ID   CBPA5_MACFA             Reviewed;         436 AA.
AC   Q4R7R2;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Carboxypeptidase A5;
DE            EC=3.4.17.-;
DE   Flags: Precursor;
GN   Name=CPA5; ORFNames=QtsA-14584;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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:0000305}.
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DR   EMBL; AB168753; BAE00860.1; -; mRNA.
DR   RefSeq; NP_001272224.1; NM_001285295.1.
DR   AlphaFoldDB; Q4R7R2; -.
DR   SMR; Q4R7R2; -.
DR   STRING; 9541.XP_005550824.1; -.
DR   MEROPS; M14.020; -.
DR   GeneID; 101865458; -.
DR   CTD; 93979; -.
DR   eggNOG; KOG2650; Eukaryota.
DR   OrthoDB; 524270at2759; -.
DR   Proteomes; UP000233100; Unplaced.
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   CDD; cd03870; M14_CPA; 1.
DR   Gene3D; 3.30.70.340; -; 1.
DR   InterPro; IPR034248; CPA_M14_CPD.
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.
DR   PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
PE   2: Evidence at transcript level;
KW   Carboxypeptidase; Cleavage on pair of basic residues; Disulfide bond;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW   Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000255"
FT   PROPEP          34..126
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000280811"
FT   CHAIN           127..436
FT                   /note="Carboxypeptidase A5"
FT                   /id="PRO_0000280812"
FT   ACT_SITE        397
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P00732"
FT   BINDING         196..199
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         196
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         199
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         254
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         271..272
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         323
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         324..325
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         375
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   DISULFID        265..288
FT                   /evidence="ECO:0000250|UniProtKB:Q96IY4"
SQ   SEQUENCE   436 AA;  49044 MW;  D2A45E7C737F189B CRC64;
     MQGTPAGGTS PGPSPMDRQT LLVFSLILAA ALGQMNFTGD QVLRVLAKDE KQLSLLRDLE
     GLKPQKVDFW RGPARPSLPV DMRVPFSELK YIKAYLESHG LAYSIMIKDI QVLLDEEREA
     MAKSRRLERS TSSFSYSSYH TLEEISSWID NFVTEHSDIV SKIQIGNSFE NRSILVLKFS
     TGGSRHPAIW IDTGIHSREW ITHATGIWTA NKIVSDYGKD RVLTDILKAM DIFIELVTNP
     DGFAFTHSMN RLWRKNKSIR PGIFCIGVDL NRNWKSGFGG NGSNSNPCSE TYHGPSPQSE
     PEVAAIVNFI TAHGNFKALI SIHSYSQMLM YPYGRSLEPV SNQRELYDLA KDAVEALYKV
     HGIEYFFGSI STTLYVASGI TVDWAYDSGI KYAFSFELRD TGRYGFLLPA TQIIPTAQET
     WMALRTIMEH TLNHPY