CBP1_SABMA
ID CBP1_SABMA Reviewed; 138 AA.
AC P86516;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 03-AUG-2022, entry version 28.
DE RecName: Full=Carboxypeptidase {ECO:0000303|PubMed:19694804};
DE Short=CP {ECO:0000303|PubMed:19694804};
DE EC=3.4.17.-;
DE Flags: Fragments;
OS Sabellastarte magnifica (Feather duster).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC Sedentaria; Canalipalpata; Sabellida; Sabellidae; Sabellastarte.
OX NCBI_TaxID=389514;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MASS SPECTROMETRY.
RX PubMed=19694804; DOI=10.1111/j.1742-4658.2009.07187.x;
RA Alonso-del-Rivero M., Trejo S.A., Rodriguez de la Vega M., Gonzalez Y.,
RA Bronsoms S., Canals F., Delfin J., Diaz J., Aviles F.X., Chavez M.A.;
RT "A novel metallocarboxypeptidase-like enzyme from the marine annelid
RT Sabellastarte magnifica--a step into the invertebrate world of proteases.";
RL FEBS J. 276:4875-4890(2009).
CC -!- FUNCTION: Carboxypeptidase that catalyzes the release of hydrophobic
CC and acidic C-terminal amino acids. {ECO:0000269|PubMed:19694804}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:19694804};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:19694804};
CC -!- ACTIVITY REGULATION: Completely inhibited by the A-type
CC carboxypeptidase inhibitor benzylsuccinic acid. Inhibited by the leech
CC carboxypeptidase inhibitor and the potato carboxydase inhibitor.
CC Inhibited by the chelating agent 1,10-phenanthroline. Partial
CC inhibition by preincubation with the chelating agent EDTA is reversed
CC by addition of Zn(2+). Not inhibited by the cysteine protease
CC inhibitors L-carboxy-trans-2,3-epoxypropyl-leycylamido (4-guanidino)
CC butane, E-64 and cystatin, the aspartic protease inhibitor pepstatin,
CC or the serine protease inhibitors Pefabloc, soybean trypsin-
CC chymotrypsin inhibitor, soybean trypsin inhibitor and aprotinin.
CC {ECO:0000269|PubMed:19694804}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.05 mM for N-(4-methoxyphenylazoformyl)-L-phenyl-alanine (AAFP)
CC {ECO:0000269|PubMed:19694804};
CC KM=0.36 mM for hippuryl-Phe {ECO:0000269|PubMed:19694804};
CC KM=0.14 mM for N-(3-[2-furyl]acryloyl)-Phe-Phe (FAPP)
CC {ECO:0000269|PubMed:19694804};
CC pH dependence:
CC Optimum pH is 7.0-7.5 with AAFP as substrate.
CC {ECO:0000269|PubMed:19694804};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P00732}.
CC -!- TISSUE SPECIFICITY: Detected in the body but not in the tentacle crown
CC (at protein level). {ECO:0000269|PubMed:19694804}.
CC -!- MASS SPECTROMETRY: Mass=33792.885; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:19694804};
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000255}.
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 AlphaFoldDB; P86516; -.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0004180; F:carboxypeptidase activity; IDA:UniProtKB.
DR GO; GO:0008237; F:metallopeptidase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Carboxypeptidase; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Metal-binding; Metalloprotease; Protease; Secreted; Zinc.
FT CHAIN 1..>138
FT /note="Carboxypeptidase"
FT /id="PRO_0000394411"
FT REGION 61..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 136
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00732"
FT BINDING 43..46
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 43
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P15086"
FT BINDING 72..73
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15085"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P15086"
FT BINDING 97..98
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15085"
FT DISULFID 66..79
FT /evidence="ECO:0000250|UniProtKB:P48052"
FT NON_CONS 19..20
FT /evidence="ECO:0000303|PubMed:19694804"
FT NON_CONS 35..36
FT /evidence="ECO:0000303|PubMed:19694804"
FT NON_CONS 45..46
FT /evidence="ECO:0000303|PubMed:19694804"
FT NON_CONS 56..57
FT /evidence="ECO:0000303|PubMed:19694804"
FT NON_CONS 60..61
FT /evidence="ECO:0000303|PubMed:19694804"
FT NON_CONS 95..96
FT /evidence="ECO:0000303|PubMed:19694804"
FT NON_CONS 100..101
FT /evidence="ECO:0000303|PubMed:19694804"
FT NON_CONS 125..126
FT /evidence="ECO:0000303|PubMed:19694804"
FT NON_CONS 129..130
FT /evidence="ECO:0000303|PubMed:19694804"
FT NON_TER 138
FT /evidence="ECO:0000303|PubMed:19694804"
SQ SEQUENCE 138 AA; 15590 MW; 880B6ED52AAAAA9D CRC64;
AFDLNDFNTL EDTYDQMNVF QLSEAGLTHE GRDMKSWIDS LTHCRSHLDE DVFMFKRNEP
DSGSACVGTD LNRSSNNPCS DTYGGSGPAS ALETRHSYSQ QYEDELNQRQ RYEPSGTTVN
NLLNKDAGSI YSYTPELR
