CBPO_DANRE
ID CBPO_DANRE Reviewed; 363 AA.
AC B8JLQ9;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Carboxypeptidase O {ECO:0000312|ZFIN:ZDB-GENE-070619-6};
DE EC=3.4.17.- {ECO:0000269|PubMed:21921028};
DE Flags: Precursor;
GN Name=cpo {ECO:0000312|ZFIN:ZDB-GENE-070619-6};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000312|Proteomes:UP000000437};
RN [1] {ECO:0000312|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000312|Proteomes:UP000000437};
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 25-29, FUNCTION, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP GLYCOSYLATION.
RX PubMed=21921028; DOI=10.1074/jbc.m111.265819;
RA Lyons P.J., Fricker L.D.;
RT "Carboxypeptidase O is a glycosylphosphatidylinositol-anchored intestinal
RT peptidase with acidic amino acid specificity.";
RL J. Biol. Chem. 286:39023-39032(2011).
CC -!- FUNCTION: Carboxypeptidase which preferentially cleaves C-terminal
CC acidic residues from peptides and proteins. Can also cleave C-terminal
CC hydrophobic amino acids, with a preference for small residues over
CC large residues. {ECO:0000269|PubMed:21921028}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P00730};
CC -!- ACTIVITY REGULATION: Strongly inhibited by potato carboxypeptidase
CC inhibitor, and the chelating agents EDTA and 1,10-phenanthroline. Also
CC inhibited by compounds with multiple carboxylic acid groups such as
CC citrate and succinate, and to a lesser exent the amino acids aspartate
CC and glutamate. Not significantly inhibited by benzylsuccinic acid.
CC {ECO:0000269|PubMed:21921028}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=346 uM for 3-(2-furyl)acryloyl-Glu-Glu (at pH 7.5)
CC {ECO:0000269|PubMed:21921028};
CC KM=324 uM for 3-(2-furyl)acryloyl-Phe-Phe (at pH 7.5)
CC {ECO:0000269|PubMed:21921028};
CC KM=794 uM for 3-(2-furyl)acryloyl-Phe-Ala (at pH 7.5)
CC {ECO:0000269|PubMed:21921028};
CC KM=743 uM for 3-(2-furyl)acryloyl-Lys-Ala (at pH 7.5)
CC {ECO:0000269|PubMed:21921028};
CC pH dependence:
CC Optimum pH is 6.5-7.5. {ECO:0000269|PubMed:21921028};
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:Q8IVL8}; Lipid-anchor, GPI-anchor
CC {ECO:0000250|UniProtKB:Q8IVL8}.
CC -!- TISSUE SPECIFICITY: Expressed in intestinal epithelium.
CC {ECO:0000269|PubMed:21921028}.
CC -!- DEVELOPMENTAL STAGE: Detected in intestine from 3 days post-
CC fertilization onwards. {ECO:0000269|PubMed:21921028}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:21921028}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
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DR EMBL; CU469569; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001139101.1; NM_001145629.1.
DR AlphaFoldDB; B8JLQ9; -.
DR SMR; B8JLQ9; -.
DR STRING; 7955.ENSDARP00000097989; -.
DR MEROPS; M14.021; -.
DR PaxDb; B8JLQ9; -.
DR PeptideAtlas; B8JLQ9; -.
DR Ensembl; ENSDART00000109756; ENSDARP00000097989; ENSDARG00000077688.
DR GeneID; 100005630; -.
DR KEGG; dre:100005630; -.
DR CTD; 130749; -.
DR ZFIN; ZDB-GENE-070619-6; cpo.
DR eggNOG; KOG2650; Eukaryota.
DR GeneTree; ENSGT00940000161508; -.
DR HOGENOM; CLU_019326_4_1_1; -.
DR InParanoid; B8JLQ9; -.
DR OMA; TKKIIWM; -.
DR OrthoDB; 524270at2759; -.
DR PhylomeDB; B8JLQ9; -.
DR TreeFam; TF317197; -.
DR PRO; PR:B8JLQ9; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 1.
DR Bgee; ENSDARG00000077688; Expressed in intestine and 5 other tissues.
DR GO; GO:0046658; C:anchored component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd06247; M14_CPO; 1.
DR InterPro; IPR033850; Carboxypeptidase_O.
DR InterPro; IPR000834; Peptidase_M14.
DR Pfam; PF00246; Peptidase_M14; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00631; Zn_pept; 1.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
PE 1: Evidence at protein level;
KW Carboxypeptidase; Cell membrane; Direct protein sequencing; Glycoprotein;
KW GPI-anchor; Hydrolase; Lipoprotein; Membrane; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Signal; Zinc.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:21921028"
FT CHAIN 25..339
FT /note="Carboxypeptidase O"
FT /evidence="ECO:0000305"
FT /id="PRO_5002875554"
FT PROPEP 340..363
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000437882"
FT ACT_SITE 298
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00732"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT LIPID 339
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 363 AA; 40964 MW; 95495F92EB375070 CRC64;
MMQASITSIL VVLTLVAQDR LAGGLEHKSY DYTKYHTMDE ISAWMNQMQR ENPDVVSTMT
YGQTYEKRNI TLLKIGFSST TPKKAIWMDC GIHAREWIAP AFCQHFVKEV LGSYKTDSRV
NMLFKNLDFY ITPVLNMDGY IYSWLNNSTR LWRKSRSPCH ENSTCSGTDL NRNFYANWGM
VGISRNCCSE VYNGATALSE PEAEAVTDFL GAHQNHLLCY LTIHSYGQLI LVPYGHPNIS
APNYDELMEV GLAAAKAIKA VHGKSYKVGS SPDVLYPNSG SSRDFARLIG IPYSFTFELR
DEGQHGFILP EDQIQPTCQE AYEGAMSIIN YVHDKNFKNT AITVTATLWT TLMALWISTS
HVF
