PEX19_RAT
ID PEX19_RAT Reviewed; 299 AA.
AC Q9QYU1;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 110.
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 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].
RA Kammerer S.;
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35; SER-39 AND SER-66, 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: 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; Y09049; CAA70258.1; -; mRNA.
DR AlphaFoldDB; Q9QYU1; -.
DR SMR; Q9QYU1; -.
DR STRING; 10116.ENSRNOP00000032453; -.
DR iPTMnet; Q9QYU1; -.
DR PhosphoSitePlus; Q9QYU1; -.
DR jPOST; Q9QYU1; -.
DR PaxDb; Q9QYU1; -.
DR PRIDE; Q9QYU1; -.
DR UCSC; RGD:1306913; rat.
DR RGD; 1306913; Pex19.
DR eggNOG; KOG3133; Eukaryota.
DR InParanoid; Q9QYU1; -.
DR PhylomeDB; Q9QYU1; -.
DR Reactome; R-RNO-1369062; ABC transporters in lipid homeostasis.
DR Reactome; R-RNO-9603798; Class I peroxisomal membrane protein import.
DR PRO; PR:Q9QYU1; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0031526; C:brush border membrane; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005778; C:peroxisomal membrane; ISO:RGD.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0051117; F:ATPase binding; ISO:RGD.
DR GO; GO:0036105; F:peroxisome membrane class-1 targeting sequence binding; ISO:RGD.
DR GO; GO:0033328; F:peroxisome membrane targeting sequence binding; IBA:GO_Central.
DR GO; GO:0140597; F:protein carrier chaperone; ISO:RGD.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:RGD.
DR GO; GO:0061077; P:chaperone-mediated protein folding; ISO:RGD.
DR GO; GO:0072663; P:establishment of protein localization to peroxisome; ISO:RGD.
DR GO; GO:1900131; P:negative regulation of lipid binding; ISO:RGD.
DR GO; GO:0016559; P:peroxisome fission; ISO:RGD.
DR GO; GO:0007031; P:peroxisome organization; ISO:RGD.
DR GO; GO:0045046; P:protein import into peroxisome membrane; ISO:RGD.
DR GO; GO:0050821; P:protein stabilization; ISO:RGD.
DR GO; GO:0006625; P:protein targeting to peroxisome; ISO:RGD.
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; 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_0000218761"
FT PROPEP 297..299
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000396703"
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 REGION 25..63
FT /note="Disordered"
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:0007744|PubMed:22673903"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40855"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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; 32497 MW; 8EDD55F1D26E53A4 CRC64;
MAAAEGGCGA GVEADRELEE LLESALDDFD KAKPSPAPSP TISAPDASGP QKRSPGDTAK
DALFASQEKF FQELFDSELA SQATAEFEKA MKELAEEEPH LVEQFQKLSE AAGRVGSDAS
SQQEFTSCLK ETLSGLAKNA TDLQNSGMSE EELTKAMEGL GMDEGDGEGN ILPIMQSLMQ
NLLSKDVLYP SLKEITEKYP EWLQSHQESI PPEQFEKYQQ QHSVMGKICE QFEAETPTDS
EATHRARFEA VLDLMQQLQD LGHPPKELAG EMPPGLNFDL DALNLSGPPG ANGEQCLIM
