| Tag |
Content |
LipidDB ID |
LipidDB-559292-00130 |
Entry Name |
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UniProt Accession |
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Theoretical PI |
4.25 |
Molecular Weight |
38706.08 |
Genbank Protein ID |
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Genbank Nucleotide ID |
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Protein Name |
Peroxisomal membrane protein import receptor PEX19 |
Protein Synonyms/Alias |
Peroxin-19; |
Gene Name |
PEX19 |
Gene Synonyms/Alias |
PAS12; YDL065C; D2528; |
Created Date |
15-DEC-1998 |
| Lipid Modification Sites |
|---|
| Position |
Sequence Form |
Peptide |
References |
Modification Type |
339 | Canonical | DKELTDGCKQQ**** | [1] | S-Farnesylation |
|
Organism |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
NCBI Taxa ID |
559292 |
Reference |
[1] Götte K, Girzalsky W, Linkert M, Baumgart E, Kammerer S, Kunau WH, Erdmann R. Pex19p, a farnesylated protein essential for peroxisome biogenesis. Mol CellBiol. 1998 Jan;18(1):616-28.[ PMID:9418908]
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Functional Description |
Required for proper post-translational import and stabilization of peroxisomal membrane proteins (PMPs). Acts as a cytosolic import receptor for PMPs and delivers them to the docking factor PEX3 at the peroxisomal membrane for subsequent insertion into the membrane. Acts as a chaperone in stabilizing or maintaining PMPs in the lipid bilayer. Directs PEX17, a peripheral component of the peroxisomal matrix protein translocation machinery, to peroxisomes. Stabilizes VPS1, a protein required for peroxisomal fission, at the peroxisomal membrane. Also acts in conjunction with PEX3 in the formation of peroxisomes from preperoxisomal compartments at the endoplasmic reticulum during de novo peroxisome synthesis, probably via the import of additional PMPs. |
Sequence Annotation |
Modified residue: 62 62 Phosphoserine.
Modified residue: 304 304 Phosphoserine.
Modified residue: 339 339 Cysteine methyl ester.
|
Protein Length |
342 AA. |
Protein Sequence
(Canonical) |
MNENEYDNFD DLDDLLDEDP TKLDEAEPDD VQAKGSVYND SENKEKNAES KDSDGVQVAN 60
ESEEDPELKE MMVDLQNEFA NLMKNNGNEN NVKTEDFNKL ISALEEAAKV PHQQMEQGCS 120
SLKSNSTDKG TVNGSNPGFK NIVSNTLDRL KENGNKVDTS LAEETKESQR SGQNNNIDDI 180
LSQLLDQMVA SGGKESAENQ FDLKDGEMDD AITKILDQMT SKEVLYEPMK EMRSEFGVWF 240
QENGENEEHK EKIGTYKRQF NIVDEIVNIY ELKDYDELKH KDRVTELLDE LEQLGDSPIR 300
SANSPLKHGN EEEELMKMLE IDGNDPNLGN LDKELTDGCK QQ 342
|
FASTA
(Canonical) |
>LipidDB-559292-00130|Q07418
MNENEYDNFDDLDDLLDEDPTKLDEAEPDDVQAKGSVYNDSENKEKNAESKDSDGVQVAN
ESEEDPELKEMMVDLQNEFANLMKNNGNENNVKTEDFNKLISALEEAAKVPHQQMEQGCS
SLKSNSTDKGTVNGSNPGFKNIVSNTLDRLKENGNKVDTSLAEETKESQRSGQNNNIDDI
LSQLLDQMVASGGKESAENQFDLKDGEMDDAITKILDQMTSKEVLYEPMKEMRSEFGVWF
QENGENEEHKEKIGTYKRQFNIVDEIVNIYELKDYDELKHKDRVTELLDELEQLGDSPIR
SANSPLKHGNEEEELMKMLEIDGNDPNLGNLDKELTDGCKQQ
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Gene Ontology |
GO:0005829; C:cytosol; IDA:SGD GO:0005783; C:endoplasmic reticulum; IDA:SGD GO:0005778; C:peroxisomal membrane; IDA:SGD GO:1990415; C:Pex17p-Pex14p docking complex; IDA:SGD GO:0033328; F:peroxisome membrane targeting sequence binding; IPI:SGD GO:0032581; P:ER-dependent peroxisome organization; IMP:SGD GO:0045033; P:peroxisome inheritance; IPI:SGD GO:0032527; P:protein exit from endoplasmic reticulum; IMP:SGD GO:0045046; P:protein import into peroxisome membrane; IMP:SGD GO:0050821; P:protein stabilization; IPI:SGD |
Interpro |
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Pfam |
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SMART |
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PROSITE |
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PRINTS |
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