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PCYOX_MACFA
ID   PCYOX_MACFA             Reviewed;         505 AA.
AC   Q95KC9;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Prenylcysteine oxidase 1;
DE            EC=1.8.3.5 {ECO:0000250|UniProtKB:Q9UHG3};
DE   Flags: Precursor;
GN   Name=PCYOX1 {ECO:0000250|UniProtKB:Q9UHG3};
GN   ORFNames=QmoA-10162 {ECO:0000303|Ref.1};
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Medulla oblongata;
RA   Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K.,
RA   Suzuki Y., Sugano S., Hashimoto K.;
RT   "Isolation of full-length cDNA clones from macaque brain cDNA libraries.";
RL   Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Prenylcysteine oxidase that cleaves the thioether bond of
CC       prenyl-L-cysteines, such as farnesylcysteine and geranylgeranylcysteine
CC       (By similarity). Only active against free prenylcysteines and not
CC       prenylcysteine residues within prenylated proteins or peptides (By
CC       similarity). Involved in the final step in the degradation of
CC       prenylated proteins, by degrading prenylcysteines after the protein has
CC       been degraded (By similarity). {ECO:0000250|UniProtKB:F1N2K1,
CC       ECO:0000250|UniProtKB:Q9UHG3}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an S-prenyl-L-cysteine + H2O + O2 = a prenal + H2O2 + L-
CC         cysteine; Xref=Rhea:RHEA:53892, Rhea:RHEA-COMP:13675, Rhea:RHEA-
CC         COMP:13676, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:35235, ChEBI:CHEBI:137934, ChEBI:CHEBI:137935;
CC         EC=1.8.3.5; Evidence={ECO:0000250|UniProtKB:Q9UHG3};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53893;
CC         Evidence={ECO:0000250|UniProtKB:Q9UHG3};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O2 + S-(2E,6E)-farnesyl-L-cysteine = (2E,6E)-farnesal +
CC         H2O2 + L-cysteine; Xref=Rhea:RHEA:30231, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:15894, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:35235, ChEBI:CHEBI:62141; EC=1.8.3.5;
CC         Evidence={ECO:0000250|UniProtKB:Q9UHG3};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30232;
CC         Evidence={ECO:0000250|UniProtKB:Q9UHG3};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(2E,6E,10E)-geranylgeranyl]-L-cysteine + H2O + O2 =
CC         (2E,6E,10E)-geranylgeranial + H2O2 + L-cysteine;
CC         Xref=Rhea:RHEA:70407, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:35235, ChEBI:CHEBI:189549,
CC         ChEBI:CHEBI:189554; EC=1.8.3.5;
CC         Evidence={ECO:0000250|UniProtKB:Q9UHG3};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70408;
CC         Evidence={ECO:0000250|UniProtKB:Q9UHG3};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:Q9UHG3};
CC   -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:Q9UHG3}.
CC   -!- SIMILARITY: Belongs to the prenylcysteine oxidase family.
CC       {ECO:0000305}.
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DR   EMBL; AB062961; BAB60740.1; -; mRNA.
DR   AlphaFoldDB; Q95KC9; -.
DR   STRING; 9541.XP_005575714.1; -.
DR   PRIDE; Q95KC9; -.
DR   eggNOG; ENOG502QSHJ; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0102149; F:farnesylcysteine lyase activity; IEA:RHEA.
DR   GO; GO:0001735; F:prenylcysteine oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030328; P:prenylcysteine catabolic process; IEA:InterPro.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR010795; Prenylcys_lyase.
DR   InterPro; IPR017046; Prenylcysteine_Oxase.
DR   PANTHER; PTHR15944; PTHR15944; 1.
DR   Pfam; PF07156; Prenylcys_lyase; 1.
DR   PIRSF; PIRSF036292; Prenylcysteine_oxidase; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   2: Evidence at transcript level;
KW   FAD; Flavoprotein; Glycoprotein; Lysosome; Oxidoreductase;
KW   Reference proteome; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..505
FT                   /note="Prenylcysteine oxidase 1"
FT                   /id="PRO_0000023299"
FT   CARBOHYD        196
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        323
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        353
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   505 AA;  56517 MW;  9CC9A113FA132897 CRC64;
     MGRAVAELVS SLLGLWLLLC SCGCPEGAEL RAPPDKIAVI GAGIGGTSAA YYLRQKFGKD
     VKIDLFEREE VGGRLATMMV QGQEYEAGGS VIHPLNLHMK RFVKDLGLST VQASGGLLGI
     YNGEALVFEE SNWFIINVIK LVWRYGFQSL RMHMWVEDVL DKFMRIYRYQ SHDYAFSSVE
     KLLHALGGDD FLGMLNRTLL ETLQKAGFSE KFLNEMIAPV MRVDYGQSTD INAFVGAVSL
     SCSDSGLWAV EGGNKLVCSG LLQASKSNLI SGSVMYIEEK TKTKHTGNPT KMYEVVYQIG
     TETHSDFYDI VLVATPLNRK MSNITFLNFD PPIEEFHQYY QHIVTTLVKG ELNTSIFSSR
     PIDKFGLSTV LTTDNSDLFI NSIGIVSSVR EKEDPEPSTD GTYVWKIFSQ ETLTKAQILK
     LFLSYDYAVK KPWLAYPHYK PPEKCPSIIL HDRLYYLNGI ECAASAMEMS AIAAHNAALL
     AYHRWNGHTD MIDQDGLYEK LKTEL
 
 
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