ID   CBPZ_SIMVI              Reviewed;         304 AA.
AC   P42788;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Zinc carboxypeptidase;
DE            EC=3.4.17.-;
DE   Flags: Fragment;
OS   Simulium vittatum (Striped black fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Simuliidae;
OC   Simulium.
OX   NCBI_TaxID=7192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Gut;
RX   PubMed=8269093; DOI=10.1111/j.1365-2583.1993.tb00116.x;
RA   Ramos A., Mahowald A., Jacobs-Lorena M.;
RT   "Gut-specific genes from the black fly Simulium vittatum encoding trypsin-
RT   like and carboxypeptidase-like proteins.";
RL   Insect Mol. Biol. 1:149-163(1993).
CC   -!- FUNCTION: Involved in the digestion of the blood meal.
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: Secreted.
CC   -!- TISSUE SPECIFICITY: Gut specific.
CC   -!- INDUCTION: By blood meal.
CC   -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
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DR   EMBL; L08481; AAA18531.1; -; mRNA.
DR   AlphaFoldDB; P42788; -.
DR   SMR; P42788; -.
DR   MEROPS; M14.A08; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR000834; Peptidase_M14.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   PRINTS; PR00765; CRBOXYPTASEA.
DR   SMART; SM00631; Zn_pept; 1.
DR   PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR   PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
PE   2: Evidence at transcript level;
KW   Carboxypeptidase; Disulfide bond; Hydrolase; Metal-binding;
KW   Metalloprotease; Protease; Secreted; Zinc.
FT   CHAIN           <1..304
FT                   /note="Zinc carboxypeptidase"
FT                   /id="PRO_0000212787"
FT   ACT_SITE        259
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         58
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         61
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         184
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   DISULFID        125..148
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   304 AA;  34849 MW;  2E6E3FF8A6AA9144 CRC64;
     QYHTLPEIYS WLDRLVQEHP EHVEPVVGGK SYEGREIRGV KVSYKKGNPV VMVESNIHAR
     EWITAATTTY LLNELLTSKN STIREMAENY DWYIFPVTNP DGYVYTHTTD RMWRKTRSPN
     PDSLCAGTDP NRNWNFHWME QGTSSRPCTE TYGGKKAFSE VETRSFSDFL KTLKGQIKVY
     LAFHSYSQLL LFPYGHTCQH TYNHDDLQAI GDAAARSLAQ RYGTDYTVGN IYDAIYPASG
     GSMDWAYDTL DIPIAYTYEL RPRDGWNGFQ LPANQIIPTG EETVDSVVTI LKESRRLGYF
     NTSD