.
AC P53112; D6VTZ8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Peroxisomal membrane protein PEX14;
DE AltName: Full=Peroxin-14;
GN Name=PEX14; OrderedLocusNames=YGL153W; ORFNames=G1870;
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].
RX PubMed=8585324; DOI=10.1002/yea.320111409;
RA James C.M., Indge K.J., Oliver S.G.;
RT "DNA sequence analysis of a 35 kb segment from Saccharomyces cerevisiae
RT chromosome VII reveals 19 open reading frames including RAD54, ACE1/CUP2,
RT PMR1, RCK1, AMS1 and CAL1/CDC43.";
RL Yeast 11:1413-1419(1995).
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 CHARACTERIZATION.
RX PubMed=9094717; DOI=10.1016/s0092-8674(00)80185-3;
RA Albertini M., Rehling P., Erdmann R., Girzalsky W., Kiel J.A.K.W.,
RA Veenhuis M., Kunau W.-H.;
RT "Pex14p, a peroxisomal membrane protein binding both receptors of the two
RT PTS-dependent import pathways.";
RL Cell 89:83-92(1997).
RN [6]
RP MUTAGENESIS OF 87-PRO--PRO-90, AND INTERACTION WITH PEX13.
RX PubMed=10087260; DOI=10.1083/jcb.144.6.1151;
RA Girzalsky W., Rehling P., Stein K., Kipper J., Blank L., Kunau W.-H.,
RA Erdmann R.;
RT "Involvement of Pex13p in Pex14p localization and peroxisomal targeting
RT signal 2-dependent protein import into peroxisomes.";
RL J. Cell Biol. 144:1151-1162(1999).
RN [7]
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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313, AND IDENTIFICATION BY
RP 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 [10]
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).
RN [11]
RP INTERACTION WITH PEX9.
RX PubMed=27678487; DOI=10.1242/jcs.195271;
RA Effelsberg D., Cruz-Zaragoza L.D., Schliebs W., Erdmann R.;
RT "Pex9p is a new yeast peroxisomal import receptor for PTS1-containing
RT proteins.";
RL J. Cell Sci. 129:4057-4066(2016).
RN [12] {ECO:0007744|PDB:1N5Z}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 83-96 IN COMPLEX WITH PEX13 SH3
RP DOMAIN.
RX PubMed=12453410; DOI=10.1016/s1097-2765(02)00749-9;
RA Douangamath A., Filipp F.V., Klein A.T., Barnett P., Zou P.,
RA Voorn-Brouwer T., Vega M.C., Mayans O.M., Sattler M., Distel B.,
RA Wilmanns M.;
RT "Topography for independent binding of alpha-helical and PPII-helical
RT ligands to a peroxisomal SH3 domain.";
RL Mol. Cell 10:1007-1017(2002).
RN [13] {ECO:0007744|PDB:2V1R}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 83-96.
RA Kursula P., Kursula I., Pinotsis N., Lehmann F., Zou P., Song Y.H.,
RA Wilmanns M.;
RT "Structural Genomics of Yeast SH3 Domains.";
RL Submitted (MAY-2007) to the PDB data bank.
CC -!- FUNCTION: Component of the peroxisomal translocation machinery with
CC PEX13 and PEX17. Interacts with both the PTS1 and PTS2 receptors. Binds
CC directly to PEX17.
CC -!- SUBUNIT: Interacts with PEX13 (via SH3 domain) (PubMed:10087260,
CC PubMed:12453410). Interacts with PEX9 (PubMed:27678487).
CC {ECO:0000269|PubMed:10087260, ECO:0000269|PubMed:12453410,
CC ECO:0000269|PubMed:27678487}.
CC -!- INTERACTION:
CC P53112; Q06389: FRQ1; NbExp=3; IntAct=EBI-13212, EBI-11946;
CC P53112; P80667: PEX13; NbExp=17; IntAct=EBI-13212, EBI-13206;
CC P53112; P40155: PEX17; NbExp=14; IntAct=EBI-13212, EBI-13218;
CC P53112; P32800: PEX2; NbExp=10; IntAct=EBI-13212, EBI-13160;
CC P53112; P35056: PEX5; NbExp=8; IntAct=EBI-13212, EBI-13170;
CC P53112; P33760: PEX6; NbExp=6; IntAct=EBI-13212, EBI-13178;
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane; Peripheral membrane protein;
CC Cytoplasmic side.
