ID   PEX14_MOUSE             Reviewed;         376 AA.
AC   Q9R0A0;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 162.
DE   RecName: Full=Peroxisomal membrane protein PEX14 {ECO:0000305};
DE   AltName: Full=PTS1 receptor-docking protein;
DE   AltName: Full=Peroxin-14 {ECO:0000305};
DE   AltName: Full=Peroxisomal membrane anchor protein PEX14;
GN   Name=Pex14 {ECO:0000303|PubMed:12488033, ECO:0000312|MGI:MGI:1927868};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Bliskovsky V., Miller M., Mock B.;
RT   "Physical linkage of Pex14 and Cast genes on mouse chromosome 4.";
RL   Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 228-237, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=12488033; DOI=10.1016/s0005-2736(02)00635-1;
RA   Oliveira M.E., Reguenga C., Gouveia A.M., Guimaraes C.P., Schliebs W.,
RA   Kunau W.H., Silva M.T., Sa-Miranda C., Azevedo J.E.;
RT   "Mammalian Pex14p: membrane topology and characterisation of the Pex14p-
RT   Pex14p interaction.";
RL   Biochim. Biophys. Acta 1567:13-22(2002).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Component of the PEX13-PEX14 docking complex, a translocon
CC       channel that specifically mediates the import of peroxisomal cargo
CC       proteins bound to PEX5 receptor (By similarity). The PEX13-PEX14
CC       docking complex forms a large import pore which can be opened to a
CC       diameter of about 9 nm (By similarity). Mechanistically, PEX5 receptor
CC       along with cargo proteins associates with the PEX14 subunit of the
CC       PEX13-PEX14 docking complex in the cytosol, leading to the insertion of
CC       the receptor into the organelle membrane with the concomitant
CC       translocation of the cargo into the peroxisome matrix. Plays a key role
CC       for peroxisome movement through a direct interaction with tubulin (By
CC       similarity). {ECO:0000250|UniProtKB:O75381,
CC       ECO:0000250|UniProtKB:P53112}.
CC   -!- SUBUNIT: Interacts with PEX13; forming the PEX13-PEX14 docking complex.
CC       Interacts with PEX5 (via WxxxF/Y motifs). Interacts with PEX19.
CC       Interacts with tubulin. {ECO:0000250|UniProtKB:O75381}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC       {ECO:0000269|PubMed:12488033}; Single-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q642G4}.
CC   -!- SIMILARITY: Belongs to the peroxin-14 family. {ECO:0000305}.
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DR   EMBL; AF097512; AAF04616.1; -; mRNA.
DR   EMBL; BC028952; AAH28952.1; -; mRNA.
DR   CCDS; CCDS18950.1; -.
DR   RefSeq; NP_062755.1; NM_019781.2.
DR   AlphaFoldDB; Q9R0A0; -.
DR   SMR; Q9R0A0; -.
DR   BioGRID; 207868; 13.
DR   IntAct; Q9R0A0; 1.
DR   STRING; 10090.ENSMUSP00000099506; -.
DR   iPTMnet; Q9R0A0; -.
DR   PhosphoSitePlus; Q9R0A0; -.
DR   EPD; Q9R0A0; -.
DR   jPOST; Q9R0A0; -.
DR   MaxQB; Q9R0A0; -.
DR   PaxDb; 10090-ENSMUSP00000099506; -.
DR   PeptideAtlas; Q9R0A0; -.
DR   ProteomicsDB; 301793; -.
DR   Pumba; Q9R0A0; -.
DR   Antibodypedia; 27930; 355 antibodies from 33 providers.
DR   Ensembl; ENSMUST00000103217.11; ENSMUSP00000099506.5; ENSMUSG00000028975.17.
DR   GeneID; 56273; -.
DR   KEGG; mmu:56273; -.
DR   UCSC; uc008vvp.1; mouse.
DR   AGR; MGI:1927868; -.
DR   CTD; 5195; -.
DR   MGI; MGI:1927868; Pex14.
DR   VEuPathDB; HostDB:ENSMUSG00000028975; -.
DR   eggNOG; KOG2629; Eukaryota.
DR   GeneTree; ENSGT00390000015047; -.
DR   HOGENOM; CLU_065928_0_0_1; -.
