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Reviewed, UniProtKB/Swiss-Prot Q00493 (CBPE_MOUSE)

Last modified June 16, 2009. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Carboxypeptidase E
      Short name=CPE
    EC=3.4.17.10
Alternative name(s):
    Carboxypeptidase H
      Short name=CPH
    Enkephalin convertase
    Prohormone-processing carboxypeptidase
Gene names
Name: Cpe
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length476 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subcellular location

Secreted. Note: Secretory granules of pancreatic islets, adrenal gland, pituitary and brain.

Involvement in disease

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

Sequence similarities

Belongs to the peptidase M14 family.

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Ontologies

Keywords
   Cellular componentSecreted
   DiseaseDisease mutation
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionCarboxypeptidase
Hydrolase
Metalloprotease
Protease
   PTMCleavage on pair of basic residues
Glycoprotein
Zymogen
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processinsulin processing Ref.2

Inferred from mutant phenotype. Source: MGI

proteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionmetallocarboxypeptidase activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 By similarity
Propeptide28 – 4215Activation peptide By similarity
PRO_0000004386
Chain43 – 476434Carboxypeptidase E
PRO_0000004387

Sites

Active site3421Nucleophile By similarity
Metal binding1141Zinc By similarity
Metal binding1171Zinc By similarity
Metal binding2481Zinc By similarity

Amino acid modifications

Glycosylation1391N-linked (GlcNAc...) Potential
Glycosylation3901N-linked (GlcNAc...) Potential

Natural variations

Natural variant2441S → P in hyperproinsulinemia obese fat/fat mice; reduced activity. Ref.2

Experimental info

Sequence conflict251A → R in CAA43550. Ref.1
Sequence conflict811R → A in CAA43550. Ref.1
Sequence conflict1671S → W in CAA43550. Ref.1
Sequence conflict1711E → Q in CAA43550. Ref.1
Sequence conflict3011R → C in CAA43550. Ref.1
Sequence conflict3101V → D in CAA43550. Ref.1
Sequence conflict3341S → SS in CAA43550. Ref.1
Sequence conflict3441S → T in CAA43550. Ref.1
Sequence conflict3671S → N in CAA43550. Ref.1
Sequence conflict3881I → N in CAA43550. Ref.1
Sequence conflict4251A → D in CAA43550. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
Q00493-1 [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: 82C5318A12A17567

FASTA47653,256
        10         20         30         40         50         60 
MAGRGGRVLL ALCAALVAGG WLLTAEAQEP GAPAAGMRRR RRLQQEDGIS FEYHRYPELR 

        70         80         90        100        110        120 
EALVSVWLQC TAISRIYTVG RSFEGRELLV IELSDNPGVH EPGEPEFKYI GNMHGNEAVG 

       130        140        150        160        170        180 
RELLIFLAQY LCNEYQKGNE TIVNLIHSTR IHIMPSLNPD GFEKAASQPG ELKDWFVGRS 

       190        200        210        220        230        240 
NAQGIDLNRN FPDLDRIVYV NEKEGGPNNH LLKNLKKIVD QNSKLAPETK AVIHWIMDIP 

       250        260        270        280        290        300 
FVLSANLHGG DLVANYPYDE TRSGTAHEYS SCPDDAIFQS LARAYSSFNP VMSDPNRPPC 

       310        320        330        340        350        360 
RKNDDDSSFV DGTTNGGAWY SVPGGMQDFN YLSSNCFEIT VELSCEKFPP EETLKSYWED 

       370        380        390        400        410        420 
NKNSLISYLE QIHRGVKGFV RDLQGNPIAN ATISVDGIDH DVTSAKDGDY WRLLAPGNYK 

       430        440        450        460        470 
LTASAPGYLA ITKKVAVPFS PAVGVDFELE SFSERKEEEK EELMEWWKMM SETLNF

« Hide

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References

« Hide 'large scale' references
[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: 7663508] [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: 15489334] [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, MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
+Additional computationally mapped references.

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Cross-references

Sequence databases

X61232 mRNA. Translation: CAA43550.1.
U23184 mRNA. Translation: AAB60488.1.
BC010197 mRNA. Translation: AAH10197.1.
IPIIPI00119152.
PIRS16383.
RefSeqNP_038522.2.
UniGeneMm.31395
Mm.470333

3D structure databases

HSSPHSSP built from PDB template 1H8L based on UniProtKB Q90240.
ModBaseSearch...

Protein family/group databases

MEROPSM14.005.

Proteomic databases

PRIDEQ00493.

Genome annotation databases

EnsemblENSMUSG00000037852. Mus musculus. [Contig view]
GeneID12876.
KEGGmmu:12876.

Organism-specific databases

MGIMGI:101932. Cpe.

Phylogenomic databases

HOGENOMQ00493.
HOVERGENQ00493.
OMAQ00493. QNTKLAP.

Enzyme and pathway databases

BRENDA3.4.17.10. 244.

Gene expression databases

ArrayExpressQ00493.
BgeeQ00493.
CleanExMM_CPE.
GermOnlineENSMUSG00000037852. Mus musculus.

Family and domain databases

InterProIPR014766. CarboxyPept_regulatory.
IPR000834. Peptidase_M14.
[Graphical view]
Gene3DG3DSA:2.60.40.1120. CarboxyPept_regulatory. 1 hit.
PfamPF00246. Peptidase_M14. 1 hit.
[Graphical view]
PRINTSPR00765. CRBOXYPTASEA.
SMARTSM00631. Zn_pept. 1 hit.
[Graphical view]
PROSITEPS00132. CARBOXYPEPT_ZN_1. 1 hit.
PS00133. CARBOXYPEPT_ZN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio282472.
SOURCESearch...

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Entry information

Entry nameCBPE_MOUSE
AccessionPrimary (citable) accession number: Q00493
Secondary accession number(s): Q64439
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: July 15, 1998
Last modified: June 16, 2009
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents