CBPA1_RAT
ID CBPA1_RAT Reviewed; 419 AA.
AC P00731;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Carboxypeptidase A1 {ECO:0000305};
DE EC=3.4.17.1 {ECO:0000250|UniProtKB:P15085};
DE Flags: Precursor;
GN Name=Cpa1 {ECO:0000312|RGD:2388}; Synonyms=Cpa;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6275388; DOI=10.1073/pnas.79.1.31;
RA Quinto C., Quiroga M., Swain W.F., Nikovits W.C. Jr., Standring D.N.,
RA Pictet R.L., Valenzuela P., Rutter W.J.;
RT "Rat preprocarboxypeptidase A: cDNA sequence and preliminary
RT characterization of the gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:31-35(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3182872; DOI=10.1016/s0021-9258(19)77911-3;
RA Clauser E., Gardell S.J., Craik C.S., Macdonald R.J., Rutter W.J.;
RT "Structural characterization of the rat carboxypeptidase A1 and B genes.
RT Comparative analysis of the rat carboxypeptidase gene family.";
RL J. Biol. Chem. 263:17837-17845(1988).
CC -!- FUNCTION: Carboxypeptidase that catalyzes the release of a C-terminal
CC amino acid, but has little or no action with -Asp, -Glu, -Arg, -Lys or
CC -Pro (By similarity). Catalyzes the conversion of leukotriene C4 to
CC leukotriene F4 via the hydrolysis of an amide bond (By similarity).
CC {ECO:0000250|UniProtKB:P00730, ECO:0000250|UniProtKB:P15085}.
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:0000250|UniProtKB:P15085};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + leukotriene C4 = glycine + leukotriene F4;
CC Xref=Rhea:RHEA:50740, ChEBI:CHEBI:15377, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:57973, ChEBI:CHEBI:133618;
CC Evidence={ECO:0000250|UniProtKB:P00730};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50741;
CC Evidence={ECO:0000250|UniProtKB:P00730};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P15085};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P15085};
CC -!- SUBUNIT: Monomer. May form a complex with proelastase 2.
CC {ECO:0000250|UniProtKB:P15085}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P15085}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; V01232; CAA24542.1; -; mRNA.
DR EMBL; J00713; AAA40893.1; -; mRNA.
DR EMBL; M23990; AAA40955.1; -; Genomic_DNA.
DR EMBL; M23960; AAA40955.1; JOINED; Genomic_DNA.
DR EMBL; M23985; AAA40955.1; JOINED; Genomic_DNA.
DR EMBL; M23986; AAA40955.1; JOINED; Genomic_DNA.
DR EMBL; M23987; AAA40955.1; JOINED; Genomic_DNA.
DR EMBL; M23988; AAA40955.1; JOINED; Genomic_DNA.
DR EMBL; M23989; AAA40955.1; JOINED; Genomic_DNA.
DR PIR; A00911; CPRTA.
DR RefSeq; NP_058694.2; NM_016998.3.
DR AlphaFoldDB; P00731; -.
DR SMR; P00731; -.
DR STRING; 10116.ENSRNOP00000014465; -.
DR MEROPS; M14.001; -.
DR PhosphoSitePlus; P00731; -.
DR PaxDb; P00731; -.
DR Ensembl; ENSRNOT00000014465; ENSRNOP00000014465; ENSRNOG00000010725.
DR GeneID; 24269; -.
DR KEGG; rno:24269; -.
DR UCSC; RGD:2388; rat.
DR CTD; 1357; -.
DR RGD; 2388; Cpa1.
DR eggNOG; KOG2650; Eukaryota.
DR GeneTree; ENSGT00940000158082; -.
DR HOGENOM; CLU_019326_0_0_1; -.
DR InParanoid; P00731; -.
DR OMA; KVHIANM; -.
DR OrthoDB; 524270at2759; -.
DR PhylomeDB; P00731; -.
DR TreeFam; TF317197; -.
DR BRENDA; 3.4.17.1; 5301.
DR SABIO-RK; P00731; -.
DR PRO; PR:P00731; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000010725; Expressed in pancreas and 14 other tissues.
DR Genevisible; P00731; RN.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0008238; F:exopeptidase activity; IDA:RGD.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006691; P:leukotriene metabolic process; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IDA:RGD.
DR GO; GO:0046686; P:response to cadmium ion; IDA:RGD.
DR CDD; cd03870; M14_CPA; 1.
DR Gene3D; 3.30.70.340; -; 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 Pfam; PF00246; Peptidase_M14; 1.
DR Pfam; PF02244; Propep_M14; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00631; Zn_pept; 1.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
PE 2: Evidence at transcript level;
KW Carboxypeptidase; Disulfide bond; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Secreted; Signal; Zinc;
KW Zymogen.
FT SIGNAL 1..16
FT PROPEP 17..110
FT /note="Activation peptide"
FT /id="PRO_0000004351"
FT CHAIN 111..419
FT /note="Carboxypeptidase A1"
FT /id="PRO_0000004352"
FT ACT_SITE 380
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00732"
FT BINDING 179..182
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 237
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 254..255
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 307..308
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 358
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT DISULFID 248..271
FT /evidence="ECO:0000250|UniProtKB:Q96IY4"
FT CONFLICT 196
FT /note="I -> V (in Ref. 1; CAA24542/AAA40893)"
FT /evidence="ECO:0000305"
FT CONFLICT 261..263
FT /note="FGM -> LGK (in Ref. 1; CAA24542/AAA40893)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="K -> E (in Ref. 1; CAA24542/AAA40893)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 419 AA; 47197 MW; BB002D1CB99B7491 CRC64;
MKRLLILSLL LEAVCGNENF VGHQVLRISA ADEAQVQKVK ELEDLEHLQL DFWRDAARAG
IPIDVRVPFP SIQSVKAFLE YHGISYEIMI EDVQLLLDEE KQQMSAFQAR ALSTDSFNYA
TYHTLDEIYE FMDLLVAEHP QLVSKIQIGN TFEGRPIHVL KFSTGGTNRP AIWIDTGIHS
REWVTQASGV WFAKKITKDY GQDPTFTAVL DNMDIFLEIV TNPDGFAYTH KTNRMWRKTR
SHTQGSLCVG VDPNRNWDAG FGMAGASSNP CSETYRGKFP NSEVEVKSIV DFVTSHGNIK
AFISIHSYSQ LLLYPYGYTS EPAPDQAELD QLAKSAVTAL TSLHGTKFKY GSIIDTIYQA
SGSTIDWTYS QGIKYSFTFE LRDTGLRGFL LPASQIIPTA EETWLALLTI MDHTVKHPY
