PEX14_RAT
ID PEX14_RAT Reviewed; 376 AA.
AC Q642G4; Q9Z2Z4;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282 AND SER-334, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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; AB017544; BAA36835.1; -; mRNA.
DR EMBL; BC081708; AAH81708.1; -; mRNA.
DR RefSeq; NP_742060.1; NM_172063.1.
DR PDB; 3FF5; X-ray; 1.80 A; A/B=25-70.
DR PDBsum; 3FF5; -.
DR AlphaFoldDB; Q642G4; -.
DR SMR; Q642G4; -.
DR BioGRID; 249075; 2.
DR DIP; DIP-58546N; -.
DR IntAct; Q642G4; 2.
DR MINT; Q642G4; -.
DR STRING; 10116.ENSRNOP00000018167; -.
DR iPTMnet; Q642G4; -.
DR PhosphoSitePlus; Q642G4; -.
DR jPOST; Q642G4; -.
DR PaxDb; Q642G4; -.
DR PRIDE; Q642G4; -.
DR Ensembl; ENSRNOT00000018167; ENSRNOP00000018167; ENSRNOG00000013498.
DR GeneID; 64460; -.
DR KEGG; rno:64460; -.
DR CTD; 5195; -.
DR RGD; 68336; Pex14.
DR eggNOG; KOG2629; Eukaryota.
DR GeneTree; ENSGT00390000015047; -.
DR HOGENOM; CLU_065928_0_0_1; -.
DR InParanoid; Q642G4; -.
DR OMA; RRDWRDW; -.
DR OrthoDB; 1033073at2759; -.
DR PhylomeDB; Q642G4; -.
DR TreeFam; TF323535; -.
DR Reactome; R-RNO-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR Reactome; R-RNO-9033241; Peroxisomal protein import.
DR Reactome; R-RNO-9603798; Class I peroxisomal membrane protein import.
DR EvolutionaryTrace; Q642G4; -.
DR PRO; PR:Q642G4; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000013498; Expressed in ovary and 20 other tissues.
DR Genevisible; Q642G4; RN.
DR GO; GO:0016021; C:integral component of membrane; IDA:RGD.
DR GO; GO:1990429; C:peroxisomal importomer complex; IBA:GO_Central.
DR GO; GO:0005778; C:peroxisomal membrane; IDA:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IDA:HGNC-UCL.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0048487; F:beta-tubulin binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0008017; F:microtubule binding; ISO:RGD.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:RGD.
DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:RGD.
DR GO; GO:0034453; P:microtubule anchoring; ISO:RGD.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; ISO:RGD.
DR GO; GO:0032091; P:negative regulation of protein binding; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0007031; P:peroxisome organization; IDA:RGD.
DR GO; GO:0036250; P:peroxisome transport along microtubule; ISO:RGD.
DR GO; GO:0016558; P:protein import into peroxisome matrix; ISO:RGD.
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:RGD.
DR GO; GO:0016561; P:protein import into peroxisome matrix, translocation; ISO:RGD.
DR GO; GO:0065003; P:protein-containing complex assembly; ISO:RGD.
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:0000250|UniProtKB:O75381"
FT CHAIN 2..376
FT /note="Peroxisomal membrane protein PEX14"
FT /id="PRO_0000371415"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 70..93
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..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..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:0007744|PubMed:22673903"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CONFLICT 303
FT /note="V -> M (in Ref. 1; BAA36835)"
FT /evidence="ECO:0000305"
FT HELIX 25..37
FT /evidence="ECO:0007829|PDB:3FF5"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:3FF5"
FT HELIX 46..55
FT /evidence="ECO:0007829|PDB:3FF5"
FT HELIX 60..69
FT /evidence="ECO:0007829|PDB:3FF5"
SQ SEQUENCE 376 AA; 40936 MW; C9DFFC0DD4DD45C8 CRC64;
MASSEQAEQP NQPSSSPGSE NVVPREPLIA TAVKFLQNSR VRQSPLATRR AFLKKKGLTD
EEIDLAFQQS GTASDEPSPV GPATPVVPVQ PPHLISQPYS PGGSRWRDYG ALAIILAGIA
FGFHQLYKKY LLPLILGGRE DRKQLERMAA SLSELSGSVA QTVTQVQTTL ASVQELLRQQ
QQKVQELAHE LAAAKATTST NWILESQNIN ELKSEINSLK GLLLNRRQFP PSPSAPKIPS
WQIPVKSPSP SSPAAVNHHS SSDISPVSNE SPSSSPGKDG HSPEGSTATY RLLGPQEEGE
GVVDVKGQVR MEVQGEEEKR EDEEGEEDED DDVSHVDEED VLGVQREDRR GGDGQINEQV
EKLRRPEGAS NESERD
