PCYXL_HUMAN
ID PCYXL_HUMAN Reviewed; 494 AA.
AC Q8NBM8; Q7Z4S2; Q8NCY5; Q8NF69; Q9BTE8; Q9BWS3;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Prenylcysteine oxidase-like;
DE EC=1.8.3.-;
DE Flags: Precursor;
GN Name=PCYOX1L; ORFNames=PSEC0105;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT PRO-5.
RC TISSUE=Teratocarcinoma;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA She X., Guo J.H., Yu L.;
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 173-494 (ISOFORM 1), AND VARIANT ASP-390.
RC TISSUE=Kidney, and Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 23-37.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 31-494, AND VARIANT ASP-390.
RC TISSUE=Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 157-494 (ISOFORM 1).
RC TISSUE=Spleen;
RA Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.;
RT "The nucleotide sequence of a long cDNA clone isolated from human spleen.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Probable oxidoreductase. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8NBM8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NBM8-2; Sequence=VSP_039271, VSP_039272;
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the prenylcysteine oxidase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH00014.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
CC Sequence=AAP97684.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
CC Sequence=BAC03391.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AK075414; BAC11604.1; -; mRNA.
DR EMBL; AF451985; AAP97684.1; ALT_SEQ; mRNA.
DR EMBL; AC131025; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000014; AAH00014.1; ALT_SEQ; mRNA.
DR EMBL; BC004166; AAH04166.3; -; mRNA.
DR EMBL; AL834220; CAD38901.2; -; mRNA.
DR EMBL; AK090410; BAC03391.1; ALT_SEQ; mRNA.
DR CCDS; CCDS4296.1; -. [Q8NBM8-1]
DR RefSeq; NP_001287983.1; NM_001301054.1.
DR RefSeq; NP_001287986.1; NM_001301057.1.
DR RefSeq; NP_076933.3; NM_024028.3. [Q8NBM8-1]
DR AlphaFoldDB; Q8NBM8; -.
DR BioGRID; 122462; 38.
DR IntAct; Q8NBM8; 9.
DR STRING; 9606.ENSP00000274569; -.
DR GlyGen; Q8NBM8; 1 site.
DR iPTMnet; Q8NBM8; -.
DR PhosphoSitePlus; Q8NBM8; -.
DR BioMuta; PCYOX1L; -.
DR DMDM; 298286841; -.
DR EPD; Q8NBM8; -.
DR jPOST; Q8NBM8; -.
DR MassIVE; Q8NBM8; -.
DR MaxQB; Q8NBM8; -.
DR PaxDb; Q8NBM8; -.
DR PeptideAtlas; Q8NBM8; -.
DR PRIDE; Q8NBM8; -.
DR ProteomicsDB; 72797; -. [Q8NBM8-1]
DR Antibodypedia; 27814; 78 antibodies from 18 providers.
DR DNASU; 78991; -.
DR Ensembl; ENST00000274569.9; ENSP00000274569.4; ENSG00000145882.11. [Q8NBM8-1]
DR Ensembl; ENST00000505669.5; ENSP00000427166.1; ENSG00000145882.11. [Q8NBM8-2]
DR Ensembl; ENST00000511945.5; ENSP00000426091.1; ENSG00000145882.11. [Q8NBM8-2]
DR GeneID; 78991; -.
DR KEGG; hsa:78991; -.
DR MANE-Select; ENST00000274569.9; ENSP00000274569.4; NM_024028.4; NP_076933.3.
DR UCSC; uc003lqk.3; human. [Q8NBM8-1]
DR CTD; 78991; -.
DR DisGeNET; 78991; -.
DR GeneCards; PCYOX1L; -.
DR HGNC; HGNC:28477; PCYOX1L.
DR HPA; ENSG00000145882; Tissue enhanced (parathyroid).
DR neXtProt; NX_Q8NBM8; -.
DR OpenTargets; ENSG00000145882; -.
DR PharmGKB; PA147357517; -.
DR VEuPathDB; HostDB:ENSG00000145882; -.
DR eggNOG; ENOG502QSHJ; Eukaryota.
DR GeneTree; ENSGT00390000011206; -.
DR HOGENOM; CLU_021176_1_0_1; -.
DR InParanoid; Q8NBM8; -.
DR OMA; NLWSVEG; -.
DR OrthoDB; 1114069at2759; -.
DR PhylomeDB; Q8NBM8; -.
DR TreeFam; TF329001; -.
DR PathwayCommons; Q8NBM8; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR SignaLink; Q8NBM8; -.
DR BioGRID-ORCS; 78991; 22 hits in 1072 CRISPR screens.
DR ChiTaRS; PCYOX1L; human.
DR GenomeRNAi; 78991; -.
DR Pharos; Q8NBM8; Tdark.
DR PRO; PR:Q8NBM8; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q8NBM8; protein.
DR Bgee; ENSG00000145882; Expressed in middle temporal gyrus and 188 other tissues.
DR ExpressionAtlas; Q8NBM8; baseline and differential.
DR Genevisible; Q8NBM8; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
DR GO; GO:0001735; F:prenylcysteine oxidase activity; IBA:GO_Central.
DR GO; GO:0030327; P:prenylated protein catabolic process; IBA:GO_Central.
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 Alternative splicing; Direct protein sequencing; FAD; Flavoprotein;
KW Glycoprotein; Oxidoreductase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 23..494
FT /note="Prenylcysteine oxidase-like"
FT /id="PRO_0000280286"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 30..82
FT /note="AVVGAGIGGSAVAHFLQQHFGPRVQIDVYEKGTVGGRLATISVNKQHYESGA
FT A -> GAGRTRGGWGWDWGLCCGPFSPAALWTSGADRRVREGNRGWPLGHHLSQQAAL
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_039271"
FT VAR_SEQ 83..494
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_039272"
FT VARIANT 5
FT /note="A -> P (in dbSNP:rs2291814)"
FT /evidence="ECO:0000269|PubMed:16303743"
FT /id="VAR_031110"
FT VARIANT 316
FT /note="A -> T (in dbSNP:rs35552800)"
FT /id="VAR_050472"
FT VARIANT 390
FT /note="E -> D (in dbSNP:rs4705336)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_031111"
FT CONFLICT 338
FT /note="H -> P (in Ref. 7; BAC03391)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="R -> P (in Ref. 7; BAC03391)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 494 AA; 54646 MW; 18C03FA338D65C9D CRC64;
MARAAPLLAA LTALLAAAAA GGDAPPGKIA VVGAGIGGSA VAHFLQQHFG PRVQIDVYEK
GTVGGRLATI SVNKQHYESG AASFHSLSLH MQDFVKLLGL RHRREVVGRS AIFGGEHFML
EETDWYLLNL FRLWWHYGIS FLRLQMWVEE VMEKFMRIYK YQAHGYAFSG VEELLYSLGE
STFVNMTQHS VAESLLQVGV TQRFIDDVVS AVLRASYGQS AAMPAFAGAM SLAGAQGSLW
SVEGGNKLVC SGLLKLTKAN VIHATVTSVT LHSTEGKALY QVAYENEVGN SSDFYDIVVI
ATPLHLDNSS SNLTFAGFHP PIDDVQGSFQ PTVVSLVHGY LNSSYFGFPD PKLFPFANIL
TTDFPSFFCT LDNICPVNIS ASFRRKQPQE AAVWRVQSPK PLFRTQLKTL FRSYYSVQTA
EWQAHPLYGS RPTLPRFALH DQLFYLNALE WAASSVEVMA VAAKNVALLA YNRWYQDLDK
IDQKDLMHKV KTEL
