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Q9BY49 (PECR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peroxisomal trans-2-enoyl-CoA reductase

Short name=TERP
EC=1.3.1.38
Alternative name(s):
2,4-dienoyl-CoA reductase-related protein
Short name=DCR-RP
HPDHase
pVI-ARL
Gene names
Name:PECR
ORF Names:PRO1004
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length303 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Participates in chain elongation of fatty acids. Has no 2,4-dienoyl-CoA reductase activity.

Catalytic activity

Acyl-CoA + NADP+ = trans-2,3-dehydroacyl-CoA + NADPH. Ref.1

Pathway

Lipid metabolism; fatty acid biosynthesis.

Subunit structure

Interacts with PEX5, probably required to target it into peroxisomes. Ref.2

Subcellular location

Peroxisome Ref.2.

Induction

Not induced by IR. Ref.9

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Sequence caution

The sequence AAF69798.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BY49-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9BY49-2)

The sequence of this isoform differs from the canonical sequence as follows:
     2-146: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 303302Peroxisomal trans-2-enoyl-CoA reductase
PRO_0000054740

Regions

Nucleotide binding23 – 4725NADP By similarity
Motif301 – 3033Microbody targeting signal

Sites

Active site1791Proton acceptor By similarity

Amino acid modifications

Modified residue321N6-succinyllysine By similarity

Natural variations

Alternative sequence2 – 146145Missing in isoform 2.
VSP_013260
Natural variant1491E → K.
Corresponds to variant rs1429148 [ dbSNP | Ensembl ].
VAR_021535
Natural variant2971F → L.
Corresponds to variant rs9288513 [ dbSNP | Ensembl ].
VAR_021536

Experimental info

Mutagenesis3031Missing: Abolishes localization to peroxisomes. Ref.2
Sequence conflict221I → F in CAB89810. Ref.2
Sequence conflict1291E → R in CAB89810. Ref.2
Sequence conflict1351T → S in CAB89810. Ref.2
Sequence conflict2481S → P in CAG33426. Ref.5

Secondary structure

.................................................. 303
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 29, 2005. Version 2.
Checksum: BCCE6AB89F58382C

FASTA30332,544
        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 

« Hide

Isoform 2 [UniParc].

Checksum: B21C1B1AC8F8A095
Show »

FASTA15816,965

References

« Hide 'large scale' references
[1]"Molecular cloning and expression of mammalian peroxisomal trans-2-enoyl-coenzyme A reductase cDNAs."
Das A.K., Uhler M.D., Hajra A.K.
J. Biol. Chem. 275:24333-24340(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME ACTIVITY.
[2]"Identification of a novel human peroxisomal 2,4-dienoyl-CoA reductase related protein using the M13 phage protein VI phage display technology."
Amery L., Mannaerts G.P., Subramani S., Van Veldhoven P.P., Fransen M.
Comb. Chem. High Throughput Screen. 4:545-552(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, INTERACTION WITH PEX5, MUTAGENESIS OF LEU-303.
[3]"A novel gene expressed in human liver non-tumor tissues."
Li Y., Wu T., Xu S., Ren S., Chen Z., Han Z.
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Liver.
[4]"Functional prediction of the coding sequences of 79 new genes deduced by analysis of cDNA clones from human fetal liver."
Zhang C., Yu Y., Zhang S., Wei H., Zhang Y., Zhou G., Bi J., Liu M., He F.
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Fetal liver.
[5]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[6]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Colon.
[7]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
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. expand/collapse author list , 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.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Placenta.
[9]"Ku86 autoantigen related protein-1 transcription initiates from a CpG island and is induced by p53 through a nearby p53 response element."
Braastad C.D., Leguia M., Hendrickson E.A.
Nucleic Acids Res. 30:1713-1724(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[10]"Crystal structure of peroxisomal trans 2-enoyl CoA reductase (PECRA)."
Structural genomics consortium (SGC)
Submitted (MAY-2005) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH ADENINE AND PHOSPHATE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF232009 mRNA. Translation: AAF69798.1. Different initiation.
AJ250303 mRNA. Translation: CAB89810.1.
AF212234 mRNA. Translation: AAK14920.1.
AF119841 mRNA. Translation: AAF69595.1.
CR457145 mRNA. Translation: CAG33426.1.
AK315795 mRNA. Translation: BAG38139.1.
AC010686 Genomic DNA. Translation: AAY14657.1.
BC002529 mRNA. Translation: AAH02529.1.
CCDSCCDS33375.1. [Q9BY49-1]
RefSeqNP_060911.2. NM_018441.5. [Q9BY49-1]
UniGeneHs.281680.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YXMX-ray1.90A/B/C/D1-303[»]
ProteinModelPortalQ9BY49.
SMRQ9BY49. Positions 7-303.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120932. 2 interactions.
IntActQ9BY49. 1 interaction.
STRING9606.ENSP00000265322.

Chemistry

DrugBankDB00173. Adenine.

PTM databases

PhosphoSiteQ9BY49.

Polymorphism databases

DMDM62287123.

Proteomic databases

MaxQBQ9BY49.
PaxDbQ9BY49.
PRIDEQ9BY49.

Protocols and materials databases

DNASU55825.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265322; ENSP00000265322; ENSG00000115425. [Q9BY49-1]
GeneID55825.
KEGGhsa:55825.
UCSCuc002vft.3. human. [Q9BY49-1]

Organism-specific databases

CTD55825.
GeneCardsGC02M216867.
HGNCHGNC:18281. PECR.
HPAHPA021593.
HPA022539.
MIM605843. gene.
neXtProtNX_Q9BY49.
PharmGKBPA134967510.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1028.
HOVERGENHBG105268.
InParanoidQ9BY49.
KOK07753.
OMAGVNRKIP.
PhylomeDBQ9BY49.
TreeFamTF315256.

Enzyme and pathway databases

BioCycMetaCyc:HS03889-MONOMER.
UniPathwayUPA00094.

Gene expression databases

ArrayExpressQ9BY49.
BgeeQ9BY49.
CleanExHS_PECR.
GenevestigatorQ9BY49.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PRINTSPR00081. GDHRDH.
ProtoNetSearch...

Other

EvolutionaryTraceQ9BY49.
GeneWikiPECR.
GenomeRNAi55825.
NextBio61022.
PROQ9BY49.
SOURCESearch...

Entry information

Entry namePECR_HUMAN
AccessionPrimary (citable) accession number: Q9BY49
Secondary accession number(s): B2RE42 expand/collapse secondary AC list , Q53TC4, Q6IAK9, Q9NRD4, Q9NY60, Q9P1A4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: March 29, 2005
Last modified: July 9, 2014
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM