ID   PEX14_CRILO             Reviewed;         377 AA.
AC   Q9Z2Z3;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Peroxisomal membrane protein PEX14;
DE   AltName: Full=PTS1 receptor-docking protein;
DE   AltName: Full=Peroxin-14;
DE   AltName: Full=Peroxisomal membrane anchor protein PEX14;
GN   Name=PEX14;
OS   Cricetulus longicaudatus (Long-tailed dwarf hamster) (Chinese hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10030;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10212238; DOI=10.1074/jbc.274.18.12593;
RA   Shimizu N., Itoh R., Hirono Y., Otera H., Ghaedi K., Tateishi K.,
RA   Tamura S., Okumoto K., Harano T., Mukai S., Fujiki Y.;
RT   "The peroxin Pex14p. cDNA cloning by functional complementation on a
RT   Chinese hamster ovary cell mutant, characterization, and functional
RT   analysis.";
RL   J. Biol. Chem. 274:12593-12604(1999).
CC   -!- FUNCTION: Peroxisome membrane protein that is an essential component of
CC       the peroxisomal import machinery. Functions as a docking factor for the
CC       predominantly cytoplasmic PTS1 receptor (PEX5). Plays a key role for
CC       peroxisome movement through a direct interaction with tubulin.
CC       {ECO:0000250|UniProtKB:O75381}.
CC   -!- SUBUNIT: Interacts with PEX5, PEX13 and PEX19. Interacts with tubulin.
CC       {ECO:0000250|UniProtKB:O75381}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC       {ECO:0000250|UniProtKB:O75381}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:O75381}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:O75381}.
CC   -!- SIMILARITY: Belongs to the peroxin-14 family. {ECO:0000305}.
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DR   EMBL; AB017545; BAA36836.1; -; mRNA.
DR   AlphaFoldDB; Q9Z2Z3; -.
DR   SMR; Q9Z2Z3; -.
DR   GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR   GO; GO:0047485; F:protein N-terminus binding; ISS:UniProtKB.
DR   GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
DR   GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0016558; P:protein import into peroxisome matrix; ISS:UniProtKB.
DR   GO; GO:0016560; P:protein import into peroxisome matrix, docking; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Acetylation; Membrane; Peroxisome; Phosphoprotein; Protein transport;
KW   Translocation; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O75381"
FT   CHAIN           2..377
FT                   /note="Peroxisomal membrane protein PEX14"
FT                   /id="PRO_0000371416"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          230..377
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        244..289
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        319..338
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        339..377
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:O75381"
FT   MOD_RES         34
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O75381"
FT   MOD_RES         232
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75381"
FT   MOD_RES         282
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q642G4"
FT   MOD_RES         335
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75381"
SQ   SEQUENCE   377 AA;  41197 MW;  149FA6BE32BE9285 CRC64;
     MASSEQAEQP SQPSSSPGSE NVVPREPLIA TAVKFLQNSR VRQSPLATRR AFLKKKGLTD
     DEIDLAFQQS GTATEEPPSL GLATPVAPVQ TPHLIAQPCS PGSSRWRDYG ALAIIMAGIA
     FGFHQLYKKY LLPLILGGRE DRKQLERMAS SLSELSGSVA QTVTQVQTTL ASVQELLRQQ
     QQKVQELAHE LAAAKATTST NWILESQNIN ELKSEINSLK GLLLNRRQFP PSPSAPKIPS
     WQIPVKSPSP SSPAAVNHHS SSDISPVSNE STSSSPGKES HSPEGSTATY HLLGPQEEGE
     GVVDVKGQVR MEVQGEEEKR EDKEEEEEEE EEDVSHVDEE DVLGVQREDR RGGDGQINEQ
     VDKLRRPEGA SNESERH