ID   A0A3B3RFW4_9TELE        Unreviewed;       752 AA.
AC   A0A3B3RFW4;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Inactive carboxypeptidase-like protein X2 {ECO:0000313|Ensembl:ENSPKIP00000017228.1};
GN   Name=CPXM2 {ECO:0000313|Ensembl:ENSPKIP00000017228.1};
OS   Paramormyrops kingsleyae.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC   Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX   NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000017228.1, ECO:0000313|Proteomes:UP000261540};
RN   [1] {ECO:0000313|Ensembl:ENSPKIP00000017228.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the peptidase M14 family.
CC       {ECO:0000256|ARBA:ARBA00005988}.
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DR   AlphaFoldDB; A0A3B3RFW4; -.
DR   STRING; 1676925.ENSPKIP00000017228; -.
DR   Ensembl; ENSPKIT00000041737.1; ENSPKIP00000017228.1; ENSPKIG00000003218.1.
DR   GeneTree; ENSGT00940000156414; -.
DR   OrthoDB; 5490979at2759; -.
DR   Proteomes; UP000261540; 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:InterPro.
DR   GO; GO:0032101; P:regulation of response to external stimulus; IEA:UniProt.
DR   CDD; cd00057; FA58C; 1.
DR   CDD; cd03869; M14_CPX_like; 1.
DR   CDD; cd11308; Peptidase_M14NE-CP-C_like; 1.
DR   Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR008969; CarboxyPept-like_regulatory.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR000834; Peptidase_M14.
DR   PANTHER; PTHR11532:SF45; INACTIVE CARBOXYPEPTIDASE-LIKE PROTEIN X2; 1.
DR   PANTHER; PTHR11532; PROTEASE M14 CARBOXYPEPTIDASE; 1.
DR   Pfam; PF13620; CarboxypepD_reg; 1.
DR   Pfam; PF00754; F5_F8_type_C; 1.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   PRINTS; PR00765; CRBOXYPTASEA.
DR   SMART; SM00231; FA58C; 1.
DR   SMART; SM00631; Zn_pept; 1.
DR   SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR   PROSITE; PS01286; FA58C_2; 1.
DR   PROSITE; PS50022; FA58C_3; 1.
PE   3: Inferred from homology;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           33..752
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017451258"
FT   DOMAIN          128..287
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   REGION          76..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          729..752
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        76..94
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        102..126
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   752 AA;  85723 MW;  AD85A0FE6A16E52A CRC64;
     MTPLGEKGSP CAFLAFSLLV LLVLLVVDGA HGRPFEDEDY YMQELLSREH YYHAPEEPVS
     PPEASDWGAD DRVNLRAAKK EPKIREKENR PDKAAAGKNG NNKVEKNKKG GMKNSINEGE
     SHFKPVKEEC PPMGLETLKI DDFQLHASTM RRYSLGPHRG RLNIQAGIYE DEFYEGGWCA
     GRNDPMQWFE VDARRLTKFT GVITQGRSSL WSSDWVTSYR VLVSNDSHTW VTLKNGSQDL
     IFTGNREKEI PVLSEFPAPV MARYIRVNPR SWFSGGSVCM RVEILGCPMP DPNNYYRRRN
     EITTTDNLDF KHHSYKEMRQ LMKIVNEMCP NITRIYNIGK SFDGLKLYAI EISDNPGEHE
     LGEPEFRYTA GSHGNEVLGR ELLLLLMQFM CQEYLAGNPR IRHLVEETRI HLLPSVNPDG
     YEKAFEVGSE LGGWSLGRWS EDGLDIHHNF PDLNSILWEA EARKLTSRRV LNHHIPIPDW
     YLAKNATVAV ETRALIAWME KIPFVLGGNL QGGELVVSYP YDRTRFRSKT REATPTPDDL
     VFRWLAFSYA STHRLMTDAS RRVCHTVDFA KEDGTVNGAS WHTAAGSMND FSYLHTNCFE
     MSMFVGCDKF PHKSELPDEW ENNRESLLVF MEQVHRGIKG VVRDTQGRGV ANAIVSVEGI
     NHDVRTVADG DYWRLLNPGE YKVIVRADGY TSTSKVCEVG YEIGATRCDF VITRTNLSRI
     KEIMDKFSKQ HGDSPLPVRR PPQPRPQRRR GA
//