ID A0A2D0RHY6_ICTPU Unreviewed; 431 AA.
AC A0A2D0RHY6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2023, sequence version 3.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Carboxypeptidase A1 {ECO:0000313|RefSeq:XP_017330143.3};
GN Name=LOC108269091 {ECO:0000313|RefSeq:XP_017330143.3};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017330143.3};
RN [1] {ECO:0000313|RefSeq:XP_017330143.3}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017330143.3};
RG RefSeq;
RL Submitted (NOV-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_017330143.1; XM_017474654.1.
DR RefSeq; XP_017330143.3; XM_017474654.3.
DR AlphaFoldDB; A0A2D0RHY6; -.
DR STRING; 7998.ENSIPUP00000020159; -.
DR Ensembl; ENSIPUT00000021029; ENSIPUP00000020159; ENSIPUG00000013685.
DR GeneID; 108269091; -.
DR KEGG; ipu:108269091; -.
DR OMA; YARYHTI; -.
DR OrthoDB; 3540647at2759; -.
DR Proteomes; UP000221080; Chromosome 8.
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 ECO:0000313|RefSeq:XP_017330143.3};
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..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..431
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039888561"
FT DOMAIN 182..204
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00132"
FT DOMAIN 318..328
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00133"
SQ SEQUENCE 431 AA; 49133 MW; 2B611E91C85CAFED CRC64;
MDSLESTFLG RKMRGLWVLL ALFVAVFGKE TFEGHQVLRI TAVNEAQINL LKELSEIEHL
GLDFWMDPVD VSLPVDVRVP FYSLQDVRAF LGYHEIHYEI MIQDLQDLLN EEQREILRSM
ALQPRSTEDY NYANYHTLNE INSFIDMLVQ ENPGFVSKIV IGQSYEKRPL NVLKFSTGAN
RPGLWIDTGI HSREWVTQAS GTWFAKKIVT DYGRDAELTD ILNKYDIFLE IVTNPDGFQF
THTNNRMWRK TRKPNSGSSC IGVDPNRNWD AGFGGAGASS SPCSETYRGP SANSEPEVKA
IVDFVKSHGK IKAFVSIHSY SQMLLYPYGY TQTPCKDQAE LHELARKAIT ALSSLYNTQY
RFGSIINTIY QASGGTIDWT YNQGIKYSYT FELRDTGRYG FILPANQIIP TAQETWLALM
AIMKHTKDNP Y
//
