CBPE_BOVIN
ID CBPE_BOVIN Reviewed; 475 AA.
AC P04836; A5PJN4; Q52S88; Q6YI55;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Carboxypeptidase E;
DE Short=CPE;
DE EC=3.4.17.10;
DE AltName: Full=Carboxypeptidase H;
DE Short=CPH;
DE AltName: Full=Enkephalin convertase;
DE AltName: Full=Prohormone-processing carboxypeptidase;
DE Flags: Precursor;
GN Name=CPE;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 42-475.
RX PubMed=3020433; DOI=10.1038/323461a0;
RA Fricker L.D., Evans C.J., Esch F.S., Herbert E.;
RT "Cloning and sequence analysis of cDNA for bovine carboxypeptidase E.";
RL Nature 323:461-464(1986).
RN [3]
RP PROTEIN SEQUENCE OF 42-51.
RX PubMed=2396993; DOI=10.1042/bj2700057;
RA Christie D.L., Palmer D.J.;
RT "Identification and characterization of glycoproteins after extraction of
RT bovine chromaffin-granule membranes with lithium di-iodosalicylate.
RT Purification of glycoprotein II from the soluble fraction.";
RL Biochem. J. 270:57-61(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 242-313, AND VARIANT HIS-255.
RA Haegeman A., Williams J.L., Law A., van Zeveren A., Peelman L.;
RT "Mapping and mutation analysis of bovine candidate genes for meat/carcass
RT traits.";
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 242-313.
RC STRAIN=Korean;
RA Chung E.R., Shin S.C., Kim W.T.;
RT "Detection of single nucleotide polymorphisms of carboxypeptidase E (CPE)
RT gene in Korean cattle.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Sorting receptor that directs prohormones to the regulated
CC secretory pathway. Acts also as a prohormone processing enzyme in
CC neuro/endocrine cells, removing dibasic residues from the C-terminal
CC end of peptide hormone precursors after initial endoprotease cleavage.
CC {ECO:0000250|UniProtKB:Q00493}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of C-terminal arginine or lysine residues from
CC polypeptides.; EC=3.4.17.10;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P00730};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P00730};
CC -!- SUBUNIT: Interacts with secretogranin III/SCG3.
CC {ECO:0000250|UniProtKB:Q00493}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle
CC {ECO:0000250|UniProtKB:Q00493}. Cytoplasmic vesicle, secretory vesicle
CC membrane {ECO:0000250|UniProtKB:P15087}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P15087}. Secreted
CC {ECO:0000250|UniProtKB:P15087}. Note=Associated with the secretory
CC granule membrane through direct binding to lipid rafts in intragranular
CC conditions. {ECO:0000250|UniProtKB:Q00493}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
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DR EMBL; BC142181; AAI42182.1; -; mRNA.
DR EMBL; X04411; CAA27999.1; -; mRNA.
DR EMBL; AH012367; AAO03557.1; -; Genomic_DNA.
DR EMBL; AH014826; AAX84651.1; -; Genomic_DNA.
DR PIR; A24327; A24327.
DR RefSeq; NP_776328.2; NM_173903.4.
DR AlphaFoldDB; P04836; -.
DR SMR; P04836; -.
DR STRING; 9913.ENSBTAP00000021955; -.
DR MEROPS; M14.005; -.
DR PaxDb; P04836; -.
DR Ensembl; ENSBTAT00000021955; ENSBTAP00000021955; ENSBTAG00000016514.
DR GeneID; 280753; -.
DR KEGG; bta:280753; -.
DR CTD; 1363; -.
DR VEuPathDB; HostDB:ENSBTAG00000016514; -.
DR VGNC; VGNC:27648; CPE.
DR eggNOG; KOG2649; Eukaryota.
DR GeneTree; ENSGT00940000157158; -.
DR HOGENOM; CLU_006722_1_3_1; -.
DR InParanoid; P04836; -.
DR OMA; WEQNRDS; -.
DR OrthoDB; 101221at2759; -.
DR TreeFam; TF315592; -.
DR Proteomes; UP000009136; Chromosome 17.
DR Bgee; ENSBTAG00000016514; Expressed in occipital lobe and 103 other tissues.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0030667; C:secretory granule membrane; IEA:Ensembl.
DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050839; F:cell adhesion molecule binding; IEA:Ensembl.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0042043; F:neurexin family protein binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0003214; P:cardiac left ventricle morphogenesis; IEA:Ensembl.
DR GO; GO:0030070; P:insulin processing; IEA:Ensembl.
DR GO; GO:0030072; P:peptide hormone secretion; IEA:Ensembl.
DR GO; GO:0006518; P:peptide metabolic process; IBA:GO_Central.
DR GO; GO:0072657; P:protein localization to membrane; IEA:Ensembl.
DR GO; GO:0033366; P:protein localization to secretory granule; IEA:Ensembl.
DR GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:Ensembl.
DR CDD; cd03865; M14_CPE; 1.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR034232; M14_CPE_CPD.
DR InterPro; IPR000834; Peptidase_M14.
DR Pfam; PF00246; Peptidase_M14; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF49464; SSF49464; 1.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
PE 1: Evidence at protein level;
KW Carboxypeptidase; Cleavage on pair of basic residues; Cytoplasmic vesicle;
KW Direct protein sequencing; Glycoprotein; Hydrolase; Membrane;
KW Metal-binding; Metalloprotease; Protease; Reference proteome; Secreted;
KW Signal; Zinc; Zymogen.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT PROPEP 28..41
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:2396993"
FT /id="PRO_0000308381"
FT CHAIN 42..475
FT /note="Carboxypeptidase E"
FT /id="PRO_0000212785"
FT ACT_SITE 341
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P14384"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 255
FT /note="Y -> H"
FT /evidence="ECO:0000269|Ref.4"
FT CONFLICT 51
FT /note="E -> G (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ 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
