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Protein

Carboxypeptidase E

Gene

Cpe

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi114 – 1141Zinc; catalyticBy similarity
Metal bindingi117 – 1171Zinc; catalyticBy similarity
Metal bindingi248 – 2481Zinc; catalyticBy similarity
Active sitei342 – 3421Proton donor/acceptorBy similarity

GO - Molecular functioni

  • carboxypeptidase activity Source: RGD
  • cobalt ion binding Source: RGD
  • metallocarboxypeptidase activity Source: InterPro
  • protein domain specific binding Source: RGD
  • zinc ion binding Source: InterPro

GO - Biological processi

  • enkephalin processing Source: RGD
  • insulin processing Source: RGD
  • negative regulation of branching morphogenesis of a nerve Source: RGD
  • peptide catabolic process Source: RGD
  • peptide hormone processing Source: RGD
  • peptide metabolic process Source: RGD
  • protein processing Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2394. Cpe.

Subcellular locationi

GO - Cellular componenti

  • dendrite Source: BHF-UCL
  • dense core granule Source: RGD
  • extracellular region Source: RGD
  • extracellular space Source: RGD
  • Golgi apparatus Source: BHF-UCL
  • membrane raft Source: RGD
  • neuronal cell body Source: RGD
  • perikaryon Source: BHF-UCL
  • secretory granule Source: RGD
  • secretory granule membrane Source: RGD
  • synaptic membrane Source: RGD
  • transport vesicle membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727Or 34Add
BLAST
Propeptidei28 – 4215Activation peptidePRO_0000004388Add
BLAST
Chaini43 – 476434Carboxypeptidase EPRO_0000004389Add
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

PRIDEiP15087.

PTM databases

UniCarbKBiP15087.

Expressioni

Tissue specificityi

Expressed in brain, heart and anterior pituitary gland. Also expressed in pancreatic islets and adrenal gland.1 Publication

Interactioni

GO - Molecular functioni

  • protein domain specific binding Source: RGD

Structurei

3D structure databases

ProteinModelPortaliP15087.
SMRiP15087. Positions 49-451.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M14 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG003410.
InParanoidiP15087.
KOiK01294.
PhylomeDBiP15087.

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.

P15087-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGRGGRVLL ALCAALVAGG WLLAAEAQEP GAPAAGMRRR RRLQQEDGIS
60 70 80 90 100
FEYHRYPELR EALVSVWLQC TAISRIYTVG RSFEGRELLV IELSDNPGVH
110 120 130 140 150
EPGEPEFKYI GNMHGNEAVG RELLIFLAQY LCNEYQRGNE TIVNLIHSTR
160 170 180 190 200
IHIMPSLNPD GFEKAASQPG ELKDWFVGRS NAQGIDLNRN FPDLDRIVYV
210 220 230 240 250
NEKEGGPNNH LLKNLKKIVD QNSKLAPETK AVIHWIMDIP FVLSANLHGG
260 270 280 290 300
DLVANYPYDE TRSGTAHEYS SCPDDAIFQS LARAYSSFNP VMSDPNRPPC
310 320 330 340 350
RKNDDDSSFV DGTTNGGAWY SVPGGMQDFN YLSSNCFEIT VELSCEKFPP
360 370 380 390 400
EETLKSYWED NKNSLINYLE QIHRGVKGFV RDLQGNPIAN ATISVDGIDH
410 420 430 440 450
DVTSAKDGDY WRLLVPGNYK LTASAPGYLA ITKKVAVPFS PAVGVDFELE
460 470
SFSERKEEEK EELMEWWKMM SETLNF
Length:476
Mass (Da):53,309
Last modified:April 1, 1990 - v1
Checksum:iC2213D1FD6ECA120
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti82 – 821S → T in AAA40873 (PubMed:2725530).Curated
Sequence conflicti415 – 4151V → A in CAA35768 (PubMed:2334405).Curated
Sequence conflicti453 – 4531S → Y in CAA35768 (PubMed:2334405).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04625 mRNA. Translation: AAA40875.1.
M31602 mRNA. Translation: AAA40873.1.
X51406 mRNA. Translation: CAA35768.1.
L07281
, L07273, L07274, L07275, L07277, L07278, L07279, L07280 Genomic DNA. Translation: AAA40957.1. Sequence problems.
PIRiA40469.
S12461.
RefSeqiNP_037260.1. NM_013128.1.
UniGeneiRn.7149.

Genome annotation databases

GeneIDi25669.
KEGGirno:25669.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04625 mRNA. Translation: AAA40875.1.
M31602 mRNA. Translation: AAA40873.1.
X51406 mRNA. Translation: CAA35768.1.
L07281
, L07273, L07274, L07275, L07277, L07278, L07279, L07280 Genomic DNA. Translation: AAA40957.1. Sequence problems.
PIRiA40469.
S12461.
RefSeqiNP_037260.1. NM_013128.1.
UniGeneiRn.7149.

3D structure databases

ProteinModelPortaliP15087.
SMRiP15087. Positions 49-451.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM14.005.

PTM databases

UniCarbKBiP15087.

Proteomic databases

PRIDEiP15087.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25669.
KEGGirno:25669.

Organism-specific databases

CTDi1363.
RGDi2394. Cpe.

Phylogenomic databases

HOVERGENiHBG003410.
InParanoidiP15087.
KOiK01294.
PhylomeDBiP15087.

Miscellaneous databases

PROiP15087.

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]
ProtoNetiSearch...

Publicationsi

  1. "Rat preprocarboxypeptidase H. Cloning, characterization, and sequence of the cDNA and regulation of the mRNA by corticotropin-releasing factor."
    Rodriquez C., Brayton K.A., Brownstein M., Dixon J.E.
    J. Biol. Chem. 264:5988-5995(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  2. "Isolation and sequence analysis of cDNA for rat carboxypeptidase E [EC 3.4.17.10], a neuropeptide processing enzyme."
    Fricker L.D., Adelman J.P., Douglass J., Thompsom R.C., von Strandmann R.P., Hutton J.
    Mol. Endocrinol. 3:666-673(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Human carboxypeptidase E. Isolation and characterization of the cDNA, sequence conservation, expression and processing in vitro."
    Manser E., Fernandez D., Loo L., Goh P.Y., Monfries C., Hall C., Lim L.
    Biochem. J. 267:517-525(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Wistar.
    Tissue: Brain.
  4. "Structural characterization of the rat carboxypeptidase-E gene."
    Jung Y.K., Kunczt C.J., Pearson R.K., Dixon J.E., Fricker L.D.
    Mol. Endocrinol. 5:1257-1268(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "Identification and cloning of a granule autoantigen (carboxypeptidase-H) associated with type I diabetes."
    Castano L., Russo E., Zhou L., Lipes M.A., Eisenbarth G.S.
    J. Clin. Endocrinol. Metab. 73:1197-1201(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 200-335.
  6. "Secretogranin III binds to cholesterol in the secretory granule membrane as an adapter for chromogranin A."
    Hosaka M., Suda M., Sakai Y., Izumi T., Watanabe T., Takeuchi T.
    J. Biol. Chem. 279:3627-3634(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, LIPID RAFT-BINDING.

Entry informationi

Entry nameiCBPE_RAT
AccessioniPrimary (citable) accession number: P15087
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: June 8, 2016
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

An autoantigen recognized by serum of pretype I diabetes.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.