Reviewed, UniProtKB/Swiss-Prot Q2KIG3 (CBPB2_BOVIN)

Names and origin

Protein names

Recommended name:
    Carboxypeptidase B2
    EC=3.4.17.20

Gene names

Name:

CPB2

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	423 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)

Function	Cleaves C-terminal arginine or lysine residues from biologically active peptides such as kinins or anaphylatoxins in the circulation thereby regulating their activities By similarity.
Catalytic activity	Release of C-terminal Arg and Lys from a polypeptide.
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subcellular location	Secreted By similarity.
Sequence similarities	Belongs to the peptidase M14 family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Carboxypeptidase Hydrolase Metalloprotease Protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	3D-structure
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	metallocarboxypeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred 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 – 22

22

Potential

Propeptide

23 – 114

92

Activation peptide

PRO_0000282869

Chain

115 – 423

309

Carboxypeptidase B2

PRO_0000282870

Sites

Active site

385

1

Nucleophile By similarity

Metal binding

181

1

Zinc By similarity

Metal binding

184

1

Zinc By similarity

Metal binding

310

1

Zinc By similarity

Amino acid modifications

Glycosylation

44

1

N-linked (GlcNAc...) Potential

Glycosylation

73

1

N-linked (GlcNAc...) Potential

Glycosylation

85

1

N-linked (GlcNAc...) Potential

Glycosylation

108

1

N-linked (GlcNAc...) Potential

Glycosylation

241

1

N-linked (GlcNAc...) Potential

Disulfide bond

178 ↔ 191

By similarity

Disulfide bond

250 ↔ 274

By similarity

Disulfide bond

265 ↔ 279

By similarity

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

423

Helix Strand Turn

Details...

Helix

119 – 121

3

Helix

126 – 139

14

Turn

141 – 143

3

Beta strand

144 – 148

5

Beta strand

159 – 163

5

Beta strand

173 – 177

5

Helix

186 – 194

9

Turn

198 – 200

3

Beta strand

216 – 221

6

Helix

229 – 233

5

Helix

255 – 257

3

Turn

273 – 277

5

Helix

287 – 298

12

Turn

299 – 302

4

Beta strand

303 – 310

8

Beta strand

312 – 317

6

Helix

330 – 347

18

Helix

370 – 375

6

Beta strand

380 – 385

6

Helix

398 – 400

3

Helix

401 – 422

22

Sequences

	Sequence		Length	Mass (Da)
	Q2KIG3-1 [UniParc]. Last modified March 7, 2006. Version 1. Checksum: 361E7FE3F885080E	FASTA	423	48,822
	10 20 30 40 50 60 MKLYSLGVLV ATVLFCGEHA FAFQRGQVLS ALPRTSRQVQ ILQNVTTTYK IVLWQPVAAE 70 80 90 100 110 120 YIVKGYEVHF FVNASDVSNV KAHLNASRIP FRVLVENVED LIRQQTSNDT ISPRASSSYY 130 140 150 160 170 180 EQYHSLNEIY SWIEVMTERY PDMVEKIHIG SSYEKYPLYV LKVSKKEQRA KNAMWIDCGI 190 200 210 220 230 240 HAREWISPAF CLWFVGSVTY YYGKEKMHTN LLKHMDFYIM PVVNVDGYDY TWKKDRMWRK 250 260 270 280 290 300 NRSLHEKNAC VGTDLNRNFA SKHWCGEGAS SSSCSEIYCG TYPESEPEVK AVADFLRRNI 310 320 330 340 350 360 KHIKAYISMH SYSQKIVFPY SYSRSRSKDH EELSLVAREA VFAMENIHRN IRYTHGSGSE 370 380 390 400 410 420 SLYLAPGGSD DWIYDLGIKY SFTFELRDKG KYGFLLPESY IRPTCSEALV AVAKIASHVV KNV

References

[1]	NIH - Mammalian Gene Collection (MGC) project Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Testis.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

BC112649 mRNA. Translation: AAI12650.1.

IPI

IPI00685411.

RefSeq

NP_001039462.1.

UniGene

Bt.93764

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3D4U	X-ray	1.70	A	115-423	[»]
3DGV	X-ray	2.50	A/B/C	23-423	[»]

ModBase

Search...

Protein family/group databases

MEROPS

M14.009.

Genome annotation databases

Ensembl

ENSBTAT00000009300; ENSBTAP00000009300; ENSBTAG00000007073; Bos taurus. [Genome view]

GeneID

508222.

KEGG

bta:508222.

Organism-specific databases

CTD

508222.

Phylogenomic databases

HOVERGEN

Q2KIG3.

OMA

IGSSYEK.

Enzyme and pathway databases

BRENDA

3.4.17.20. 251.

Family and domain databases

InterPro

IPR000834. Peptidase_M14.
IPR003146. Prot_inh_M14A.
[Graphical view]

Pfam

PF00246. Peptidase_M14. 1 hit.
PF02244. Propep_M14. 1 hit.
[Graphical view]

PRINTS

PR00765. CRBOXYPTASEA.

SMART

SM00631. Zn_pept. 1 hit.
[Graphical view]

PROSITE

PS00132. CARBOXYPEPT_ZN_1. False negative.
PS00133. CARBOXYPEPT_ZN_2. False negative.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

CBPB2_BOVIN

Accession

Primary (citable) accession number: Q2KIG3

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 3, 2007
Last sequence update:	March 7, 2006
Last modified:	November 3, 2009
This is version 28 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)