PEX19_YEAS7
ID PEX19_YEAS7 Reviewed; 341 AA.
AC A6ZXR1;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 2.
DT 25-MAY-2022, entry version 46.
DE RecName: Full=Peroxisomal membrane protein import receptor PEX19;
DE AltName: Full=Peroxin-19;
DE Flags: Precursor;
GN Name=PEX19; ORFNames=SCY_0849;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC -!- FUNCTION: Required for proper post-translational import and
CC stabilization of peroxisomal membrane proteins (PMPs). Acts as a
CC cytosolic import receptor for PMPs and delivers them to the docking
CC factor PEX3 at the peroxisomal membrane for subsequent insertion into
CC the membrane. Acts as a chaperone in stabilizing or maintaining PMPs in
CC the lipid bilayer. Directs PEX17, a peripheral component of the
CC peroxisomal matrix protein translocation machinery, to peroxisomes.
CC Stabilizes VPS1, a protein required for peroxisomal fission, at the
CC peroxisomal membrane. Also acts in conjunction with PEX3 in the
CC formation of peroxisomes from preperoxisomal compartments at the
CC endoplasmic reticulum during de novo peroxisome synthesis, probably via
CC the import of additional PMPs. {ECO:0000250|UniProtKB:Q07418}.
CC -!- SUBUNIT: Interacts (farnesylated) with PEX3; farnesylation is required
CC for this interaction. Interacts with PEX2, PEX5, PEX10, PEX11, PEX12,
CC PEX13, PEX14, PEX17, PEX22, PEX25, PEX30 and PEX32; the interaction
CC requires well-defined PEX19-binding sites within the peroxisomal
CC membrane protein targeting signal (mPTS) of the PMPs and is independent
CC on the presence of PEX3. Interacts with VPS1 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q07418}.
CC Peroxisome membrane {ECO:0000250|UniProtKB:Q07418}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q07418}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q07418}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q07418}. Note=Predominantly cytoplasmic.
CC Concentrates in a PEX3-dependent manner to defined foci on the
CC endoplasmic reticulum membrane, which then bud off to form newly
CC sythesized peroxisomes. {ECO:0000250|UniProtKB:Q07418}.
CC -!- INDUCTION: By oleic acid (at protein level). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peroxin-19 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDN60291.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AAFW02000145; EDN60291.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; A6ZXR1; -.
DR SMR; A6ZXR1; -.
DR PRIDE; A6ZXR1; -.
DR EnsemblFungi; EDN60291; EDN60291; SCY_0849.
DR HOGENOM; CLU_863835_0_0_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007031; P:peroxisome organization; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.900; -; 1.
DR InterPro; IPR006708; Pex19.
DR InterPro; IPR038322; Pex19_C_sf.
DR PANTHER; PTHR12774; PTHR12774; 1.
DR Pfam; PF04614; Pex19; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Endoplasmic reticulum; Lipoprotein; Membrane; Methylation;
KW Peroxisome; Peroxisome biogenesis; Phosphoprotein; Prenylation.
FT CHAIN 1..338
FT /note="Peroxisomal membrane protein import receptor PEX19"
FT /id="PRO_0000343447"
FT PROPEP 339..341
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000396706"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 39..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 109..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07418"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07418"
FT MOD_RES 338
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 338
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 341 AA; 38854 MW; 53C35DA2CE6B5B6B CRC64;
MNENEYDNFD DLDDLLDEDP TKLDEQSPMM CKRRFCVHDS ENKEKNAESK DSDGVQVANE
SEEDPELKEM MVDLQNEFAN LMKNNGNENN VKTEDFNKLI SALEEAAKVP RQQMEQGSSS
LKSNSTDKGT LNGSNPGFKN IVSNTLDRLK ENGNKVDTSL AEETKESQRS GQNNNIDDIL
SQLLDQMVAS GGKESAENQF DLKDGEMDDA ITKILDQMTS KEVLYEPMKE MRSEFGVWFQ
ENGENEEHKE KIGTYKRQFN IVDEIVNIYE LKDYDELKHK DRVTELLDEL EQLGDSPIRS
ANSPLKHGNE EEELMKMLEI DGNDPNLGNL DKELTDGCKQ Q
