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Carboxypeptidase E (CPE) (EC 3.4.17.10) (Carboxypeptidase H) (CPH) (Enkephalin convertase) (Prohormone-processing carboxypeptidase)

 CBPE_PANTR              Reviewed;         476 AA.
A5A6K7;
21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
12-JUN-2007, sequence version 1.
22-NOV-2017, entry version 69.
RecName: Full=Carboxypeptidase E;
Short=CPE;
EC=3.4.17.10;
AltName: Full=Carboxypeptidase H;
Short=CPH;
AltName: Full=Enkephalin convertase;
AltName: Full=Prohormone-processing carboxypeptidase;
Flags: Precursor;
Name=CPE;
Pan troglodytes (Chimpanzee).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Pan.
NCBI_TaxID=9598;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=17574350; DOI=10.1016/j.gene.2007.04.013;
Sakate R., Suto Y., Imanishi T., Tanoue T., Hida M., Hayasaka I.,
Kusuda J., Gojobori T., Hashimoto K., Hirai M.;
"Mapping of chimpanzee full-length cDNAs onto the human genome unveils
large potential divergence of the transcriptome.";
Gene 399:1-10(2007).
-!- FUNCTION: Removes residual C-terminal Arg or Lys remaining after
initial endoprotease cleavage during prohormone processing.
Processes proinsulin (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Release of C-terminal arginine or lysine
residues from polypeptides.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000250|UniProtKB:P00730};
Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P00730};
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle
membrane {ECO:0000250|UniProtKB:P15087}; Peripheral membrane
protein {ECO:0000250|UniProtKB:P15087}. Secreted
{ECO:0000250|UniProtKB:P15087}. Note=Associated with the secretory
granule membrane through direct binding to lipid rafts in
intragranular conditions. {ECO:0000250|UniProtKB:P15087}.
-!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
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EMBL; AB222135; BAF62380.1; -; mRNA.
RefSeq; NP_001092029.1; NM_001098559.1.
UniGene; Ptr.88; -.
ProteinModelPortal; A5A6K7; -.
SMR; A5A6K7; -.
STRING; 9598.ENSPTRP00000038931; -.
MEROPS; M14.005; -.
PaxDb; A5A6K7; -.
GeneID; 461592; -.
KEGG; ptr:461592; -.
CTD; 1363; -.
eggNOG; KOG2649; Eukaryota.
eggNOG; ENOG410XX0H; LUCA.
HOGENOM; HOG000232185; -.
HOVERGEN; HBG003410; -.
InParanoid; A5A6K7; -.
KO; K01294; -.
Proteomes; UP000002277; Unplaced.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
GO; GO:0030141; C:secretory granule; IBA:GO_Central.
GO; GO:0097060; C:synaptic membrane; IBA:GO_Central.
GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0004181; F:metallocarboxypeptidase activity; IBA:GO_Central.
GO; GO:0004185; F:serine-type carboxypeptidase activity; IBA:GO_Central.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0030070; P:insulin processing; IBA:GO_Central.
InterPro; IPR008969; CarboxyPept-like_regulatory.
InterPro; IPR000834; Peptidase_M14.
Pfam; PF00246; Peptidase_M14; 1.
PRINTS; PR00765; CRBOXYPTASEA.
SMART; SM00631; Zn_pept; 1.
SUPFAM; SSF49464; SSF49464; 1.
PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
2: Evidence at transcript level;
Carboxypeptidase; Cleavage on pair of basic residues;
Complete proteome; Cytoplasmic vesicle; Glycoprotein; Hydrolase;
Membrane; Metal-binding; Metalloprotease; Protease;
Reference proteome; Secreted; Signal; Zinc; Zymogen.
SIGNAL 1 25 {ECO:0000255}.
PROPEP 26 42 Activation peptide.
/FTId=PRO_0000297554.
CHAIN 43 476 Carboxypeptidase E.
/FTId=PRO_0000297555.
ACT_SITE 342 342 Proton donor/acceptor.
{ECO:0000250|UniProtKB:P14384}.
METAL 114 114 Zinc; catalytic.
{ECO:0000250|UniProtKB:P00730}.
METAL 117 117 Zinc; catalytic.
{ECO:0000250|UniProtKB:P00730}.
METAL 248 248 Zinc; catalytic.
{ECO:0000250|UniProtKB:P00730}.
CARBOHYD 139 139 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 390 390 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
SEQUENCE 476 AA; 53046 MW; 50611CA3F9CDE345 CRC64;
MAGRGGSALL ALCGALAACG WLLGAEAQEP GAPAAGMRRR RRLQQEDGIS FEYHRYPELR
EALVSVWLQC TAISRIYTVG RSFEGRELLV IELSDNPGVH EPGEPEFKYI GNMHGNEAVG
RELLIFLAQY LCNEYQKGNE TIVNLIHSTR IHIMPSLNPD GFEKAASQPG ELKDWFVGRS
NAQGIDLNRN FPDLDRIVYV NEKEGGPNNH LLKNMKKIVD QNTKLAPETK AVIHWIMDIP
FVLSANLHGG DLVANYPYDE TRSGSAHEYS SSPDDAIFQS LARAYSSFNP AMSDPNRPPC
HKNDDDSSFV DGTTNGGAWY SVPGGMQDFN YLSSNCFEIT VELSCEKFPP EETLKTYWED
NKNSLISYLE QIHRGVKGFV RDLQGNPIAN ATISVEGIDH DVTSAKDGDY WRLLIPGNYK
LTASAPGYLA VTKKVAVPYS PAAGVDFELE SFSGRKEEEK EELMEWWKMM SETLNF


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