Reviewed, UniProtKB/Swiss-Prot Q9BY49 (PECR_HUMAN)

Names and origin

Protein names

Recommended name:
    Peroxisomal trans-2-enoyl-CoA reductase
    EC=1.3.1.38
Alternative name(s):
    TERP
    HPDHase
    pVI-ARL
    2,4-dienoyl-CoA reductase-related protein
      Short name=DCR-RP

Gene names

Name:	PECR
ORF Names:	PRO1004

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	303 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis
Cellular component	Peroxisome
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	NADP
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW regulation of apoptosis Inferred from electronic annotation. Source: InterPro
Cellular component	peroxisome Ref.1 Non-traceable author statement. Source: ProtInc
Molecular function	binding Inferred from electronic annotation. Source: InterPro trans-2-enoyl-CoA reductase (NADPH) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

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:
     1-146: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 303

303

Peroxisomal trans-2-enoyl-CoA reductase

PRO_0000054740

Regions

Nucleotide binding

23 – 47

25

NADP By similarity

Motif

301 – 303

3

Microbody targeting signal

Sites

Active site

179

1

Proton acceptor By similarity

Amino acid modifications

Modified residue

179

1

Phosphotyrosine Ref.10

Natural variations

Alternative sequence

1 – 146

146

Missing in isoform 2.

VSP_013260

Natural variant

149

1

E → K: dbSNP rs1429148.

VAR_021535

Natural variant

297

1

F → L: dbSNP rs9288513.

VAR_021536

Experimental info

Mutagenesis

303

1

Missing: Abolishes localization to peroxisomes. Ref.2

Sequence conflict

22

1

I → F in CAB89810. Ref.2

Sequence conflict

129

1

E → R in CAB89810. Ref.2

Sequence conflict

135

1

T → S in CAB89810. Ref.2

Sequence conflict

248

1

S → P in CAG33426. Ref.5

Secondary structure

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303

Helix Strand Turn

Details...

Turn

13 – 18

6

Beta strand

20 – 24

5

Turn

25 – 27

3

Helix

29 – 40

12

Beta strand

44 – 50

7

Helix

52 – 64

13

Beta strand

74 – 78

5

Helix

84 – 98

15

Beta strand

103 – 106

4

Helix

116 – 118

3

Helix

121 – 131

11

Helix

133 – 145

13

Helix

147 – 150

4

Beta strand

152 – 157

6

Helix

169 – 188

20

Helix

190 – 192

3

Beta strand

194 – 201

8

Helix

208 – 210

3

Helix

214 – 221

8

Helix

224 – 227

4

Helix

237 – 247

11

Helix

249 – 251

3

Beta strand

258 – 262

5

Helix

265 – 267

3

Helix

288 – 302

15

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 29, 2005. Version 2. Checksum: BCCE6AB89F58382C	FASTA	303	32,544
	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
	Isoform 2. Checksum: 8215EB7A51D81D48	FASTA	157	16,834
	10 20 30 40 50 60 MKEHGGSIVN IIVPTKAGFP LAVHSGAARA GVYNLTKSLA LEWACSGIRI NCVAPGVIYS 70 80 90 100 110 120 QTAVENYGSW GQSFFEGSFQ KIPAKRIGVP EEVSSVVCFL LSPAASFITG QSVDVDGGRS 130 140 150 LYTHSYEVPD HDNWPKGAGD LSVVKKMKET FKEKAKL

References

	« Hide 'large scale' referencesShow '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: 10811639] [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: 11669066] [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 tissue." 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. , 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: 14702039] [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. , 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: 15815621] [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: 15489334] [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: 11937624] [Abstract] Cited for: INDUCTION.
[10]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." 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. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-179, MASS SPECTROMETRY.
[11]	"Crystal structure of perixomal 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

EMBLGenBankDDBJ

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.

IPI

IPI00554710.
IPI00744627.

RefSeq

NP_060911.2.

UniGene

Hs.281680

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1YXM	X-ray	1.90	A/B/C/D	1-303	[»]

ModBase

Search...

PTM databases

PhosphoSite

Q9BY49.

Proteomic databases

PRIDE

Q9BY49.

Genome annotation databases

Ensembl

ENSG00000115425. Homo sapiens. [Contig view]

GeneID

55825.

KEGG

hsa:55825.

UCSC

uc002vfr.1. human.
uc002vft.1. human.

Organism-specific databases

GeneCards

GC02M216611.

H-InvDB

HIX0002806.

HGNC

HGNC:18281. PECR.

MIM

605843. gene.

PharmGKB

PA134967510.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q9BY49.

HOVERGEN

Q9BY49.

OMA

Q9BY49. ARVIPIQ.

Enzyme and pathway databases

BRENDA

1.3.1.38. 247.

Gene expression databases

ArrayExpress

Q9BY49.

Bgee

Q9BY49.

CleanEx

HS_PECR.

GermOnline

ENSG00000115425. Homo sapiens.

Family and domain databases

InterPro

IPR000712. Bcl2_BH.
IPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

PANTHER

PTHR19410. ADH_short_C2. 1 hit.

Pfam

PF00106. adh_short. 1 hit.
[Graphical view]

PRINTS

PR00081. GDHRDH.

SMART

SM00337. BCL. 1 hit.
[Graphical view]

PROSITE

PS00061. ADH_SHORT. False negative.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00173. Adenine.

NextBio

61022.

SOURCE

Search...

Entry information

Entry name

PECR_HUMAN

Accession

Primary (citable) accession number: Q9BY49
Secondary accession number(s): B2RE42 , Q53TC4, Q6IAK9, Q9NRD4, Q9NY60, Q9P1A4

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2005
Last sequence update:	March 29, 2005
Last modified:	July 7, 2009
This is version 72 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)