Reviewed,
UniProtKB/Swiss-Prot O89001 (CBPD_MOUSE)
Last modified
June 16, 2009.
Version 71.
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Carboxypeptidase D EC=3.4.17.22 Alternative name(s): Metallocarboxypeptidase D gp180 | ||
| Gene names |
| ||
| Organism | Mus musculus (Mouse) | ||
| Taxonomic identifier | 10090 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus |
Protein attributes
| Sequence length | 1377 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | Releases C-terminal Arg and Lys from polypeptides. |
| Cofactor | Binds 2 zinc ions per subunit By similarity. |
| Subcellular location | Membrane; Single-pass type I membrane protein Potential. |
| Domain | There are 3 carboxypeptidase-like domains. Only the first two domains seem to have kept a catalytic activity. |
| Sequence similarities | Belongs to the peptidase M14 family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Membrane |
| Domain | Repeat Signal Transmembrane |
| Ligand | Metal-binding Zinc |
| Molecular function | Carboxypeptidase Hydrolase Metalloprotease Protease |
| PTM | Glycoprotein Lipoprotein Palmitate Phosphoprotein |
| Gene Ontology (GO) | |
| Biological process | proteolysis Inferred from electronic annotation. Source: InterPro |
| Cellular component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | metallocarboxypeptidase activity Inferred from electronic annotation. Source: InterPro serine-type carboxypeptidase activityInferred from electronic annotation. Source: InterPro zinc ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 37 | 37 | Potential | ||||||
| Chain | 38 – 1377 | 1340 | Carboxypeptidase D | PRO_0000004402 | |||||
Regions | |||||||||
| Topological domain | 38 – 1296 | 1259 | Extracellular Potential | ||||||
| Transmembrane | 1297 – 1317 | 21 | Potential | ||||||
| Topological domain | 1318 – 1377 | 60 | Cytoplasmic Potential | ||||||
| Region | 38 – 492 | 455 | Carboxypeptidase-like 1 | ||||||
| Region | 493 – 896 | 404 | Carboxypeptidase-like 2 | ||||||
| Region | 897 – 1296 | 400 | Carboxypeptidase-like 3 | ||||||
| Motif | 161 – 163 | 3 | Cell attachment site Potential | ||||||
Sites | |||||||||
| Active site | 349 | 1 | Nucleophile 1 By similarity | ||||||
| Active site | 761 | 1 | Nucleophile 2 By similarity | ||||||
| Metal binding | 138 | 1 | Zinc 1 By similarity | ||||||
| Metal binding | 141 | 1 | Zinc 1 By similarity | ||||||
| Metal binding | 256 | 1 | Zinc 1 By similarity | ||||||
| Metal binding | 563 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 566 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 670 | 1 | Zinc 2 By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 1341 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 1365 | 1 | Phosphothreonine Ref.2 | ||||||
| Modified residue | 1367 | 1 | Phosphothreonine Ref.2 | ||||||
| Modified residue | 1373 | 1 | Phosphotyrosine By similarity | ||||||
| Lipidation | 1314 | 1 | S-palmitoyl cysteine By similarity | ||||||
| Lipidation | 1318 | 1 | S-palmitoyl cysteine By similarity | ||||||
| Lipidation | 1320 | 1 | S-palmitoyl cysteine By similarity | ||||||
| Glycosylation | 171 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 216 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 398 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 409 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 428 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 521 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 625 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 810 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 854 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 866 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 878 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 952 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 975 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1067 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1139 | 1 | N-linked (GlcNAc...) Potential | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Cloning, functional expression, and chromosomal localization of the human and mouse gp180-carboxypeptidase D-like enzyme." Ishikawa T., Murakami K., Kido Y., Ohnishi S., Yazaki Y., Harada F., Kuroki K. Gene 215:361-370(1998) [PubMed: 9714835] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c. Tissue: Liver. |
| [2] | "Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1365 AND THR-1367, MASS SPECTROMETRY. Tissue: Liver. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| D85391 mRNA. Translation: BAA33371.1. | |
| IPI | IPI00130573. |
| UniGene | Mm.276736 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1H8L based on UniProtKB Q90240. |
| SMR | O89001. Positions 493-872. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | M14.016. |
PTM databases | |
| PhosphoSite | O89001. |
Proteomic databases | |
| PRIDE | O89001. |
Genome annotation databases | |
| Ensembl | ENSMUSG00000020841. Mus musculus. [Contig view] |
Organism-specific databases | |
| MGI | MGI:107265. Cpd. |
Phylogenomic databases | |
| HOGENOM | O89001. |
| HOVERGEN | O89001. |
Enzyme and pathway databases | |
| BRENDA | 3.4.17.22. 244. |
Gene expression databases | |
| ArrayExpress | O89001. |
| Bgee | O89001. |
| CleanEx | MM_CPD. |
| GermOnline | ENSMUSG00000020841. Mus musculus. |
Family and domain databases | |
| InterPro | IPR014766. CarboxyPept_regulatory. IPR015567. Pept_M14B_carboxypept_D2. IPR000834. Peptidase_M14. [Graphical view] |
| Gene3D | G3DSA:2.60.40.1120. CarboxyPept_regulatory. 3 hits. |
| PANTHER | PTHR11532:SF8. C_peptidase_D. 1 hit. |
| Pfam | PF00246. Peptidase_M14. 3 hits. [Graphical view] |
| PRINTS | PR00765. CRBOXYPTASEA. |
| SMART | SM00631. Zn_pept. 3 hits. [Graphical view] |
| PROSITE | PS00132. CARBOXYPEPT_ZN_1. 2 hits. PS00133. CARBOXYPEPT_ZN_2. 2 hits. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| SOURCE | Search... |
Entry information
| Entry name | CBPD_MOUSE | ||||||||
| Accession | Primary (citable) accession number: O89001 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |
