ID   A0A3Q4GF77_NEOBR        Unreviewed;       430 AA.
AC   A0A3Q4GF77;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Carboxypeptidase X (M14 family), member 1a {ECO:0000313|Ensembl:ENSNBRP00000007416.1};
GN   Name=CPXM1 {ECO:0000313|Ensembl:ENSNBRP00000007416.1};
OS   Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX   NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000007416.1, ECO:0000313|Proteomes:UP000261580};
RN   [1] {ECO:0000313|Ensembl:ENSNBRP00000007416.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase M14 family.
CC       {ECO:0000256|ARBA:ARBA00005988}.
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DR   AlphaFoldDB; A0A3Q4GF77; -.
DR   STRING; 32507.ENSNBRP00000007416; -.
DR   Ensembl; ENSNBRT00000007624.1; ENSNBRP00000007416.1; ENSNBRG00000005756.1.
DR   GeneTree; ENSGT00940000156141; -.
DR   OMA; DIFSEHE; -.
DR   Proteomes; UP000261580; Unplaced.
DR   Bgee; ENSNBRG00000005756; Expressed in zone of skin and 4 other cell types or tissues.
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:InterPro.
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; IPR000834; Peptidase_M14.
DR   PANTHER; PTHR11532:SF93; CARBOXYPEPTIDASE X1-RELATED; 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.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000261580}.
FT   DOMAIN          83..105
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|PROSITE:PS00132"
FT   DOMAIN          207..217
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|PROSITE:PS00133"
SQ   SEQUENCE   430 AA;  49875 MW;  575F6BBEB6AF91E8 CRC64;
     VTGNICYFLL DPSDIFSEHE SGSKDALDFR HHNYKEMRKL MKSVTEECPD ITRVYTIGRS
     YMGLKLYVME ISDNPGKHEI GEPEFRYVAG MHGNEALGRE LVLNLMQYMC KEYKKGNQRI
     VRLVTETRIH LLPSMNPDGY EGAYVKVDNP TTTLCLRTYI SYNCSSVKHN DFKHFKKSLD
     PLTLRRETRA VISWMQDIPF VLSANLHGGE LVVTYPFDCT RDWAPQEDTP TADNAFFRWL
     ASVYASTNLV MANPDRRICH YEDFQLHNNI INGGAWHTVP GSMNDFSYLH TNCFEVTVEL
     SCDKFPHVSE LPIEWENNKE SLLVYMEQVH RGIKGVVRDK LTKKGIADAI IKVEDHDHDI
     RSATDGDYWR LLNPGEYKVI VWAVGYFPSM RRCNVGMEPN PTICDFILTK TPIQRLKEIR
     NRFLNWFKYP
//