PEX19_CRIGR
ID PEX19_CRIGR Reviewed; 299 AA.
AC Q60415;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 92.
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 Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 32-48; 70-88; 93-154;
RP 186-211 AND 228-242, ISOPRENYLATION AT CYS-296, TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Ovarian carcinoma;
RX PubMed=8188701; DOI=10.1016/s0021-9258(17)36772-8;
RA James G.L., Goldstein J.L., Pathak R.K., Anderson R.G.W., Brown M.S.;
RT "PxF, a prenylated protein of peroxisomes.";
RL J. Biol. Chem. 269:14182-14190(1994).
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:0000269|PubMed:8188701}; Lipid-anchor
CC {ECO:0000269|PubMed:8188701}; Cytoplasmic side
CC {ECO:0000269|PubMed:8188701}. Note=Mainly cytoplasmic. Some fraction is
CC membrane-associated to the outer surface of peroxisomes.
CC {ECO:0000250|UniProtKB:P40855}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:8188701}.
CC -!- SIMILARITY: Belongs to the peroxin-19 family. {ECO:0000305}.
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DR EMBL; U05959; AAA20595.1; -; mRNA.
DR PIR; A54090; A54090.
DR RefSeq; NP_001233665.1; NM_001246736.1.
DR AlphaFoldDB; Q60415; -.
DR SMR; Q60415; -.
DR STRING; 10029.NP_001233665.1; -.
DR Ensembl; ENSCGRT00001031567; ENSCGRP00001027320; ENSCGRG00001024356.
DR GeneID; 100689302; -.
DR KEGG; cge:100689302; -.
DR CTD; 5824; -.
DR eggNOG; KOG3133; Eukaryota.
DR GeneTree; ENSGT00390000010993; -.
DR OMA; NPQCPTM; -.
DR OrthoDB; 1282367at2759; -.
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 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Lipoprotein; Membrane;
KW Methylation; Peroxisome; Peroxisome biogenesis; Phosphoprotein;
KW Prenylation.
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_0000218758"
FT PROPEP 297..299
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000396700"
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:0000305"
FT LIPID 296
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000269|PubMed:8188701"
SQ SEQUENCE 299 AA; 32627 MW; 7680E8070B4E4375 CRC64;
MAAAEEGCDA GVEADRELEE LLESALDDFD KAKPSPAPPP TTSAPDASGP QKKSPGDTAK
DALFASQEKF FQELFDSELA SQATAEFEKA MKELAEEEPH LVEQFQKLSE AAGRVGSDAN
SQQEFTSCLK ETLSGLAKNA TDLQNSGMSE EELTKAMEGL GMDDGDGDGN ILPIMQSIMQ
NLLSKDVLYP SLKEITEKYP EWLQSHQESI PPEQFEKYQE QHSVMGKICE QFEAETPTDS
EATHRARFEA VLDLMQQLQD LGHPPKELAG EMPPGLNFDL DTLNLSGPPG ANGEQCLIM
