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

 CBPE_BOVIN              Reviewed;         475 AA.
P04836; A5PJN4; Q52S88; Q6YI55;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
23-OCT-2007, sequence version 2.
22-NOV-2017, entry version 142.
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;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford; TISSUE=Uterus;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 42-475.
PubMed=3020433; DOI=10.1038/323461a0;
Fricker L.D., Evans C.J., Esch F.S., Herbert E.;
"Cloning and sequence analysis of cDNA for bovine carboxypeptidase
E.";
Nature 323:461-464(1986).
[3]
PROTEIN SEQUENCE OF 42-51.
PubMed=2396993; DOI=10.1042/bj2700057;
Christie D.L., Palmer D.J.;
"Identification and characterization of glycoproteins after extraction
of bovine chromaffin-granule membranes with lithium di-iodosalicylate.
Purification of glycoprotein II from the soluble fraction.";
Biochem. J. 270:57-61(1990).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 242-313, AND VARIANT HIS-255.
Haegeman A., Williams J.L., Law A., van Zeveren A., Peelman L.;
"Mapping and mutation analysis of bovine candidate genes for
meat/carcass traits.";
Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 242-313.
STRAIN=Korean;
Chung E.R., Shin S.C., Kim W.T.;
"Detection of single nucleotide polymorphisms of carboxypeptidase E
(CPE) gene in Korean cattle.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
-!- 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: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; BC142181; AAI42182.1; -; mRNA.
EMBL; X04411; CAA27999.1; -; mRNA.
EMBL; AH012367; AAO03557.1; -; Genomic_DNA.
EMBL; AH014826; AAX84651.1; -; Genomic_DNA.
PIR; A24327; A24327.
RefSeq; NP_776328.2; NM_173903.4.
UniGene; Bt.73670; -.
ProteinModelPortal; P04836; -.
SMR; P04836; -.
STRING; 9913.ENSBTAP00000021955; -.
MEROPS; M14.005; -.
PaxDb; P04836; -.
PRIDE; P04836; -.
Ensembl; ENSBTAT00000021955; ENSBTAP00000021955; ENSBTAG00000016514.
GeneID; 280753; -.
KEGG; bta:280753; -.
CTD; 1363; -.
eggNOG; KOG2649; Eukaryota.
eggNOG; ENOG410XX0H; LUCA.
GeneTree; ENSGT00760000119124; -.
HOGENOM; HOG000232185; -.
HOVERGEN; HBG003410; -.
InParanoid; P04836; -.
KO; K01294; -.
OMA; EELMDWW; -.
OrthoDB; EOG091G06A9; -.
TreeFam; TF315592; -.
Reactome; R-BTA-264876; Insulin processing.
Proteomes; UP000009136; Chromosome 17.
Bgee; ENSBTAG00000016514; -.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
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:0050839; F:cell adhesion molecule binding; IEA:Ensembl.
GO; GO:0004181; F:metallocarboxypeptidase activity; IBA:GO_Central.
GO; GO:0042043; F:neurexin family protein binding; IEA:Ensembl.
GO; GO:0004185; F:serine-type carboxypeptidase activity; IBA:GO_Central.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0003214; P:cardiac left ventricle morphogenesis; IEA:Ensembl.
GO; GO:0030070; P:insulin processing; IBA:GO_Central.
GO; GO:0072657; P:protein localization to membrane; IEA:Ensembl.
GO; GO:0016055; P:Wnt signaling pathway; IEA:Ensembl.
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.
1: Evidence at protein level;
Carboxypeptidase; Cleavage on pair of basic residues;
Complete proteome; Cytoplasmic vesicle; Direct protein sequencing;
Glycoprotein; Hydrolase; Membrane; Metal-binding; Metalloprotease;
Polymorphism; Protease; Reference proteome; Secreted; Signal; Zinc;
Zymogen.
SIGNAL 1 27 {ECO:0000255}.
PROPEP 28 41 Activation peptide.
{ECO:0000269|PubMed:2396993}.
/FTId=PRO_0000308381.
CHAIN 42 475 Carboxypeptidase E.
/FTId=PRO_0000212785.
ACT_SITE 341 341 Proton donor/acceptor.
{ECO:0000250|UniProtKB:P14384}.
METAL 113 113 Zinc; catalytic.
{ECO:0000250|UniProtKB:P00730}.
METAL 116 116 Zinc; catalytic.
{ECO:0000250|UniProtKB:P00730}.
METAL 247 247 Zinc; catalytic.
{ECO:0000250|UniProtKB:P00730}.
CARBOHYD 138 138 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 389 389 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 255 255 Y -> H. {ECO:0000269|Ref.4}.
CONFLICT 51 51 E -> G (in Ref. 3; AA sequence).
{ECO:0000305}.
SEQUENCE 475 AA; 53309 MW; 6516FE48E39321BF CRC64;
MARRGGCALL VLCGSLAACA WLLGAEARGP GGPVAGARRR RRPQEDGISF EYHRYPELRE
ALVSVWLQCA AVSRIYTVGR SFEGRELLVL ELSDNPGVHE PGEPEFKYIG NMHGNEAVGR
ELLIFLAQYL CNEYQKGNET IVQLIHNTRI HIMPSLNPDG FEKAASQLGE LKDWFVGRSN
AQGIDLNRNF PDLDRIVYIN EKEGGPNNHL LKNLKKIVDQ NTKLAPETKA VIHWIMDIPF
VLSANLHGGD LVANYPYDET RSGSAHEYSS CPDDDIFQSL ARAYSSFNPP MSDPDRPPCR
KNDDDSSFVE GTTNGAAWYS VPGGMQDFNY LSSNCFEITV ELSCEKFPPE ETLKNYWEDN
KNSLISYIQQ IHRGVKGFVR DLQGNPIANA TLSVEGIDHD VTSAKDGDYW RLLVPGNYKL
TASAPGYLAI AKKVAVPYSP AVRVDFELES FSERKEEEKE ELMEWWKMMS ETLNF


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