ID A0A3Q3AF34_KRYMA Unreviewed; 422 AA.
AC A0A3Q3AF34;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Carboxypeptidase A1 {ECO:0000256|ARBA:ARBA00040642};
DE EC=3.4.17.1 {ECO:0000256|ARBA:ARBA00039144};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000014740.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000014740.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of a C-terminal amino acid, but little or no action
CC with -Asp, -Glu, -Arg, -Lys or -Pro.; EC=3.4.17.1;
CC Evidence={ECO:0000256|ARBA:ARBA00036253};
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_017292307.1; XM_017436818.1.
DR AlphaFoldDB; A0A3Q3AF34; -.
DR STRING; 37003.ENSKMAP00000014740; -.
DR Ensembl; ENSKMAT00000014954.1; ENSKMAP00000014740.1; ENSKMAG00000011054.1.
DR GeneID; 108248203; -.
DR KEGG; kmr:108248203; -.
DR CTD; 93979; -.
DR GeneTree; ENSGT00940000158082; -.
DR OMA; SHGISYE; -.
DR OrthoDB; 3540647at2759; -.
DR Proteomes; UP000264800; 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:InterPro.
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:SF94; CARBOXYPEPTIDASE A1; 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 Coiled coil {ECO:0000256|SAM:Coils};
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 Reference proteome {ECO:0000313|Proteomes:UP000264800};
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..422
FT /note="Carboxypeptidase A1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018598908"
FT DOMAIN 173..195
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00132"
FT DOMAIN 309..319
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00133"
FT COILED 80..111
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 422 AA; 48131 MW; 6D0F7B72A62AFE22 CRC64;
MMRGMLTFAA LFVVVLAKET FEGHQVLRII PKNDIQLSLI KDLEKMIEFE LDIWMRVTNI
FSPVDVRVPS HTLQSFKSYL ENLNIEYATM IENLQAILDE EQEEMDSAAR VAQPKHTDSF
DYTRYHPINE IYSFQNMLVA ENPNLVSKIV IGQSYEGRPL NVLKFSTGGT NHPAIWIDTG
IHSREWVTQA SGIWFAKKIV KEYGRDPALT AILNNMDIFL EIVTNPDGYY YTHTSNRMWR
KTRKPNSGSS CIGVDPNRNW DAGFGGPGAS SYPCSETYCG PRAHSESEVK SIVDFVKSHG
NIKAFISIHS YSQMLMYPYG YTRTPVKDQA ELHQLAQKAI TDLASLYGTR YRYGSIINTI
YQASGGTIDW TYNQGVKYSY TFELRDTGRY GFLLPANQIV PTAEETWLAL MAIMDHTYKN
PY
//