ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q9BY49


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name PECR_HUMAN
Primary accession number Q9BY49
Secondary accession numbers Q53TC4 Q6IAK9 Q9NRD4 Q9NY60 Q9P1A4
Integrated into Swiss-Prot on March 29, 2005
Sequence was last modified on March 29, 2005 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 63)
Name and origin of the protein
Protein name Peroxisomal trans-2-enoyl-CoA reductase
Synonyms EC 1.3.1.38
TERP
HPDHase
pVI-ARL
2,4-dienoyl-CoA reductase-related protein
DCR-RP
Gene name
Name: PECR
ORFNames: PRO1004
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND ENZYME ACTIVITY.
DOI=10.1074/jbc.M001168200; PubMed=10811639 [NCBI, ExPASy, EBI, Israel, Japan]
Das A.K., Uhler M.D., Hajra A.K.;
"Molecular cloning and expression of mammalian peroxisomal trans-2-enoyl-coenzyme A reductase cDNAs.";
J. Biol. Chem. 275:24333-24340(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, INTERACTION WITH PEX5, AND MUTAGENESIS OF LEU-303.
PubMed=11669066 [NCBI, ExPASy, EBI, Israel, Japan]
Amery L., Mannaerts G.P., Subramani S., Van Veldhoven P.P., Fransen M.;
"Identification of a novel human peroxisomal 2,4-dienoyl-CoA reductase related protein using the M13 phage protein VI phage display technology.";
Comb. Chem. High Throughput Screen. 4:545-552(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Liver;
Li Y., Wu T., Xu S., Ren S., Chen Z., Han Z.;
"A novel gene expressed in human liver non-tumor tissue.";
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Fetal liver;
Zhang C., Yu Y., Zhang S., Wei H., Zhang Y., Zhou G., Bi J., Liu M., He F.;
"Functional prediction of the coding sequences of 79 new genes deduced by analysis of cDNA clones from human fetal liver.";
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature03466; PubMed=15815621 [NCBI, ExPASy, EBI, Israel, Japan]
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2 and 4.";
Nature 434:724-731(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
INDUCTION.
DOI=10.1093/nar/30.8.1713; PubMed=11937624 [NCBI, ExPASy, EBI, Israel, Japan]
Braastad C.D., Leguia M., Hendrickson E.A.;
"Ku86 autoantigen related protein-1 transcription initiates from a CpG island and is induced by p53 through a nearby p53 response element.";
Nucleic Acids Res. 30:1713-1724(2002).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-179, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[10]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH ADENINE AND PHOSPHATE.
Structural genomics consortium (SGC);
"Crystal structure of perixomal trans 2-enoyl CoA reductase (PECRA).";
Submitted (MAY-2005) to the PDB data bank.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF232009; AAF69798.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ250303; CAB89810.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF212234; AAK14920.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF119841; AAF69595.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR457145; CAG33426.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC010686; AAY14657.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC002529; AAH02529.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_060911.2; -.
UniGene Hs.281680
3D structure databases
PDB
1YXM; X-ray; 1.90 A; A/B/C/D=1-303.[ExPASy / RCSB / EBI]
PDBsum 1YXM; -.
ModBase Q9BY49.
PTM databases
PhosphoSite Q9BY49; -.
Organism-specific databases
H-InvDB HIX0002806; -.
HGNC HGNC:18281; PECR.
GenAtlas PECR.
MIM 605843; gene. [NCBI / EBI]
PharmGKB PA134967510; -.
GeneCards Q9BY49.
Gene expression databases
ArrayExpress Q9BY49; -.
