UniProt Accession

 CBPD_HUMAN; O75976; B7Z7T9; B7ZAU4; F5GZH6; O15377; Q86SH9; Q86XE6 

Genbank Protein ID

 D85390; U65090; AK302497; AK316409; AC006050; AC090685; BC045549; BC045624; BC051702 

Genbank Nucleotide ID

 BAA33370.1; AAC51775.2; BAH13725.1; BAH14780.1; AAH45549.1; AAH45624.1; AAH51702.1 

Protein Name

 Carboxypeptidase D 

Protein Synonyms/Alias

 Metallocarboxypeptidase D; gp180 

Gene Name

 CPD 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
531	TRLYSLGKSVESREL	ubiquitination	[1]
1356	RMMSTGSKKSLLSHE	ubiquitination	[2, 3]
1357	MMSTGSKKSLLSHEF	ubiquitination	[1]
1379	EETLYSSKH******	ubiquitination	[3, 4, 5, 6]

Reference

 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Proteomic snapshot of the EGF-induced ubiquitin network.
 Argenzio E, Bange T, Oldrini B, Bianchi F, Peesari R, Mari S, Di Fiore PP, Mann M, Polo S.
 Mol Syst Biol. 2011 Jan 18;7:462. [PMID: 21245847]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [5] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [6] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661] 

Functional Description

  

Sequence Annotation

 REGION 32 493 Carboxypeptidase-like 1.
 REGION 494 897 Carboxypeptidase-like 2.
 REGION 898 1299 Carboxypeptidase-like 3.
 MOTIF 162 164 Cell attachment site (Potential).
 ACT_SITE 350 350 Nucleophile 1 (By similarity).
 ACT_SITE 762 762 Nucleophile 2 (By similarity).
 METAL 139 139 Zinc 1 (By similarity).
 METAL 142 142 Zinc 1 (By similarity).
 METAL 257 257 Zinc 1 (By similarity).
 METAL 564 564 Zinc 2 (By similarity).
 METAL 567 567 Zinc 2 (By similarity).
 METAL 671 671 Zinc 2 (By similarity).
 MOD_RES 1358 1358 Phosphoserine.
 MOD_RES 1361 1361 Phosphoserine.
 MOD_RES 1368 1368 Phosphothreonine.
 MOD_RES 1370 1370 Phosphothreonine.
 LIPID 1317 1317 S-palmitoyl cysteine.
 LIPID 1321 1321 S-palmitoyl cysteine.
 LIPID 1323 1323 S-palmitoyl cysteine.
 CARBOHYD 172 172 N-linked (GlcNAc...).
 CARBOHYD 217 217 N-linked (GlcNAc...) (Potential).
 CARBOHYD 399 399 N-linked (GlcNAc...) (Potential).
 CARBOHYD 410 410 N-linked (GlcNAc...) (Potential).
 CARBOHYD 429 429 N-linked (GlcNAc...) (Potential).
 CARBOHYD 522 522 N-linked (GlcNAc...) (Potential).
 CARBOHYD 626 626 N-linked (GlcNAc...) (Potential).
 CARBOHYD 811 811 N-linked (GlcNAc...).
 CARBOHYD 855 855 N-linked (GlcNAc...) (Potential).
 CARBOHYD 867 867 N-linked (GlcNAc...) (Potential).
 CARBOHYD 879 879 N-linked (GlcNAc...) (Potential).
 CARBOHYD 955 955 N-linked (GlcNAc...).
 CARBOHYD 978 978 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1070 1070 N-linked (GlcNAc...).
 CARBOHYD 1142 1142 N-linked (GlcNAc...) (Potential).  

Keyword

 Alternative splicing; Carboxypeptidase; Complete proteome; Glycoprotein; Hydrolase; Lipoprotein; Membrane; Metal-binding; Metalloprotease; Palmitate; Phosphoprotein; Polymorphism; Protease; Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix; Zinc. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 1380 AA 

Protein Sequence

Gene Ontology

 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0016020; C:membrane; TAS:ProtInc.
 GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
 GO:0004185; F:serine-type carboxypeptidase activity; TAS:ProtInc.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW. 

Interpro

 IPR008969; CarboxyPept-like_regulatory.
 IPR014766; CarboxyPept_regulatory_dom.
 IPR015567; Pept_M14B_carboxypept_D2.
 IPR000834; Peptidase_M14. 

Pfam

 PF00246; Peptidase_M14 

SMART

 SM00631; Zn_pept 

PROSITE

 PS00132; CARBOXYPEPT_ZN_1
 PS00133; CARBOXYPEPT_ZN_2 

PRINTS

 PR00765; CRBOXYPTASEA.