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PEX19_PONAB
ID   PEX19_PONAB             Reviewed;         299 AA.
AC   Q5R7U2;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Peroxisomal biogenesis factor 19;
DE   AltName: Full=Peroxin-19;
DE   AltName: Full=Peroxisomal farnesylated protein;
DE   Flags: Precursor;
GN   Name=PEX19; Synonyms=PXF;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Necessary for early peroxisomal biogenesis. Acts both as a
CC       cytosolic chaperone and as an import receptor for peroxisomal membrane
CC       proteins (PMPs). Binds and stabilizes newly synthesized PMPs in the
CC       cytoplasm by interacting with their hydrophobic membrane-spanning
CC       domains, and targets them to the peroxisome membrane by binding to the
CC       integral membrane protein PEX3. Excludes CDKN2A from the nucleus and
CC       prevents its interaction with MDM2, which results in active degradation
CC       of TP53. {ECO:0000250|UniProtKB:P40855}.
CC   -!- SUBUNIT: Interacts with a broad range of peroxisomal membrane proteins,
CC       including PEX3, PEX10, PEX11A, PEX11B, PEX12, PEX13, PEX14 and PEX16,
CC       PXMP2/PMP22, PXMP4/PMP24, SLC25A17/PMP34, ABCD1/ALDP, ABCD2/ALDRP, and
CC       ABCD3/PMP70. Also interacts with the tumor suppressor CDKN2A/p19ARF (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P40855}.
CC       Peroxisome membrane {ECO:0000250|UniProtKB:P40855}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:P40855}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P40855}. Note=Mainly cytoplasmic. Some fraction
CC       membrane-associated to the outer surface of peroxisomes.
CC       {ECO:0000250|UniProtKB:P40855}.
CC   -!- SIMILARITY: Belongs to the peroxin-19 family. {ECO:0000305}.
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DR   EMBL; CR860017; CAH92168.1; -; mRNA.
DR   RefSeq; NP_001126269.1; NM_001132797.1.
DR   AlphaFoldDB; Q5R7U2; -.
DR   SMR; Q5R7U2; -.
DR   STRING; 9601.ENSPPYP00000000743; -.
DR   Ensembl; ENSPPYT00000000772; ENSPPYP00000000743; ENSPPYG00000000636.
DR   GeneID; 100173241; -.
DR   KEGG; pon:100173241; -.
DR   CTD; 5824; -.
DR   eggNOG; KOG3133; Eukaryota.
DR   GeneTree; ENSGT00390000010993; -.
DR   HOGENOM; CLU_043063_3_0_1; -.
DR   InParanoid; Q5R7U2; -.
DR   OrthoDB; 1282367at2759; -.
DR   TreeFam; TF315082; -.
DR   Proteomes; UP000001595; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005778; C:peroxisomal membrane; ISS:UniProtKB.
DR   GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR   GO; GO:0051117; F:ATPase binding; IEA:Ensembl.
DR   GO; GO:0036105; F:peroxisome membrane class-1 targeting sequence binding; IEA:Ensembl.
DR   GO; GO:0140597; F:protein carrier chaperone; IEA:Ensembl.
DR   GO; GO:0047485; F:protein N-terminus binding; IEA:Ensembl.
DR   GO; GO:0061077; P:chaperone-mediated protein folding; IEA:Ensembl.
DR   GO; GO:1900131; P:negative regulation of lipid binding; IEA:Ensembl.
DR   GO; GO:0016559; P:peroxisome fission; IEA:Ensembl.
DR   GO; GO:0016557; P:peroxisome membrane biogenesis; ISS:UniProtKB.
DR   GO; GO:0007031; P:peroxisome organization; ISS:UniProtKB.
DR   GO; GO:0045046; P:protein import into peroxisome membrane; IEA:Ensembl.
DR   GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR   GO; GO:0006625; P:protein targeting to peroxisome; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Lipoprotein; Membrane; Methylation; Peroxisome;
KW   Peroxisome biogenesis; Phosphoprotein; Prenylation; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P40855"
FT   CHAIN           2..296
FT                   /note="Peroxisomal biogenesis factor 19"
FT                   /id="PRO_0000253624"
FT   PROPEP          297..299
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000396702"
FT   REGION          1..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2..91
FT                   /note="Necessary for PEX19 function on peroxisome
FT                   biogenesis"
FT                   /evidence="ECO:0000250"
FT   REGION          2..56
FT                   /note="Docking to the peroxisome membrane and binding to
FT                   PEX3"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        9..30
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:P40855"
FT   MOD_RES         35
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P40855"
FT   MOD_RES         54
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P40855"
FT   MOD_RES         66
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QYU1"
FT   MOD_RES         236
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VCI5"
FT   MOD_RES         296
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           296
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   299 AA;  32881 MW;  9816BDB328B4377A CRC64;
     MAAAEEDYGV GAEADRELEE LLESALDDFD KAKPSPAPPS TTTAPDASGP QKRSPGDTAK
     DSLFASQEKF FQELFDSELA SQATAEFEKA MKELAEEEPH LVEQFQKLSE AAGRVGSDMT
     SQQEFTSCLK ETLSGLAKNA TDLQNSGMSE EELTKAMEGL GMDEGDGEGN ILPIMQSIMQ
     NLLSKDVLYP SLKEITEKYP EWLQSHRESL PPEQFEKYQE QHSVMCKICE QFEAETPTDS
     ETTQKARFEM VLDLMQQLQD LGHPPKELAG EMPPGLNFDL DALNLSGPPG ASGEQCLIM
 
 
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