CBPE_PANTR
ID CBPE_PANTR Reviewed; 476 AA.
AC A5A6K7;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
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 Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=17574350; DOI=10.1016/j.gene.2007.04.013;
RA Sakate R., Suto Y., Imanishi T., Tanoue T., Hida M., Hayasaka I.,
RA Kusuda J., Gojobori T., Hashimoto K., Hirai M.;
RT "Mapping of chimpanzee full-length cDNAs onto the human genome unveils
RT large potential divergence of the transcriptome.";
RL Gene 399:1-10(2007).
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; AB222135; BAF62380.1; -; mRNA.
DR RefSeq; NP_001092029.1; NM_001098559.1.
DR AlphaFoldDB; A5A6K7; -.
DR SMR; A5A6K7; -.
DR STRING; 9598.ENSPTRP00000038931; -.
DR MEROPS; M14.005; -.
DR PaxDb; A5A6K7; -.
DR GeneID; 461592; -.
DR KEGG; ptr:461592; -.
DR CTD; 1363; -.
DR eggNOG; KOG2649; Eukaryota.
DR InParanoid; A5A6K7; -.
DR OrthoDB; 101221at2759; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006518; P:peptide metabolic process; IBA:GO_Central.
DR GO; GO:0016485; P:protein processing; IBA:GO_Central.
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_0000297554"
FT CHAIN 43..476
FT /note="Carboxypeptidase E"
FT /id="PRO_0000297555"
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; 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
