ID   CBPA1_DROPS             Reviewed;         425 AA.
AC   Q29NC4;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Zinc carboxypeptidase A 1;
DE            EC=3.4.17.-;
DE   Flags: Precursor;
GN   ORFNames=GA14587;
OS   Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=46245;
RN   [1] {ECO:0000312|EMBL:EAL33419.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MV2-25 / Tucson 14011-0121.94;
RX   PubMed=15632085; DOI=10.1101/gr.3059305;
RA   Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA   Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA   Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA   Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA   Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA   Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA   Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA   Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA   Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA   Weinstock G.M., Gibbs R.A.;
RT   "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT   gene, and cis-element evolution.";
RL   Genome Res. 15:1-18(2005).
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000255}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAL33419.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CH379060; EAL33419.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001356356.1; XM_001356320.3.
DR   AlphaFoldDB; Q29NC4; -.
DR   SMR; Q29NC4; -.
DR   STRING; 7237.FBpp0280257; -.
DR   MEROPS; M14.A08; -.
DR   EnsemblMetazoa; FBtr0281819; FBpp0280257; FBgn0074615.
DR   GeneID; 4817137; -.
DR   KEGG; dpo:Dpse_GA14587; -.
DR   eggNOG; KOG2650; Eukaryota.
DR   HOGENOM; CLU_019326_2_1_1; -.
DR   InParanoid; Q29NC4; -.
DR   OMA; MYKVNSE; -.
DR   PhylomeDB; Q29NC4; -.
DR   Proteomes; UP000001819; Chromosome 4.
DR   Bgee; FBgn0074615; Expressed in adult organism and 1 other tissue.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
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   Gene3D; 3.30.70.340; -; 1.
DR   InterPro; IPR036990; M14A-like_propep.
DR   InterPro; IPR003146; M14A_act_pep.
DR   InterPro; IPR000834; Peptidase_M14.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   Pfam; PF02244; Propep_M14; 1.
DR   PRINTS; PR00765; CRBOXYPTASEA.
DR   SMART; SM00631; Zn_pept; 1.
DR   PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase; Disulfide bond; Hydrolase; Metal-binding;
KW   Metalloprotease; Protease; Reference proteome; Secreted; Signal; Zinc.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..425
FT                   /note="Zinc carboxypeptidase A 1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000233308"
FT   ACT_SITE        381
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         182
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         185
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         306
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   DISULFID        247..270
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
SQ   SEQUENCE   425 AA;  46982 MW;  36E8DFE8A704FAB6 CRC64;
     MSLTKSLLLA LLAVVALAGV SAERARYDNY RLYKANAENA EQLAVLKQLE SSSDSILFLD
     GVHIVGADVK MVVAPHKVPD LLEILGKAEI KYLLQSSDVQ KTMDEIDEKV AMKGRAGEAY
     NWAQYYELDD TYAWLQTLAI ENPGVVTLIE GGKTYQGRSI LGVKITKSGK EKPGIFLEAG
     IHAREWIAPA AATYIINQLL TSEVEAVKQL AENYTWYVLP HANPDGYVYT HTTDRMWRKT
     RTPYQGCFGA DPNRNWAFHW NEVGASSNPC SDTYAGPSAF SEIETLSLSN YLASLKGKIQ
     LYISLHAYSQ YLLYPYGHTG DLPDNVADFR KVYDVSIAAV NKRYGTTYTG GNIYDAIYPA
     AGASVDWAYG TQDVRMAFCY ELRPSSNSFI TGFKLPAAQI VPASEELLDS IVAMAAEVNN
     LGYFN