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Q00493 (CBPE_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

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

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

Cytoplasmic vesiclesecretory vesicle membrane; 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.

Involvement in disease

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.

Sequence similarities

Belongs to the peptidase M14 family.

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

Sequences

Sequence LengthMass (Da)Tools
Q00493 [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

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] [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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X61232 mRNA. Translation: CAA43550.1.
U23184 mRNA. Translation: AAB60488.1.
BC010197 mRNA. Translation: AAH10197.1.
PIRS16383.
RefSeqNP_038522.2. NM_013494.3.
UniGeneMm.31395.
Mm.470333.

3D structure databases

ProteinModelPortalQ00493.
SMRQ00493. Positions 49-450.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198855. 1 interaction.
IntActQ00493. 3 interactions.
MINTMINT-4090042.

Protein family/group databases

MEROPSM14.005.

PTM databases

PhosphoSiteQ00493.

Proteomic databases

PaxDbQ00493.
PRIDEQ00493.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000048967; ENSMUSP00000048555; ENSMUSG00000037852.
GeneID12876.
KEGGmmu:12876.
UCSCuc009luw.2. mouse.

Organism-specific databases

CTD1363.
MGIMGI:101932. Cpe.

Phylogenomic databases

eggNOGNOG322453.
HOGENOMHOG000232185.
HOVERGENHBG003410.
InParanoidQ00493.
KOK01294.
OMATIVNLIH.
OrthoDBEOG7B8S32.
PhylomeDBQ00493.
TreeFamTF315592.

Gene expression databases

ArrayExpressQ00493.
BgeeQ00493.
CleanExMM_CPE.
GenevestigatorQ00493.

Family and domain databases

Gene3D2.60.40.1120. 1 hit.
InterProIPR008969. CarboxyPept-like_regulatory.
IPR014766. CarboxyPept_regulatory_dom.
IPR000834. Peptidase_M14.
[Graphical view]
PfamPF00246. Peptidase_M14. 1 hit.
[Graphical view]
PRINTSPR00765. CRBOXYPTASEA.
SMARTSM00631. Zn_pept. 1 hit.
[Graphical view]
SUPFAMSSF49464. SSF49464. 1 hit.
PROSITEPS00132. CARBOXYPEPT_ZN_1. 1 hit.
PS00133. CARBOXYPEPT_ZN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCPE. mouse.
NextBio282472.
PROQ00493.
SOURCESearch...

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: April 16, 2014
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

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