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Q00493

- CBPE_MOUSE

UniProt

Q00493 - CBPE_MOUSE

Protein

Carboxypeptidase E

Gene

Cpe

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 2 (15 Jul 1998)
      Previous versions | rss
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    Functioni

    Removes residual C-terminal Arg or Lys remaining after initial endoprotease cleavage during prohormone processing. Processes proinsulin.

    Catalytic activityi

    Release of C-terminal arginine or lysine residues from polypeptides.

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi114 – 1141ZincBy similarity
    Metal bindingi117 – 1171ZincBy similarity
    Metal bindingi248 – 2481ZincBy similarity
    Active sitei342 – 3421NucleophileBy similarity

    GO - Molecular functioni

    1. carboxypeptidase activity Source: MGI
    2. metallocarboxypeptidase activity Source: InterPro
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cardiac left ventricle morphogenesis Source: Ensembl
    2. insulin processing Source: MGI
    3. protein localization to membrane Source: Ensembl

    Keywords - Molecular functioni

    Carboxypeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_207837. Insulin processing.

    Protein family/group databases

    MEROPSiM14.005.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carboxypeptidase E (EC:3.4.17.10)
    Short name:
    CPE
    Alternative name(s):
    Carboxypeptidase H
    Short name:
    CPH
    Enkephalin convertase
    Prohormone-processing carboxypeptidase
    Gene namesi
    Name:Cpe
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:101932. Cpe.

    Subcellular locationi

    Cytoplasmic vesiclesecretory vesicle membrane By similarity; Peripheral membrane protein By similarity. Secreted By similarity
    Note: Associated with the secretory granule membrane through direct binding to lipid rafts in intragranular conditions. This binding is Ca2+-dependent By similarity.By similarity

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell
    2. Golgi apparatus Source: Ensembl
    3. transport vesicle membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasmic vesicle, Membrane, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Defects in Cpe are the cause of the fat phenotype. Mice homozygous for the fat mutation develop obesity and hyperglycemia that can be suppressed by treatment with exogenous insulin.

    Keywords - Diseasei

    Disease mutation

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2727By similarityAdd
    BLAST
    Propeptidei28 – 4215Activation peptideBy similarityPRO_0000004386Add
    BLAST
    Chaini43 – 476434Carboxypeptidase EPRO_0000004387Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi139 – 1391N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi390 – 3901N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Cleavage on pair of basic residues, Glycoprotein, Zymogen

    Proteomic databases

    MaxQBiQ00493.
    PaxDbiQ00493.
    PRIDEiQ00493.

    PTM databases

    PhosphoSiteiQ00493.

    Expressioni

    Gene expression databases

    ArrayExpressiQ00493.
    BgeeiQ00493.
    CleanExiMM_CPE.
    GenevestigatoriQ00493.

    Interactioni

    Protein-protein interaction databases

    BioGridi198855. 1 interaction.
    IntActiQ00493. 3 interactions.
    MINTiMINT-4090042.

    Structurei

    3D structure databases

    ProteinModelPortaliQ00493.
    SMRiQ00493. Positions 49-450.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M14 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG322453.
    HOGENOMiHOG000232185.
    HOVERGENiHBG003410.
    InParanoidiQ00493.
    KOiK01294.
    OMAiTIVNLIH.
    OrthoDBiEOG7B8S32.
    PhylomeDBiQ00493.
    TreeFamiTF315592.

    Family and domain databases

    Gene3Di2.60.40.1120. 1 hit.
    InterProiIPR008969. CarboxyPept-like_regulatory.
    IPR014766. CarboxyPept_regulatory_dom.
    IPR000834. Peptidase_M14.
    [Graphical view]
    PfamiPF00246. Peptidase_M14. 1 hit.
    [Graphical view]
    PRINTSiPR00765. CRBOXYPTASEA.
    SMARTiSM00631. Zn_pept. 1 hit.
    [Graphical view]
    SUPFAMiSSF49464. SSF49464. 1 hit.
    PROSITEiPS00132. CARBOXYPEPT_ZN_1. 1 hit.
    PS00133. CARBOXYPEPT_ZN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q00493-1 [UniParc]FASTAAdd to Basket

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    MAGRGGRVLL ALCAALVAGG WLLTAEAQEP GAPAAGMRRR RRLQQEDGIS    50
    FEYHRYPELR EALVSVWLQC TAISRIYTVG RSFEGRELLV IELSDNPGVH 100
    EPGEPEFKYI GNMHGNEAVG RELLIFLAQY LCNEYQKGNE TIVNLIHSTR 150
    IHIMPSLNPD GFEKAASQPG ELKDWFVGRS NAQGIDLNRN FPDLDRIVYV 200
    NEKEGGPNNH LLKNLKKIVD QNSKLAPETK AVIHWIMDIP FVLSANLHGG 250
    DLVANYPYDE TRSGTAHEYS SCPDDAIFQS LARAYSSFNP VMSDPNRPPC 300
    RKNDDDSSFV DGTTNGGAWY SVPGGMQDFN YLSSNCFEIT VELSCEKFPP 350
    EETLKSYWED NKNSLISYLE QIHRGVKGFV RDLQGNPIAN ATISVDGIDH 400
    DVTSAKDGDY WRLLAPGNYK LTASAPGYLA ITKKVAVPFS PAVGVDFELE 450
    SFSERKEEEK EELMEWWKMM SETLNF 476
    Length:476
    Mass (Da):53,256
    Last modified:July 15, 1998 - v2
    Checksum:i82C5318A12A17567
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti25 – 251A → R in CAA43550. 1 PublicationCurated
    Sequence conflicti81 – 811R → A in CAA43550. 1 PublicationCurated
    Sequence conflicti167 – 1671S → W in CAA43550. 1 PublicationCurated
    Sequence conflicti171 – 1711E → Q in CAA43550. 1 PublicationCurated
    Sequence conflicti301 – 3011R → C in CAA43550. 1 PublicationCurated
    Sequence conflicti310 – 3101V → D in CAA43550. 1 PublicationCurated
    Sequence conflicti334 – 3341S → SS in CAA43550. 1 PublicationCurated
    Sequence conflicti344 – 3441S → T in CAA43550. 1 PublicationCurated
    Sequence conflicti367 – 3671S → N in CAA43550. 1 PublicationCurated
    Sequence conflicti388 – 3881I → N in CAA43550. 1 PublicationCurated
    Sequence conflicti425 – 4251A → D in CAA43550. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti244 – 2441S → P in hyperproinsulinemia obese fat/fat mice; reduced activity. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X61232 mRNA. Translation: CAA43550.1.
    U23184 mRNA. Translation: AAB60488.1.
    BC010197 mRNA. Translation: AAH10197.1.
    CCDSiCCDS22327.1.
    PIRiS16383.
    RefSeqiNP_038522.2. NM_013494.3.
    UniGeneiMm.31395.
    Mm.470333.

    Genome annotation databases

    EnsembliENSMUST00000048967; ENSMUSP00000048555; ENSMUSG00000037852.
    GeneIDi12876.
    KEGGimmu:12876.
    UCSCiuc009luw.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X61232 mRNA. Translation: CAA43550.1 .
    U23184 mRNA. Translation: AAB60488.1 .
    BC010197 mRNA. Translation: AAH10197.1 .
    CCDSi CCDS22327.1.
    PIRi S16383.
    RefSeqi NP_038522.2. NM_013494.3.
    UniGenei Mm.31395.
    Mm.470333.

    3D structure databases

    ProteinModelPortali Q00493.
    SMRi Q00493. Positions 49-450.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198855. 1 interaction.
    IntActi Q00493. 3 interactions.
    MINTi MINT-4090042.

    Protein family/group databases

    MEROPSi M14.005.

    PTM databases

    PhosphoSitei Q00493.

    Proteomic databases

    MaxQBi Q00493.
    PaxDbi Q00493.
    PRIDEi Q00493.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000048967 ; ENSMUSP00000048555 ; ENSMUSG00000037852 .
    GeneIDi 12876.
    KEGGi mmu:12876.
    UCSCi uc009luw.2. mouse.

    Organism-specific databases

    CTDi 1363.
    MGIi MGI:101932. Cpe.

    Phylogenomic databases

    eggNOGi NOG322453.
    HOGENOMi HOG000232185.
    HOVERGENi HBG003410.
    InParanoidi Q00493.
    KOi K01294.
    OMAi TIVNLIH.
    OrthoDBi EOG7B8S32.
    PhylomeDBi Q00493.
    TreeFami TF315592.

    Enzyme and pathway databases

    Reactomei REACT_207837. Insulin processing.

    Miscellaneous databases

    ChiTaRSi CPE. mouse.
    NextBioi 282472.
    PROi Q00493.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q00493.
    Bgeei Q00493.
    CleanExi MM_CPE.
    Genevestigatori Q00493.

    Family and domain databases

    Gene3Di 2.60.40.1120. 1 hit.
    InterProi IPR008969. CarboxyPept-like_regulatory.
    IPR014766. CarboxyPept_regulatory_dom.
    IPR000834. Peptidase_M14.
    [Graphical view ]
    Pfami PF00246. Peptidase_M14. 1 hit.
    [Graphical view ]
    PRINTSi PR00765. CRBOXYPTASEA.
    SMARTi SM00631. Zn_pept. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49464. SSF49464. 1 hit.
    PROSITEi PS00132. CARBOXYPEPT_ZN_1. 1 hit.
    PS00133. CARBOXYPEPT_ZN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Parkinson D.
      Submitted (AUG-1991) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Hyperproinsulinaemia in obese fat/fat mice associated with a carboxypeptidase E mutation which reduces enzyme activity."
      Naggert J.K., Fricker L.D., Varlamov O., Nishina P.M., Rouille Y., Steiner D.F., Carroll R.J., Paigen B.J., Leiter E.H.
      Nat. Genet. 10:135-142(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT PRO-244.
      Strain: HRS/J.
    3. "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].
      Strain: FVB/N.
      Tissue: Mammary gland.
    4. Lubec G., Kang S.U.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 43-55; 87-108; 363-374 AND 413-420, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain.

    Entry informationi

    Entry nameiCBPE_MOUSE
    AccessioniPrimary (citable) accession number: Q00493
    Secondary accession number(s): Q64439
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: July 15, 1998
    Last modified: October 1, 2014
    This is version 135 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3