CBPA1_PIG
ID CBPA1_PIG Reviewed; 419 AA.
AC P09954; Q9TV85;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 07-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Carboxypeptidase A1 {ECO:0000305};
DE EC=3.4.17.1 {ECO:0000250|UniProtKB:P15085};
DE Flags: Precursor;
GN Name=CPA1; Synonyms=CPA;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pancreas;
RX PubMed=10092856; DOI=10.1046/j.1432-1327.1999.00091.x;
RA Darnis S., Juge N., Marino C., Aviles F.X., Puigserver A., Chaix J.-C.,
RA Guo X.-J.;
RT "Cloning, sequencing and functional expression of a cDNA encoding porcine
RT pancreatic preprocarboxypeptidase A1.";
RL Eur. J. Biochem. 259:719-725(1999).
RN [2]
RP PROTEIN SEQUENCE OF 17-110.
RX PubMed=3801014; DOI=10.1016/s0006-291x(86)80203-0;
RA Vendrell J., Aviles F.X., Genesca E., San Segundo B., Soriano F.,
RA Mendez E.;
RT "Primary structure of the activation segment of procarboxypeptidase A from
RT porcine pancreas.";
RL Biochem. Biophys. Res. Commun. 141:517-523(1986).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 17-416 IN COMPLEX WITH ZINC, AND
RP DISULFIDE BONDS.
RX PubMed=1548696; DOI=10.1016/0022-2836(92)90581-4;
RA Guasch A., Coll M., Aviles F.X., Huber R.;
RT "Three-dimensional structure of porcine pancreatic procarboxypeptidase A. A
RT comparison of the A and B zymogens and their determinants for inhibition
RT and activation.";
RL J. Mol. Biol. 224:141-157(1992).
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:0000269|PubMed:1548696};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:1548696};
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}.
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DR EMBL; AF076222; AAD17690.1; -; mRNA.
DR PIR; A25833; A25833.
DR RefSeq; NP_999409.1; NM_214244.1.
DR PDB; 1PCA; X-ray; 2.00 A; A=17-416.
DR PDBsum; 1PCA; -.
DR AlphaFoldDB; P09954; -.
DR SMR; P09954; -.
DR STRING; 9823.ENSSSCP00000017542; -.
DR MEROPS; M14.001; -.
DR PaxDb; P09954; -.
DR PeptideAtlas; P09954; -.
DR PRIDE; P09954; -.
DR Ensembl; ENSSSCT00000018027; ENSSSCP00000017542; ENSSSCG00000016557.
DR Ensembl; ENSSSCT00005021812; ENSSSCP00005013034; ENSSSCG00005012876.
DR Ensembl; ENSSSCT00015109965; ENSSSCP00015046871; ENSSSCG00015080770.
DR Ensembl; ENSSSCT00025005864; ENSSSCP00025002350; ENSSSCG00025004377.
DR Ensembl; ENSSSCT00030101649; ENSSSCP00030046883; ENSSSCG00030072216.
DR Ensembl; ENSSSCT00035095737; ENSSSCP00035040283; ENSSSCG00035070804.
DR Ensembl; ENSSSCT00040089710; ENSSSCP00040039429; ENSSSCG00040064161.
DR Ensembl; ENSSSCT00045022732; ENSSSCP00045015681; ENSSSCG00045013082.
DR Ensembl; ENSSSCT00050040692; ENSSSCP00050016802; ENSSSCG00050030259.
DR Ensembl; ENSSSCT00055049881; ENSSSCP00055039852; ENSSSCG00055024544.
DR Ensembl; ENSSSCT00060073136; ENSSSCP00060031548; ENSSSCG00060053692.
DR Ensembl; ENSSSCT00065065865; ENSSSCP00065028533; ENSSSCG00065048136.
DR Ensembl; ENSSSCT00070055028; ENSSSCP00070046686; ENSSSCG00070027422.
DR GeneID; 397476; -.
DR KEGG; ssc:397476; -.
DR CTD; 1357; -.
DR VGNC; VGNC:86930; CPA1.
DR eggNOG; KOG2650; Eukaryota.
DR GeneTree; ENSGT00940000158082; -.
DR HOGENOM; CLU_019326_0_0_1; -.
DR InParanoid; P09954; -.
DR OMA; SHGISYE; -.
