ID A0A3B4TLW1_SERDU Unreviewed; 432 AA.
AC A0A3B4TLW1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Carboxypeptidase A1 {ECO:0000313|Ensembl:ENSSDUP00000006982.1};
OS Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000006982.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000006982.1}
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 AlphaFoldDB; A0A3B4TLW1; -.
DR STRING; 41447.ENSSDUP00000006982; -.
DR Ensembl; ENSSDUT00000007113.1; ENSSDUP00000006982.1; ENSSDUG00000005129.1.
DR GeneTree; ENSGT00940000158082; -.
DR OMA; SHGISYE; -.
DR OrthoDB; 3540647at2759; -.
DR Proteomes; UP000261420; 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..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..432
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017233971"
FT DOMAIN 183..205
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00132"
FT DOMAIN 319..329
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00133"
FT REGION 272..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 432 AA; 48904 MW; 910B7183C9125F8A CRC64;
MGPAGLTLLV MMRGLLAFAA LFVAVLGKET FEGHQVLRIV PKDEVQLALI KDLEDIIEFE
LDFWRGVTEA ATPVDVRVPF HSLQSTKIYL ETQEIEYSIM IEDLQVMLDE EQEEMDSAAR
VAEPRNTDSF DFSRYHTINE IYSFQDMLVA ENPNMVSKIV IGRSYEGRPL NVLKFSTGGT
NRPAIWIDTG IHSREWVTQA SGTWFAKKIV TDYGRDPALT AILDQMDIFL EMVTNPDGYY
YTHNSNRMWR KTRKPNSGSN CVGVDPNRNW NAGFGGPGAS GQPCSETYRG PRAESESEVK
SIVDFVKSHG NFKAFISIHS YSQMLLYPYG YTRTPAKDQA ELHALAKKAI SDLASLYGTR
YRYGSIINTI YQASGGTIDW TYNQGIKYSY TFELRDTGRY GFILPANQII PTARETWLAL
MAIMDHTNRN PY
//
