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Q9BY49

- PECR_HUMAN

UniProt

Q9BY49 - PECR_HUMAN

Protein

Peroxisomal trans-2-enoyl-CoA reductase

Gene

PECR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 2 (29 Mar 2005)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei179 – 1791Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi23 – 4725NADPBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. receptor binding Source: UniProtKB
    2. trans-2-enoyl-CoA reductase (NADPH) activity Source: UniProtKB

    GO - Biological processi

    1. fatty acid biosynthetic process Source: UniProtKB-UniPathway
    2. oxidation-reduction process Source: UniProtKB
    3. phytol metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciMetaCyc:HS03889-MONOMER.
    UniPathwayiUPA00094.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peroxisomal trans-2-enoyl-CoA reductase (EC:1.3.1.38)
    Short name:
    TERP
    Alternative name(s):
    2,4-dienoyl-CoA reductase-related protein
    Short name:
    DCR-RP
    HPDHase
    pVI-ARL
    Gene namesi
    Name:PECR
    ORF Names:PRO1004
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:18281. PECR.

    Subcellular locationi

    Peroxisome 1 Publication

    GO - Cellular componenti

    1. intracellular membrane-bounded organelle Source: HPA
    2. mitochondrion Source: Ensembl
    3. peroxisomal membrane Source: UniProtKB
    4. peroxisome Source: UniProtKB

    Keywords - Cellular componenti

    Peroxisome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi303 – 3031Missing: Abolishes localization to peroxisomes. 1 Publication

    Organism-specific databases

    PharmGKBiPA134967510.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 303302Peroxisomal trans-2-enoyl-CoA reductasePRO_0000054740Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei32 – 321N6-succinyllysineBy similarity

    Proteomic databases

    MaxQBiQ9BY49.
    PaxDbiQ9BY49.
    PRIDEiQ9BY49.

    PTM databases

    PhosphoSiteiQ9BY49.

    Expressioni

    Inductioni

    Not induced by IR.1 Publication

    Gene expression databases

    ArrayExpressiQ9BY49.
    BgeeiQ9BY49.
    CleanExiHS_PECR.
    GenevestigatoriQ9BY49.

    Organism-specific databases

    HPAiHPA021593.
    HPA022539.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi120932. 2 interactions.
    IntActiQ9BY49. 1 interaction.
    STRINGi9606.ENSP00000265322.

    Structurei

    Secondary structure

    1
    303
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni13 – 186
    Beta strandi20 – 245
    Turni25 – 273
    Helixi29 – 4012
    Beta strandi44 – 507
    Helixi52 – 6413
    Beta strandi74 – 785
    Helixi84 – 9815
    Beta strandi103 – 1064
    Helixi116 – 1183
    Helixi121 – 13111
    Helixi133 – 14513
    Helixi147 – 1504
    Beta strandi152 – 1576
    Helixi169 – 18820
    Helixi190 – 1923
    Beta strandi194 – 2018
    Helixi208 – 2103
    Helixi214 – 2218
    Helixi224 – 2274
    Helixi237 – 24711
    Helixi249 – 2513
    Beta strandi258 – 2625
    Helixi265 – 2673
    Helixi288 – 30215

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1YXMX-ray1.90A/B/C/D1-303[»]
    ProteinModelPortaliQ9BY49.
    SMRiQ9BY49. Positions 7-303.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9BY49.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi301 – 3033Microbody targeting signal

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1028.
    HOVERGENiHBG105268.
    InParanoidiQ9BY49.
    KOiK07753.
    OMAiGVNRKIP.
    PhylomeDBiQ9BY49.
    TreeFamiTF315256.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR002347. Glc/ribitol_DH.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PRINTSiPR00081. GDHRDH.