CleanEx HS_PECR; -.
GermOnline ENSG00000115425; Homo sapiens.
Ontologies
GO
GO:0005777; Cellular component: peroxisome (non-traceable author statement from ProtInc).
GO:0006631; Biological process: fatty acid metabolic process (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR000712; Bcl2_BH.
IPR002198; DHase_sc/Rdtase_SDR.
IPR002347; Glc/ribitol_DHase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
PANTHER PTHR19410; ADH_short_C2; 1.
Pfam PF00106; adh_short; 1.
Pfam graphical view of domain structure.
PRINTS PR00081; GDHRDH.
PR00080; SDRFAMILY.
SMART SM00337; BCL; 1.
SMART graphical view of domain structure.
PROSITE PS00061; ADH_SHORT; FALSE_NEG.
BLOCKS Q9BY49.
Genome annotation databases
Ensembl ENSG00000115425; Homo sapiens. [Contig view]
GeneID 55825; -.
KEGG hsa:55825; -.
Phylogenomic databases
HOGENOM Q9BY49; -.
HOVERGEN Q9BY49; -.
Other
DrugBank DB00173; Adenine.
SOURCE PECR; Homo sapiens.
ProtoNet Q9BY49.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Fatty acid biosynthesis; Lipid synthesis; NADP; Oxidoreductase; Peroxisome; Phosphoprotein; Polymorphism.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   303  303     Peroxisomal trans-2-enoyl-CoA reductase. PRO_0000054740
NP_BIND   23    47  25     NADP (By similarity). 
MOTIF   301   303  3     Microbody targeting signal. 
ACT_SITE   179   179        Proton acceptor (By similarity). 
MOD_RES   179   179        Phosphotyrosine. 
VAR_SEQ   1   146        Missing (in isoform 2). VSP_013260
VARIANT   149   149  1     E -> K (in dbSNP:rs1429148 [NCBI]). VAR_021535 
VARIANT   297   297  1     F -> L (in dbSNP:rs9288513 [NCBI]). VAR_021536 
MUTAGEN   303   303        Missing: Abolishes localization to peroxisomes. 
CONFLICT   22    22        I -> F (in Ref. 2; CAB89810). 
CONFLICT   129   129        E -> R (in Ref. 2; CAB89810). 
CONFLICT   135   135        T -> S (in Ref. 2; CAB89810). 
CONFLICT   248   248        S -> P (in Ref. 5; CAG33426). 
TURN   13    18  6      
STRAND   20    24  5      
TURN   25    27  3      
HELIX   29    40  12      
STRAND   44    50  7      
HELIX   52    64  13      
STRAND   74    78  5      
HELIX   84    98  15      
STRAND   103   106  4      
HELIX   116   118  3      
HELIX   121   131  11      
HELIX   133   145  13      
HELIX   147   150  4      
STRAND   152   157  6      
HELIX   169   188  20      
HELIX   190   192  3      
STRAND   194   201  8      
HELIX   208   210  3      
HELIX   214   221  8      
HELIX   224   227  4      
HELIX   237   247  11      
HELIX   249   251  3      
STRAND   258   262  5      
HELIX   265   267  3      
HELIX   288   302  15      
Sequence information
Length: 303 AA [This is the length of the unprocessed precursor] Molecular weight: 32544 Da [This is the MW of the unprocessed precursor] CRC64: BCCE6AB89F58382C [This is a checksum on the sequence]
        10         20         30         40         50         60 
MASWAKGRSY LAPGLLQGQV AIVTGGATGI GKAIVKELLE LGSNVVIASR KLERLKSAAD 

        70         80         90        100        110        120 
ELQANLPPTK QARVIPIQCN IRNEEEVNNL VKSTLDTFGK INFLVNNGGG QFLSPAEHIS 

       130        140        150        160        170        180 
SKGWHAVLET NLTGTFYMCK AVYSSWMKEH GGSIVNIIVP TKAGFPLAVH SGAARAGVYN 

       190        200        210        220        230        240 
LTKSLALEWA CSGIRINCVA PGVIYSQTAV ENYGSWGQSF FEGSFQKIPA KRIGVPEEVS 

       250        260        270        280        290        300 
SVVCFLLSPA ASFITGQSVD VDGGRSLYTH SYEVPDHDNW PKGAGDLSVV KKMKETFKEK 


AKL 

Q9BY49 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!