CC -!- MISCELLANEOUS: Present with 2570 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peroxin-14 family. {ECO:0000305}.
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DR EMBL; Z48618; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z72675; CAA96864.1; -; Genomic_DNA.
DR EMBL; AY558503; AAS56829.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07959.1; -; Genomic_DNA.
DR PIR; S60431; S60431.
DR RefSeq; NP_011362.3; NM_001181018.3.
DR PDB; 1N5Z; X-ray; 2.70 A; P/Q=83-96.
DR PDB; 2V1R; X-ray; 2.10 A; P/Q/R=83-96.
DR PDBsum; 1N5Z; -.
DR PDBsum; 2V1R; -.
DR AlphaFoldDB; P53112; -.
DR SMR; P53112; -.
DR BioGRID; 33101; 211.
DR ComplexPortal; CPX-1904; Peroxisomal PEX13-PEX14-PEX17 docking complex.
DR DIP; DIP-1749N; -.
DR ELM; P53112; -.
DR IntAct; P53112; 31.
DR MINT; P53112; -.
DR STRING; 4932.YGL153W; -.
DR TCDB; 3.A.20.1.5; the peroxisomal protein importer (ppi) family.
DR iPTMnet; P53112; -.
DR MaxQB; P53112; -.
DR PaxDb; P53112; -.
DR PRIDE; P53112; -.
DR EnsemblFungi; YGL153W_mRNA; YGL153W; YGL153W.
DR GeneID; 852724; -.
DR KEGG; sce:YGL153W; -.
DR SGD; S000003121; PEX14.
DR VEuPathDB; FungiDB:YGL153W; -.
DR eggNOG; KOG2629; Eukaryota.
DR GeneTree; ENSGT00390000015047; -.
DR HOGENOM; CLU_045718_0_1_1; -.
DR InParanoid; P53112; -.
DR OMA; LYGAYEV; -.
DR BioCyc; YEAST:G3O-30644-MON; -.
DR Reactome; R-SCE-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR Reactome; R-SCE-9033241; Peroxisomal protein import.
DR Reactome; R-SCE-9603798; Class I peroxisomal membrane protein import.
DR EvolutionaryTrace; P53112; -.
DR PRO; PR:P53112; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53112; protein.
DR GO; GO:1990429; C:peroxisomal importomer complex; IDA:SGD.
DR GO; GO:0005778; C:peroxisomal membrane; IDA:SGD.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IPI:SGD.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0016560; P:protein import into peroxisome matrix, docking; IMP:SGD.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR025655; PEX14.
DR InterPro; IPR006785; Pex14_N.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR23058; PTHR23058; 1.
DR Pfam; PF04695; Pex14_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Membrane; Peroxisome; Phosphoprotein;
KW Protein transport; Reference proteome; Translocation; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..341
FT /note="Peroxisomal membrane protein PEX14"
FT /id="PRO_0000058329"
FT REGION 276..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 86..94
FT /note="SH3-binding"
FT /evidence="ECO:0000269|PubMed:10087260"
FT COMPBIAS 276..300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..341
FT /note="Polar 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 313
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 87..90
FT /note="PTLP->ATLA: Loss of interaction with SH3 domain of
FT PEX13. No effect on membrane association."
FT /evidence="ECO:0000269|PubMed:10087260"
SQ SEQUENCE 341 AA; 38420 MW; B714D7DA045E2DCB CRC64;
MSDVVSKDRK ALFDSAVSFL KDESIKDAPL LKKIEFLKSK GLTEKEIEIA MKEPKKDGIV
GDEVSKKIGS TENRASQDMY LYEAMPPTLP HRDWKDYFVM ATATAGLLYG AYEVTRRYVI
PNILPEAKSK LEGDKKEIDD QFSKIDTVLN AIEAEQAEFR KKESETLKEL SDTIAELKQA
LVQTTRSREK IEDEFRIVKL EVVNMQNTID KFVSDNDGMQ ELNNIQKEME SLKSLMNNRM
ESGNAQDNRL FSISPNGIPG IDTIPSASEI LAKMGMQEES DKEKENGSDA NKDDNAVPAW
KKAREQTIDS NASIPEWQKN TAANEISVPD WQNGQVEDSI P