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9BY49-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MASWAKGRSY LAPGLLQGQV AIVTGGATGI GKAIVKELLE LGSNVVIASR    50
    KLERLKSAAD ELQANLPPTK QARVIPIQCN IRNEEEVNNL VKSTLDTFGK 100
    INFLVNNGGG QFLSPAEHIS SKGWHAVLET NLTGTFYMCK AVYSSWMKEH 150
    GGSIVNIIVP TKAGFPLAVH SGAARAGVYN LTKSLALEWA CSGIRINCVA 200
    PGVIYSQTAV ENYGSWGQSF FEGSFQKIPA KRIGVPEEVS SVVCFLLSPA 250
    ASFITGQSVD VDGGRSLYTH SYEVPDHDNW PKGAGDLSVV KKMKETFKEK 300
    AKL 303
    Length:303
    Mass (Da):32,544
    Last modified:March 29, 2005 - v2
    Checksum:iBCCE6AB89F58382C
    GO
    Isoform 2 (identifier: Q9BY49-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:158
    Mass (Da):16,965
    Checksum:iB21C1B1AC8F8A095
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti22 – 221I → F in CAB89810. (PubMed:11669066)Curated
    Sequence conflicti129 – 1291E → R in CAB89810. (PubMed:11669066)Curated
    Sequence conflicti135 – 1351T → S in CAB89810. (PubMed:11669066)Curated
    Sequence conflicti248 – 2481S → P in CAG33426. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti149 – 1491E → K.
    Corresponds to variant rs1429148 [ dbSNP | Ensembl ].
    VAR_021535
    Natural varianti297 – 2971F → L.
    Corresponds to variant rs9288513 [ dbSNP | Ensembl ].
    VAR_021536

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei2 – 146145Missing in isoform 2. 2 PublicationsVSP_013260Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS33375.1. [Q9BY49-1]
    RefSeqiNP_060911.2. NM_018441.5. [Q9BY49-1]
    UniGeneiHs.281680.

    Genome annotation databases

    EnsembliENST00000265322; ENSP00000265322; ENSG00000115425. [Q9BY49-1]
    GeneIDi55825.
    KEGGihsa:55825.
    UCSCiuc002vft.3. human. [Q9BY49-1]

    Polymorphism databases

    DMDMi62287123.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS33375.1. [Q9BY49-1 ]
    RefSeqi NP_060911.2. NM_018441.5. [Q9BY49-1 ]
    UniGenei Hs.281680.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1YXM X-ray 1.90 A/B/C/D 1-303 [» ]
    ProteinModelPortali Q9BY49.
    SMRi Q9BY49. Positions 7-303.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120932. 2 interactions.
    IntActi Q9BY49. 1 interaction.
    STRINGi 9606.ENSP00000265322.

    Chemistry

    DrugBanki DB00173. Adenine.

    PTM databases

    PhosphoSitei Q9BY49.

    Polymorphism databases

    DMDMi 62287123.

    Proteomic databases

    MaxQBi Q9BY49.
    PaxDbi Q9BY49.
    PRIDEi Q9BY49.

    Protocols and materials databases

    DNASUi 55825.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265322 ; ENSP00000265322 ; ENSG00000115425 . [Q9BY49-1 ]
    GeneIDi 55825.
    KEGGi hsa:55825.
    UCSCi uc002vft.3. human. [Q9BY49-1 ]

    Organism-specific databases

    CTDi 55825.
    GeneCardsi GC02M216867.
    HGNCi HGNC:18281. PECR.
    HPAi HPA021593.
    HPA022539.
    MIMi 605843. gene.
    neXtProti NX_Q9BY49.
    PharmGKBi PA134967510.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1028.
    HOVERGENi HBG105268.
    InParanoidi Q9BY49.
    KOi K07753.
    OMAi GVNRKIP.
    PhylomeDBi Q9BY49.
    TreeFami TF315256.

    Enzyme and pathway databases

    UniPathwayi UPA00094 .
    BioCyci MetaCyc:HS03889-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q9BY49.
    GeneWikii PECR.
    GenomeRNAii 55825.
    NextBioi 61022.
    PROi Q9BY49.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BY49.
    Bgeei Q9BY49.
    CleanExi HS_PECR.
    Genevestigatori Q9BY49.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    InterProi IPR002347. Glc/ribitol_DH.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    PRINTSi PR00081. GDHRDH.
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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.

    Entry informationi

    Entry nameiPECR_HUMAN
    AccessioniPrimary (citable) accession number: Q9BY49
    Secondary accession number(s): B2RE42
    , Q53TC4, Q6IAK9, Q9NRD4, Q9NY60, Q9P1A4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2005
    Last sequence update: March 29, 2005
    Last modified: October 1, 2014
    This is version 120 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3