ID A0A1V4IX61_PATFA Unreviewed; 470 AA.
AC A0A1V4IX61;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Carboxypeptidase E {ECO:0000256|ARBA:ARBA00024081};
DE EC=3.4.17.10 {ECO:0000256|ARBA:ARBA00024064};
DE AltName: Full=Carboxypeptidase H {ECO:0000256|ARBA:ARBA00031341};
DE AltName: Full=Enkephalin convertase {ECO:0000256|ARBA:ARBA00032488};
DE AltName: Full=Prohormone-processing carboxypeptidase {ECO:0000256|ARBA:ARBA00031745};
GN Name=CPE {ECO:0000313|EMBL:OPJ64344.1};
GN ORFNames=AV530_009159 {ECO:0000313|EMBL:OPJ64344.1};
OS Patagioenas fasciata monilis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ64344.1, ECO:0000313|Proteomes:UP000190648};
RN [1] {ECO:0000313|EMBL:OPJ64344.1, ECO:0000313|Proteomes:UP000190648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ64344.1};
RC TISSUE=Blood {ECO:0000313|EMBL:OPJ64344.1};
RA Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA Shapiro B.;
RT "Band-tailed pigeon sequencing and assembly.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of C-terminal arginine or lysine residues from
CC polypeptides.; EC=3.4.17.10;
CC Evidence={ECO:0000256|ARBA:ARBA00023961};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane
CC {ECO:0000256|ARBA:ARBA00004268}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004268}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family.
CC {ECO:0000256|ARBA:ARBA00005988}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OPJ64344.1}.
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DR EMBL; LSYS01009665; OPJ64344.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4IX61; -.
DR STRING; 372326.A0A1V4IX61; -.
DR Proteomes; UP000190648; Unassembled WGS sequence.
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:InterPro.
DR CDD; cd03865; M14_CPE; 1.
DR CDD; cd11308; Peptidase_M14NE-CP-C_like; 1.
DR Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR034232; M14_CPE_CPD.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR11532:SF92; CARBOXYPEPTIDASE E; 1.
DR PANTHER; PTHR11532; PROTEASE M14 CARBOXYPEPTIDASE; 1.
DR Pfam; PF13620; CarboxypepD_reg; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW ECO:0000313|EMBL:OPJ64344.1};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000190648};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..470
FT /note="Carboxypeptidase E"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012121382"
FT DOMAIN 99..121
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00132"
FT DOMAIN 242..252
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00133"
SQ SEQUENCE 470 AA; 52375 MW; 664564595C470C20 CRC64;
MALRLLLVLC GLLAACQAAE PAAGPGLGGA ASRRRRLSAE EGISFEYHRY AELREALVAV
WLQCPAISRI YTVGRSAEGR ELLVIEVSDR PGEHEPGEPE FKYVGNMHGN EAVGRELLIF
LAQYLCNEYQ KGNETIINLI HSTRIHIMPS LNPDGFEKAA SQPGELKDWF VGRSNAQGID
LNRNFPDLDR IVYVNEKEGG PNNHLLKNMK KAVDQNPKLA PETKGVIHWI MDIPFVLSAN
LHGGDLVANY PYDETRSGST HEYSSCPDDA IFQSLARSYS SFNPAMSDPN RPPCRKNDDD
SSFVDGTTNG GAWYSVPGGM QDFNYLSSNC FEITVELSCE KFPPEETLKG YWEDNKNSLI
NYIEQIHRGV KGFVKDLQGN PIANATISVE GISHDITSAK DGDYWRLLVP GNYKLTASAP
GYLAITKKVA VPFSPAVVID FELESLSERK EEEKEELMEW WKMMSETLNF
//
