PEX14_PICPA
ID PEX14_PICPA Reviewed; 425 AA.
AC Q9HG09;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=Peroxisomal membrane protein PEX14;
DE AltName: Full=Peroxin-14;
GN Name=PEX14 {ECO:0000312|EMBL:AAG28574.1};
OS Komagataella pastoris (Yeast) (Pichia pastoris).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Komagataella.
OX NCBI_TaxID=4922;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAG28574.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, INTERACTION WITH
RP PEX3; PEX5; PEX7; PEX8; PEX13 AND PEX17, AND PHOSPHORYLATION.
RX PubMed=11329173; DOI=10.1002/yea.711;
RA Johnson M.A., Snyder W.B., Cereghino J.L., Veenhuis M., Subramani S.,
RA Cregg J.M.;
RT "Pichia pastoris Pex14p, a phosphorylated peroxisomal membrane protein, is
RT part of a PTS-receptor docking complex and interacts with many peroxins.";
RL Yeast 18:621-641(2001).
CC -!- FUNCTION: Component of the peroxisomal translocation machinery with
CC PEX13 and PEX17. Interacts with both the PTS1 and PTS2 receptors.
CC {ECO:0000269|PubMed:11329173}.
CC -!- SUBUNIT: Binds PEX3, PEX5, PEX7, PEX8, SH3 domain of PEX13, PEX17 and
CC itself. {ECO:0000250|UniProtKB:P53112, ECO:0000269|PubMed:11329173}.
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC {ECO:0000269|PubMed:11329173}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11329173}; Cytoplasmic side
CC {ECO:0000269|PubMed:11329173}.
CC -!- PTM: Phosphorylated on serine or threonine residues.
CC {ECO:0000269|PubMed:11329173}.
CC -!- SIMILARITY: Belongs to the peroxin-14 family. {ECO:0000305}.
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DR EMBL; AF200421; AAG28574.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9HG09; -.
DR GO; GO:0005778; C:peroxisomal membrane; IDA:UniProtKB.
DR GO; GO:0016560; P:protein import into peroxisome matrix, docking; NAS:UniProtKB.
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 Membrane; Peroxisome; Phosphoprotein; Protein transport; Translocation;
KW Transport.
FT CHAIN 1..425
FT /note="Peroxisomal membrane protein PEX14"
FT /id="PRO_0000058328"
FT REGION 49..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 89..97
FT /note="SH3-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 50..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..88
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 425 AA; 46589 MW; 5DCC4EDE593F40E0 CRC64;
MSSIREEMVT SAVEFLKNPQ IADSPLAKKI EFIESKGLNE AEVKEALLRS QGGNGSSSVA
SQVSSYSPSA SQSSVAPSPP PFPDHYRNAP PLPERDWKDY FVMATATAGV SFGLYKVISN
YVLPKLLPPS KEAIELDKEA IDREFTRVEA LLNTFEEDQK AFYEEQREKS GKIEDTLTEI
DAIISKTNEK NLNNEESLKY LKLEIESIKN TLMKNIDSQK STISSELGSI EAQLDELKKL
IVAKPEDEPI RAAPQPSLTT GANSLTSESS GRSSIPHSQS VPIRTQLTTP PSDSDTSGPA
KLHIPPATSI PSLKDILRKE KNRTVDTFSK SNLGKDLESV AQSDPDKVEK YEGRRDLKSL
ERPEEDEKKE DDVEDGGDKD KLASSLESVK LPPSSEQVQA PAPKERTSSS SSRSGIPAWQ
LAAQS