DR   InParanoid; Q9R0A0; -.
DR   OMA; YNQWQPP; -.
DR   OrthoDB; 358337at2759; -.
DR   PhylomeDB; Q9R0A0; -.
DR   TreeFam; TF323535; -.
DR   Reactome; R-MMU-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR   Reactome; R-MMU-9033241; Peroxisomal protein import.
DR   Reactome; R-MMU-9603798; Class I peroxisomal membrane protein import.
DR   BioGRID-ORCS; 56273; 4 hits in 77 CRISPR screens.
DR   ChiTaRS; Pex14; mouse.
DR   PRO; PR:Q9R0A0; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q9R0A0; Protein.
DR   Bgee; ENSMUSG00000028975; Expressed in otic placode and 262 other cell types or tissues.
DR   ExpressionAtlas; Q9R0A0; baseline and differential.
DR   GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR   GO; GO:1990429; C:peroxisomal importomer complex; IBA:GO_Central.
DR   GO; GO:0005778; C:peroxisomal membrane; IDA:MGI.
DR   GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0048487; F:beta-tubulin binding; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0008017; F:microtubule binding; ISO:MGI.
DR   GO; GO:0008320; F:protein transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; ISS:UniProtKB.
DR   GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR   GO; GO:0003714; F:transcription corepressor activity; ISO:MGI.
DR   GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:MGI.
DR   GO; GO:0034453; P:microtubule anchoring; ISO:MGI.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISO:MGI.
DR   GO; GO:0007031; P:peroxisome organization; ISO:MGI.
DR   GO; GO:0036250; P:peroxisome transport along microtubule; ISO:MGI.
DR   GO; GO:0016558; P:protein import into peroxisome matrix; ISO:MGI.
DR   GO; GO:0016560; P:protein import into peroxisome matrix, docking; ISS:UniProtKB.
DR   GO; GO:0044721; P:protein import into peroxisome matrix, substrate release; ISO:MGI.
DR   GO; GO:0016561; P:protein import into peroxisome matrix, translocation; ISO:MGI.
DR   GO; GO:0065003; P:protein-containing complex assembly; ISO:MGI.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR025655; PEX14.
DR   InterPro; IPR006785; Pex14_N.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR23058; PEROXISOMAL MEMBRANE PROTEIN PEX14; 1.
DR   PANTHER; PTHR23058:SF0; PEROXISOMAL MEMBRANE PROTEIN PEX14; 1.
DR   Pfam; PF04695; Pex14_N; 1.
DR   Genevisible; Q9R0A0; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Membrane; Peroxisome;
KW   Phosphoprotein; Protein transport; Reference proteome; Translocation;
KW   Transmembrane; Transmembrane helix; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O75381"
FT   CHAIN           2..376
FT                   /note="Peroxisomal membrane protein PEX14"
FT                   /id="PRO_0000058326"
FT   TOPO_DOM        2..108
FT                   /note="Peroxisomal"
FT                   /evidence="ECO:0000250|UniProtKB:Q642G4"
FT   TRANSMEM        109..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        128..376
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q642G4"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          70..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          230..376
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..98
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        241..289
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        319..337
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        338..376
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         334
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355"
SQ   SEQUENCE   376 AA;  41208 MW;  F7863CE4B6433580 CRC64;
     MASSEQAEQP NQPSSPPGSE NVVPREPLIA TAVKFLQNSR VRQSPLATRR AFLKKKGLTD
     EEIDLAFQQS GTAADEPSPL GPATPVVPVQ PPHLTPQPYS PRGSRWRDYG ALAIIMAGIA
     FGFHQLYKRY LLPLILGGRE DRKQLERMAA SLSELSGTVA QTVTQVQTTL ASVQELLRQQ
     QQKVQELAHE LATAKATTST NWILESQNIN ELKSEINSLK GLLLNRRQFP PSPSAPKIPS
     WQIPVKSSSP SSPAAVNHHS SSDISPVSNE STSSSPGKDS HSPEGSTATY HLLGPQEEGE
     GVLDVKGQVR MEVQGEEEKR EDKEDEDDED DDVSHVDEED VLGVQREDRR GGDGQINEQV
     EKLRRPEGAS NETERD
//