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

 CBPE_RAT                Reviewed;         476 AA.
P15087;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 1.
25-OCT-2017, entry version 131.
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;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
PubMed=2784437;
Rodriquez C., Brayton K.A., Brownstein M., Dixon J.E.;
"Rat preprocarboxypeptidase H. Cloning, characterization, and sequence
of the cDNA and regulation of the mRNA by corticotropin-releasing
factor.";
J. Biol. Chem. 264:5988-5995(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2725530; DOI=10.1210/mend-3-4-666;
Fricker L.D., Adelman J.P., Douglass J., Thompsom R.C.,
von Strandmann R.P., Hutton J.;
"Isolation and sequence analysis of cDNA for rat carboxypeptidase E
[EC 3.4.17.10], a neuropeptide processing enzyme.";
Mol. Endocrinol. 3:666-673(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Wistar; TISSUE=Brain;
PubMed=2334405; DOI=10.1042/bj2670517;
Manser E., Fernandez D., Loo L., Goh P.Y., Monfries C., Hall C.,
Lim L.;
"Human carboxypeptidase E. Isolation and characterization of the cDNA,
sequence conservation, expression and processing in vitro.";
Biochem. J. 267:517-525(1990).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1770952; DOI=10.1210/mend-5-9-1257;
Jung Y.K., Kunczt C.J., Pearson R.K., Dixon J.E., Fricker L.D.;
"Structural characterization of the rat carboxypeptidase-E gene.";
Mol. Endocrinol. 5:1257-1268(1991).
[5]
NUCLEOTIDE SEQUENCE OF 200-335.
PubMed=1955501; DOI=10.1210/jcem-73-6-1197;
Castano L., Russo E., Zhou L., Lipes M.A., Eisenbarth G.S.;
"Identification and cloning of a granule autoantigen
(carboxypeptidase-H) associated with type I diabetes.";
J. Clin. Endocrinol. Metab. 73:1197-1201(1991).
[6]
SUBCELLULAR LOCATION, AND LIPID RAFT-BINDING.
PubMed=14597614; DOI=10.1074/jbc.M310104200;
Hosaka M., Suda M., Sakai Y., Izumi T., Watanabe T., Takeuchi T.;
"Secretogranin III binds to cholesterol in the secretory granule
membrane as an adapter for chromogranin A.";
J. Biol. Chem. 279:3627-3634(2004).
-!- FUNCTION: Removes residual C-terminal Arg or Lys remaining after
initial endoprotease cleavage during prohormone processing.
-!- 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:0000269|PubMed:14597614}; Peripheral membrane
protein {ECO:0000269|PubMed:14597614}. Secreted
{ECO:0000269|PubMed:14597614}. Note=Associated with the secretory
granule membrane through direct binding to lipid rafts in
intragranular conditions. This binding is Ca(2+)-dependent.
{ECO:0000269|PubMed:14597614}.
-!- TISSUE SPECIFICITY: Expressed in brain, heart and anterior
pituitary gland. Also expressed in pancreatic islets and adrenal
gland. {ECO:0000269|PubMed:2784437}.
-!- MISCELLANEOUS: An autoantigen recognized by serum of pretype I
diabetes.
-!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; J04625; AAA40875.1; -; mRNA.
EMBL; M31602; AAA40873.1; -; mRNA.
EMBL; X51406; CAA35768.1; -; mRNA.
EMBL; L07281; AAA40957.1; ALT_SEQ; Genomic_DNA.
EMBL; L07273; AAA40957.1; JOINED; Genomic_DNA.
EMBL; L07274; AAA40957.1; JOINED; Genomic_DNA.
EMBL; L07275; AAA40957.1; JOINED; Genomic_DNA.
EMBL; L07277; AAA40957.1; JOINED; Genomic_DNA.
EMBL; L07278; AAA40957.1; JOINED; Genomic_DNA.
EMBL; L07279; AAA40957.1; JOINED; Genomic_DNA.
EMBL; L07280; AAA40957.1; JOINED; Genomic_DNA.
PIR; A40469; A40469.
PIR; S12461; S12461.
RefSeq; NP_037260.1; NM_013128.1.
