CBPE_MACFA
ID CBPE_MACFA Reviewed; 476 AA.
AC Q4R4M3;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 71.
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; ORFNames=QflA-11442;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Frontal cortex;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-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; AB169871; BAE01952.1; -; mRNA.
DR RefSeq; NP_001272091.1; NM_001285162.1.
DR AlphaFoldDB; Q4R4M3; -.
DR SMR; Q4R4M3; -.
DR STRING; 9541.XP_005556300.1; -.
DR MEROPS; M14.005; -.
DR GeneID; 101926881; -.
DR CTD; 1363; -.
DR eggNOG; KOG2649; Eukaryota.
DR OrthoDB; 101221at2759; -.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Carboxypeptidase; Cleavage on pair of basic residues; Cytoplasmic vesicle;
KW Glycoprotein; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT PROPEP 26..42
FT /note="Activation peptide"
FT /id="PRO_0000280814"
FT CHAIN 43..476
FT /note="Carboxypeptidase E"
FT /id="PRO_0000280815"
FT ACT_SITE 342
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P14384"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 248
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 476 AA; 53300 MW; F289839539D49C62 CRC64;
MAGRGGRALL ALCGALAACG WLLGAEAQEP GAPAAGMRRR RRLQQEDGIS FEYHRYPELR
EALVSVWLQC TAISRIYTVG RSFEGRELLV IELSDNPGVH EPGEPEFKYI GNMHGNEAVG
RELLIFLAQY LRNEYQKGNE TIVNLIHSTR IHIMPSLNPD GFEKAASQPG ELKDWFVGRS
NAQGIDLNRN FPDLDRIVYV NEKEGGPNNH LLKNMKKIVD QNTKLAPETK AVIHWIMDIP
FVLSANLHGG DLVANYPYDE TRSGSAHEYS SSPDDAIFQS LARAYSSFNP AMSNPNRPPC
RKNDDDSSFV DGTTNGGAWY SVPGGMQDFN YLSSNCFEIT VELSCEKFPP EETLKTYWED
NKNSLISYLE QIHRGVKGFV RDLQGNPIAN ATISVEGIDH DVTSAKDGDY WRLLIPGNYK
LTASAPGYLA ITKKVAVPYS PAVGVDFELE SFSERKEEEK EELMEWWKMM SETLNF