DR OrthoDB; 524270at2759; -.
DR TreeFam; TF317197; -.
DR EvolutionaryTrace; P09954; -.
DR Proteomes; UP000008227; Chromosome 18.
DR Proteomes; UP000314985; Chromosome 18.
DR Bgee; ENSSSCG00000016557; Expressed in testis and 30 other tissues.
DR ExpressionAtlas; P09954; baseline and differential.
DR Genevisible; P09954; SS.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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 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 1: Evidence at protein level;
KW 3D-structure; Carboxypeptidase; Direct protein sequencing; Disulfide bond;
KW Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:3801014"
FT PROPEP 17..110
FT /note="Activation peptide"
FT /id="PRO_0000004349"
FT CHAIN 111..419
FT /note="Carboxypeptidase A1"
FT /id="PRO_0000004350"
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:0007744|PDB:1PCA"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0007744|PDB:1PCA"
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:0007744|PDB:1PCA"
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:0007744|PDB:1PCA"
FT STRAND 24..28
FT /evidence="ECO:0007829|PDB:1PCA"
FT HELIX 33..42
FT /evidence="ECO:0007829|PDB:1PCA"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:1PCA"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:1PCA"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:1PCA"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:1PCA"
FT HELIX 72..81
FT /evidence="ECO:0007829|PDB:1PCA"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:1PCA"
FT HELIX 93..106
FT /evidence="ECO:0007829|PDB:1PCA"
FT HELIX 125..138
FT /evidence="ECO:0007829|PDB:1PCA"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:1PCA"
FT STRAND 143..150
FT /evidence="ECO:0007829|PDB:1PCA"
FT STRAND 156..162
FT /evidence="ECO:0007829|PDB:1PCA"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:1PCA"
FT HELIX 183..199
FT /evidence="ECO:0007829|PDB:1PCA"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:1PCA"
FT HELIX 204..210
FT /evidence="ECO:0007829|PDB:1PCA"
FT STRAND 214..219
FT /evidence="ECO:0007829|PDB:1PCA"
FT HELIX 223..231
FT /evidence="ECO:0007829|PDB:1PCA"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:1PCA"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:1PCA"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:1PCA"
FT HELIX 284..296
FT /evidence="ECO:0007829|PDB:1PCA"
FT STRAND 299..306
FT /evidence="ECO:0007829|PDB:1PCA"
FT STRAND 308..315
FT /evidence="ECO:0007829|PDB:1PCA"
FT HELIX 326..344
FT /evidence="ECO:0007829|PDB:1PCA"
FT STRAND 349..352
FT /evidence="ECO:0007829|PDB:1PCA"
FT HELIX 353..356
FT /evidence="ECO:0007829|PDB:1PCA"
FT HELIX 364..370
FT /evidence="ECO:0007829|PDB:1PCA"
FT STRAND 375..380
FT /evidence="ECO:0007829|PDB:1PCA"
FT STRAND 384..387
FT /evidence="ECO:0007829|PDB:1PCA"
FT HELIX 393..395
FT /evidence="ECO:0007829|PDB:1PCA"
FT HELIX 396..416
FT /evidence="ECO:0007829|PDB:1PCA"
SQ SEQUENCE 419 AA; 47235 MW; 84B4CB557B714FC1 CRC64;
MWGLLIFSVL LGGVLAKEDF VGHQVLRISV DDEAQVQKVK ELEDLEHLQL DFWRGPARPG
FPIDVRVPFP SIQAVKVFLE AHGIRYTIMI EDVQLLLDEE QEQMFASQGR ARTTSTFNYA
TYHTLEEIYD FMDILVAEHP QLVSKLQIGS SYEGRPIYVL KFSTGGNNRP AIWIDTGIHS
REWVTQASGV WFAKKITEDY GQDPAFTAIL DNLDIFLEIV TNPDGFAFTH SENRMWRKTR
SRTSGSFCVG VDPNRNWDAG FGGAGASSNP CSETYHGKFP NSEVEVKSIV DFVNDHGNIK
AFISIHSYSQ LLLYPYGYKT EAPADKDELD QISKSAVAAL TSLYGTKFQY GSIITTIYQA
SGGTIDWTYN QGIKYSFSFE LRDTGRYGFL LPASQIIPTA QETWLALLTI MEHTLNHPY
