ID A0A3B3VE09_9TELE Unreviewed; 415 AA.
AC A0A3B3VE09;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Carboxypeptidase A1-like {ECO:0000313|Ensembl:ENSPLAP00000023995.1};
GN Name=CPA1 {ECO:0000313|Ensembl:ENSPLAP00000023995.1};
OS Poecilia latipinna (sailfin molly).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000023995.1, ECO:0000313|Proteomes:UP000261500};
RN [1] {ECO:0000313|Ensembl:ENSPLAP00000023995.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M14 family.
CC {ECO:0000256|ARBA:ARBA00005988}.
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DR RefSeq; XP_014915538.1; XM_015060052.1.
DR AlphaFoldDB; A0A3B3VE09; -.
DR Ensembl; ENSPLAT00000004503.1; ENSPLAP00000023995.1; ENSPLAG00000010123.1.
DR GeneID; 106964494; -.
DR GeneTree; ENSGT00940000158082; -.
DR OrthoDB; 3540647at2759; -.
DR Proteomes; UP000261500; Unplaced.
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; Metallocarboxypeptidase-like; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 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 PANTHER; PTHR11705:SF91; CARBOXYPEPTIDASE A1 (PANCREATIC)-RELATED; 1.
DR PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR Pfam; PF02244; Propep_M14; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 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 Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..415
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017429439"
FT DOMAIN 166..188
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00132"
FT DOMAIN 302..312
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00133"
SQ SEQUENCE 415 AA; 47229 MW; F8570E432236081E CRC64;
MMKKLVAFAA LLVAVLSKED FRGHQVFRIV PKDDVQLALV RVMEDILDLE LDFWSWVTPV
DVRVPSHSLQ VVKSYMERHS IKYFTMIKDL QALLDEERRQ MKSAAPAGNT DSFDYTNYHT
LSQIYSFQDM LVVENPKLVS KTVIGHSVEG RPLNVLKFST GGSNRPAIWI DTGIHAREWV
TQASGIVFAK KILTEYGTDS VLTEILNRMD IFLEMVVNPD GYHFTHTNNR MWRKNRKQNE
DSSCVGVDLN RNWNAGFGGR GSSNNPCTET YHGTRAHSEP EVKSIVKFVR SHGNIKAFIS
IHSYSQMLLY PYGYTRNPAK DQAELDQVAQ KAVTALASLY GTNYRYGSII KTIYQSSGGS
IDWTYKKGIK YSYTFELRDT GHFGFILPAN QIVPTANETW LALKVIMDHT LKNPY
//
