ID   CBPE_LOPAM              Reviewed;         454 AA.
AC   P37892;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 95.
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   Lophius americanus (American angler) (Anglerfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Lophiiformes; Lophiidae; Lophius.
OX   NCBI_TaxID=8073;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pancreatic islet;
RX   PubMed=1778303; DOI=10.1016/0303-7207(91)90120-h;
RA   Roth W.W., Mackin R.B., Spiess J., Goodman R.H., Noe B.D.;
RT   "Primary structure and tissue distribution of anglerfish carboxypeptidase
RT   H.";
RL   Mol. Cell. Endocrinol. 78:171-178(1991).
CC   -!- FUNCTION: Removes residual C-terminal Arg or Lys remaining after
CC       initial endoprotease cleavage during prohormone processing.
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   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane
CC       {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:P15087}.
CC   -!- TISSUE SPECIFICITY: Expressed in brain, pituitary and islet organs, but
CC       not in other tissues which do not secrete peptide hormones.
CC   -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U01909; AAC59636.1; -; mRNA.
DR   EMBL; S80565; AAA03252.1; -; mRNA.
DR   PIR; A54324; A54324.
DR   AlphaFoldDB; P37892; -.
DR   SMR; P37892; -.
DR   MEROPS; M14.005; -.
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; Cytoplasmic vesicle; Glycoprotein; Hydrolase; Membrane;
KW   Metal-binding; Metalloprotease; Protease; Secreted; Signal; Zinc.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..454
FT                   /note="Carboxypeptidase E"
FT                   /id="PRO_0000004390"
FT   ACT_SITE        320
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P14384"
FT   BINDING         92
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         95
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         226
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   CARBOHYD        117
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        368
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   454 AA;  51416 MW;  9796B86C74F25129 CRC64;
     MKQICSIVLL GAAVVSLVSA AGSDSEISFE YHRYEELRKA LVSVWLQCPT IARIYTIGES
     FEGRELLVLE MSDNPGTHEP GEPEFKYIAN MHGNEAVGRE LLIYLAQYLC NQYQQGNETI
     IDLIHSTRIH LMPSMNPDGF EKAASQPGEI KDWFVGRSNA QGVDLNRNFP DLDRIIYTNE
     REGGANNHLL QNMKKAVDEN TKLAPETKAV IHWIMEIPFV LSANLHGGDV VANYPYDETR
     TGSTHEYSAS PDDVIFKSLA KAFSIYNPVM SDPQRPPCRK HDDDSSFKDG ITNGGAWYSV
     PGGMQDFNYL SSNCFEITLE LSCDKFPNED TLKTYWEQNR NSLVNYIEQV HRGVKGYVRD
     LQGNPIFNAT ISVEGIDHDI TTAKDGDYWR LLRQGNYKVA ASAPGYLTVI KKVAVPHSPA
     TRVDFELESL MERKEEEREE LMDWWKMMSE TLNF