PCYOX_ARATH
ID PCYOX_ARATH Reviewed; 500 AA.
AC P57681;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Farnesylcysteine lyase;
DE EC=1.8.3.6;
DE Flags: Precursor;
GN Name=FLCY; OrderedLocusNames=At5g63910; ORFNames=MGI19.11, MGI19.4;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=17425716; DOI=10.1111/j.1365-313x.2007.03091.x;
RA Crowell D.N., Huizinga D.H., Deem A.K., Trobaugh C., Denton R., Sen S.E.;
RT "Arabidopsis thaliana plants possess a specific farnesylcysteine lyase that
RT is involved in detoxification and recycling of farnesylcysteine.";
RL Plant J. 50:839-847(2007).
CC -!- FUNCTION: Involved in the degradation of prenylcysteine. Cleaves
CC specifically the thioether bond of S-farnesyl-L-cysteine and has no
CC activity with S-geranylgeranyl-L-cysteine. Recognizes also N-acetyl-
CC farnesylcysteine and may have a role in deprenylation of farnesylated
CC proteins. {ECO:0000269|PubMed:17425716}.
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=1.8.3.6;
CC Evidence={ECO:0000269|PubMed:17425716};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in seedilings, flowers, stems, leaves and
CC roots. {ECO:0000269|PubMed:17425716}.
CC -!- MISCELLANEOUS: Plants with decreased levels of farnesylcysteine lyase
CC exhibit delayed germination and hypersensitivity to abscisic acid.
CC -!- SIMILARITY: Belongs to the prenylcysteine oxidase family.
CC {ECO:0000305}.
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DR EMBL; AB007646; BAB11039.1; -; Genomic_DNA.
DR EMBL; AB019227; BAB11039.1; JOINED; Genomic_DNA.
DR EMBL; CP002688; AED97815.1; -; Genomic_DNA.
DR EMBL; AY081255; AAL91144.1; -; mRNA.
DR EMBL; AY128716; AAM91116.1; -; mRNA.
DR RefSeq; NP_201196.1; NM_125787.5.
DR AlphaFoldDB; P57681; -.
DR STRING; 3702.AT5G63910.1; -.
DR PaxDb; P57681; -.
DR PRIDE; P57681; -.
DR ProteomicsDB; 234821; -.
DR EnsemblPlants; AT5G63910.1; AT5G63910.1; AT5G63910.
DR GeneID; 836512; -.
DR Gramene; AT5G63910.1; AT5G63910.1; AT5G63910.
DR KEGG; ath:AT5G63910; -.
DR Araport; AT5G63910; -.
DR TAIR; locus:2163966; AT5G63910.
DR eggNOG; ENOG502QSHJ; Eukaryota.
DR HOGENOM; CLU_021176_1_0_1; -.
DR InParanoid; P57681; -.
DR OMA; EYPRVTF; -.
DR OrthoDB; 1114069at2759; -.
DR PhylomeDB; P57681; -.
DR BioCyc; ARA:AT5G63910-MON; -.
DR BioCyc; MetaCyc:AT5G63910-MON; -.
DR BRENDA; 1.8.3.5; 399.
DR BRENDA; 1.8.3.6; 399.
DR PRO; PR:P57681; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P57681; baseline and differential.
DR Genevisible; P57681; AT.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0102149; F:farnesylcysteine lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0001735; F:prenylcysteine oxidase activity; IDA:TAIR.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IMP:TAIR.
DR GO; GO:0045338; P:farnesyl diphosphate metabolic process; IDA:TAIR.
DR GO; GO:0030327; P:prenylated protein catabolic process; IDA:TAIR.
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 1: Evidence at protein level;
KW FAD; Flavoprotein; Glycoprotein; Lysosome; Oxidoreductase;
KW Reference proteome; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..500
FT /note="Farnesylcysteine lyase"
FT /id="PRO_0000023303"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 500 AA; 55298 MW; E60B89C4990AB29A CRC64;
MKDFPIAISL LFALLSPVLL PCSGDSTGGV EDDSPATVCI VGSGIGGSSV AHFLRNYSVS
TGLNQAKILM FERHEIVGGR MRTVTVAGDT FEAGGSILHP KNYHVKDFVE RFNLTVRLPT
PIEESSAIGI WDGKRFVVKT FGSGTKFPFL DTIVSWVNDL YLFLRYGLSL LRMSSFIENT
VDNFLKYYES LESRPIFDNV EGMLKWSGLY NLTKLTLQEK LSEAQLSPLL VNELVTVITR
INYGQSVLIS GLAGAVSLAG SGGGLWSVEG GNWQMAAKLI NHSDVTLHLN EKIESISYLE
NHYELKSTKG NSYKCDVTVV ATPLDEVDIQ FSPTISIPKR ELQHTHTTFV RGLLNPGYFG
MKSLSDVPAL VGTLEDPLIP FSCISILRKY SKTDMTYKIF TRQPASDSLL DELFSRRTET
VRIDWGAYPK YHAPEVFAPF ILDDHHLYYV NAFENAASTM ETSAVAGENI ARLIISRFMT
KESLSSSDKR SCSSGLHSDS