UniGene; Rn.7149; -.
ProteinModelPortal; P15087; -.
SMR; P15087; -.
MEROPS; M14.005; -.
UniCarbKB; P15087; -.
PRIDE; P15087; -.
GeneID; 25669; -.
KEGG; rno:25669; -.
CTD; 1363; -.
RGD; 2394; Cpe.
HOVERGEN; HBG003410; -.
InParanoid; P15087; -.
KO; K01294; -.
PhylomeDB; P15087; -.
PRO; PR:P15087; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0030425; C:dendrite; IDA:BHF-UCL.
GO; GO:0031045; C:dense core granule; IDA:RGD.
GO; GO:0005576; C:extracellular region; IDA:RGD.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0005794; C:Golgi apparatus; IDA:BHF-UCL.
GO; GO:0045121; C:membrane raft; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0043204; C:perikaryon; IDA:BHF-UCL.
GO; GO:0030141; C:secretory granule; IDA:RGD.
GO; GO:0030667; C:secretory granule membrane; IDA:RGD.
GO; GO:0097060; C:synaptic membrane; IDA:RGD.
GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0004180; F:carboxypeptidase activity; IDA:RGD.
GO; GO:0050897; F:cobalt ion binding; IMP:RGD.
GO; GO:0004181; F:metallocarboxypeptidase activity; IBA:GO_Central.
GO; GO:0019904; F:protein domain specific binding; IDA:RGD.
GO; GO:0004185; F:serine-type carboxypeptidase activity; IBA:GO_Central.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0034230; P:enkephalin processing; IDA:RGD.
GO; GO:0030070; P:insulin processing; IDA:RGD.
GO; GO:2000173; P:negative regulation of branching morphogenesis of a nerve; IMP:RGD.
GO; GO:0043171; P:peptide catabolic process; IDA:RGD.
GO; GO:0016486; P:peptide hormone processing; TAS:RGD.
GO; GO:0006518; P:peptide metabolic process; IDA:RGD.
GO; GO:0016485; P:protein processing; IDA:RGD.
CDD; cd03865; M14_CPE; 1.
Gene3D; 2.60.40.1120; -; 1.
InterPro; IPR008969; CarboxyPept-like_regulatory.
InterPro; IPR034232; M14_CPE_CPD.
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.
1: Evidence at protein 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 27 Or 34.
PROPEP 28 42 Activation peptide.
/FTId=PRO_0000004388.
CHAIN 43 476 Carboxypeptidase E.
/FTId=PRO_0000004389.
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}.
CONFLICT 82 82 S -> T (in Ref. 2; AAA40873).
{ECO:0000305}.
CONFLICT 415 415 V -> A (in Ref. 3; CAA35768).
{ECO:0000305}.
CONFLICT 453 453 S -> Y (in Ref. 3; CAA35768).
{ECO:0000305}.
SEQUENCE 476 AA; 53309 MW; C2213D1FD6ECA120 CRC64;
MAGRGGRVLL ALCAALVAGG WLLAAEAQEP GAPAAGMRRR RRLQQEDGIS FEYHRYPELR
EALVSVWLQC TAISRIYTVG RSFEGRELLV IELSDNPGVH EPGEPEFKYI GNMHGNEAVG
RELLIFLAQY LCNEYQRGNE TIVNLIHSTR IHIMPSLNPD GFEKAASQPG ELKDWFVGRS
NAQGIDLNRN FPDLDRIVYV NEKEGGPNNH LLKNLKKIVD QNSKLAPETK AVIHWIMDIP
FVLSANLHGG DLVANYPYDE TRSGTAHEYS SCPDDAIFQS LARAYSSFNP VMSDPNRPPC
RKNDDDSSFV DGTTNGGAWY SVPGGMQDFN YLSSNCFEIT VELSCEKFPP EETLKSYWED
NKNSLINYLE QIHRGVKGFV RDLQGNPIAN ATISVDGIDH DVTSAKDGDY WRLLVPGNYK
LTASAPGYLA ITKKVAVPFS PAVGVDFELE SFSERKEEEK EELMEWWKMM SETLNF


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