CBPA1_MOUSE
ID CBPA1_MOUSE Reviewed; 419 AA.
AC Q7TPZ8;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Carboxypeptidase A1;
DE EC=3.4.17.1;
DE Flags: Precursor;
GN Name=Cpa1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Egg;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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. {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P00730};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P00730};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
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DR EMBL; BC052661; AAH52661.1; -; mRNA.
DR CCDS; CCDS19977.1; -.
DR RefSeq; NP_079626.2; NM_025350.4.
DR AlphaFoldDB; Q7TPZ8; -.
DR SMR; Q7TPZ8; -.
DR STRING; 10090.ENSMUSP00000031806; -.
DR MEROPS; M14.001; -.
DR iPTMnet; Q7TPZ8; -.
DR PhosphoSitePlus; Q7TPZ8; -.
DR MaxQB; Q7TPZ8; -.
DR PaxDb; Q7TPZ8; -.
DR PRIDE; Q7TPZ8; -.
DR ProteomicsDB; 279930; -.
DR Antibodypedia; 17964; 540 antibodies from 39 providers.
DR DNASU; 109697; -.
DR Ensembl; ENSMUST00000031806; ENSMUSP00000031806; ENSMUSG00000054446.
DR GeneID; 109697; -.
DR KEGG; mmu:109697; -.
DR UCSC; uc009bfq.1; mouse.
DR CTD; 1357; -.
DR MGI; MGI:88478; Cpa1.
DR VEuPathDB; HostDB:ENSMUSG00000054446; -.
DR eggNOG; KOG2650; Eukaryota.
DR GeneTree; ENSGT00940000158082; -.
DR HOGENOM; CLU_019326_0_0_1; -.
DR InParanoid; Q7TPZ8; -.
DR OMA; SHGISYE; -.
DR OrthoDB; 524270at2759; -.
DR PhylomeDB; Q7TPZ8; -.
DR TreeFam; TF317197; -.
DR BioGRID-ORCS; 109697; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Cpa1; mouse.
DR PRO; PR:Q7TPZ8; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q7TPZ8; protein.
DR Bgee; ENSMUSG00000054446; Expressed in pyloric antrum and 57 other tissues.
DR Genevisible; Q7TPZ8; MM.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0008238; F:exopeptidase activity; ISO:MGI.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; ISO:MGI.
DR GO; GO:0046686; P:response to cadmium ion; ISO:MGI.
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 Carboxypeptidase; Disulfide bond; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Secreted; Signal; Zinc;
KW Zymogen.
FT SIGNAL 1..16
FT /evidence="ECO:0000250"
FT PROPEP 17..110
FT /note="Activation peptide"
FT /id="PRO_0000004347"
FT CHAIN 111..419
FT /note="Carboxypeptidase A1"
FT /id="PRO_0000004348"
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"
SQ SEQUENCE 419 AA; 47385 MW; 837CD5FEA3FBBECC CRC64;
MKRLLVLSVL LAAVFGNENF VGHQVLRISA TDEAQVQKVR ELEELEHLKL DFWRDPARAG
LPIDVRVPFP TIQSVKAFLE YHDISYEIMI EDVQSLLDEE KQQMSAFQAR ALSTDAFNYA
TYHTLDEIYE FMDLLVTEHP QLVSKIQIGS TFEGRPINVL KFSTGGTNRP AIWIDTGIHS
REWVTQASGV WFAKKITKDY GQEPTLTAIL DNMDIFLEIV TNPDGFVYTH KTNRMWRKTR
SHTEGSLCVG VDPNRNWDAA FGMPGASSNP CSETYRGKFP NSEVEVKSIV DFVTSHGNIK
AFISIHSYSQ LLLYPYGYTS EPAPDKEELD QLAKSAVTAL TSLHGTKFKY GSIIDTIYQA
SGSTIDWTYS QGIKYSFTFE LRDTGLRGFL LPASQIIPTA EETWLALLTI MDHTVKHPY
