PEX14_MOUSE
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 03-AUG-2022, entry version 153.
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 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 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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC 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: 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; 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; Q9R0A0; -.
DR PeptideAtlas; Q9R0A0; -.
DR PRIDE; Q9R0A0; -.
DR ProteomicsDB; 301793; -.
DR Antibodypedia; 27930; 312 antibodies from 33 providers.
DR Ensembl; ENSMUST00000103217; ENSMUSP00000099506; ENSMUSG00000028975.
DR GeneID; 56273; -.
DR KEGG; mmu:56273; -.
DR UCSC; uc008vvp.1; mouse.
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; RRDWRDW; -.
DR OrthoDB; 1033073at2759; -.
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 72 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 258 other tissues.
DR ExpressionAtlas; Q9R0A0; baseline and differential.
DR Genevisible; Q9R0A0; MM.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; 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:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:MGI.
DR GO; GO:0034453; P:microtubule anchoring; ISO:MGI.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0032091; P:negative regulation of protein binding; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; 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; IBA:GO_Central.
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; -; 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 Acetylation; Direct protein sequencing; Membrane; Peroxisome;
KW Phosphoprotein; Protein transport; Reference proteome; Translocation;
KW 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 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
