P08819 (CBP2_WHEAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine carboxypeptidase 2
EC=3.4.16.6

Alternative name(s):
CPDW-II
Short name=CP-WII
Carboxypeptidase D
Serine carboxypeptidase II

Cleaved into the following 2 chains:

1. Serine carboxypeptidase 2 chain A
   Alternative name(s):
   Serine carboxypeptidase II chain A
2. Serine carboxypeptidase 2 chain B
   Alternative name(s):
   Serine carboxypeptidase II chain B

Gene names

Name:

CBP2

Organism

Triticum aestivum (Wheat)

Taxonomic identifier

4565 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › Liliopsida › commelinids › Poales › Poaceae › BEP clade › Pooideae › Triticeae › Triticum

Protein attributes

Sequence length	444 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	Preferential release of a C-terminal arginine or lysine residue.
Subunit structure	Carboxypeptidase II is a dimer, where each monomer is composed of two chains linked by a disulfide bond.
Post-translational modification	N-glycosylated.
Allergenic properties	Causes an allergic reaction in human. Binds to IgE. Ref.2
Sequence similarities	Belongs to the peptidase S10 family.

Ontologies

Keywords
Disease	Allergen
Molecular function	Carboxypeptidase Hydrolase Protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	serine-type carboxypeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 259

259

Serine carboxypeptidase 2 chain A

PRO_0000004312

Propeptide

260 – 286

27

Linker peptide

PRO_0000274569

Chain

287 – 444

158

Serine carboxypeptidase 2 chain B

PRO_0000004313

Regions

Region

51 – 53

3

Substrate binding

Region

157 – 159

3

Substrate binding

Sites

Active site

158

1

Active site

361

1

Active site

413

1

Binding site

251

1

Substrate

Binding site

414

1

Substrate

Amino acid modifications

Glycosylation

116

1

N-linked (GlcNAc...)

Glycosylation

127

1

N-linked (GlcNAc...)

Glycosylation

259

1

N-linked (GlcNAc...)

Glycosylation

312

1

N-linked (GlcNAc...)

Glycosylation

318

1

N-linked (GlcNAc...)

Disulfide bond

65 ↔ 324

Interchain (between A and B chains)

Disulfide bond

222 ↔ 234

Disulfide bond

258 ↔ 291

Interchain (between A and B chains)

Natural variations

Natural variant

1 – 3

3

Missing in a' chain.

Experimental info

Sequence conflict

209

1

I → L in CAI64396. Ref.3

Sequence conflict

216

1

R → Q in CAI64396. Ref.3

Sequence conflict

219

1

K → R in CAI64396. Ref.3

Sequence conflict

307

1

M → T in CAI64396. Ref.3

Sequence conflict

322

1

A → S in CAI64396. Ref.3

Sequence conflict

440 – 441

2

TK → AT in CAI64396. Ref.3

Sequence conflict

444

1

T → TVA in CAI64396. Ref.3

Secondary structure

1

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444

Helix Strand Turn

Details...

Beta strand

24 – 32

9

Turn

33 – 36

4

Beta strand

37 – 44

8

Helix

48 – 50

3

Beta strand

55 – 59

5

Turn

62 – 64

3

Turn

67 – 70

4

Helix

71 – 74

4

Beta strand

75 – 81

7

Helix

83 – 85

3

Beta strand

88 – 90

3

Helix

95 – 97

3

Beta strand

99 – 104

6

Beta strand

114 – 117

4

Helix

118 – 122

5

Helix

126 – 143

18

Helix

145 – 147

3

Beta strand

151 – 158

8

Helix

160 – 174

15

Beta strand

180 – 189

10

Helix

193 – 205

13

Turn

206 – 208

3

Helix

212 – 222

11

Beta strand

227 – 229

3

Helix

232 – 245

14

Helix

292 – 300

9

Helix

303 – 309

7

Helix

326 – 330

5

Helix

340 – 348

9

Beta strand

352 – 358

7

Beta strand

362 – 364

3

Helix

366 – 374

9

Beta strand

380 – 389

10

Beta strand

392 – 400

9

Beta strand

403 – 408

6

Helix

415 – 418

4

Helix

420 – 432

13

Sequences

	Sequence		Length	Mass (Da)
	P08819 [UniParc]. Last modified February 6, 2007. Version 2. Checksum: 983B9BCC1C2DECB2	FASTA	444	49,506
	10 20 30 40 50 60 VEPSGHAADR IARLPGQPAV DFDMYSGYIT VDEGAGRSLF YLLQEAPEDA QPAPLVLWLN 70 80 90 100 110 120 GGPGCSSVAY GASEELGAFR VKPRGAGLVL NEYRWNKVAN VLFLDSPAGV GFSYTNTSSD 130 140 150 160 170 180 IYTSGDNRTA HDSYAFLAKW FERFPHYKYR DFYIAGESYA GHYVPELSQL VHRSKNPVIN 190 200 210 220 230 240 LKGFMVGNGL IDDYHDYVGT FEFWWNHGIV SDDTYRRLKE ACLHDSFIHP SPACDAATDV 250 260 270 280 290 300 ATAEQGNIDM YSLYTPVCNI TSSSSSSSSS LSQQRRSRGR YPWLTGSYDP CTERYSTAYY 310 320 330 340 350 360 NRRDVQMALH ANVTGAMNYT WATCSDTINT HWHDAPRSML PIYRELIAAG LRIWVFSGDT 370 380 390 400 410 420 DAVVPLTATR YSIGALGLPT TTSWYPWYDD QEVGGWSQVY KGLTLVSVRG AGHEVPLHRP 430 440 RQALVLFQYF LQGKPMPGQT KNAT

References

[1]	"Primary structure and enzymatic properties of carboxypeptidase II from wheat bran." Breddam K., Soerensen S.B., Svendsen I. Carlsberg Res. Commun. 52:297-311(1987) Cited for: PROTEIN SEQUENCE OF 1-263 AND 285-444.
[2]	"Screening the allergenic repertoires of wheat and maize with sera from double-blind, placebo-controlled food challenge positive patients." Weichel M., Vergoossen N.J., Bonomi S., Scibilia J., Ortolani C., Ballmer-Weber B.K., Pastorello E.A., Crameri R. Allergy 61:128-135(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 187-444, ALLERGEN. Strain: cv. Wyuna. Tissue: Endosperm.
[3]	"Structure of wheat serine carboxypeptidase II at 3.5-A resolution. A new class of serine proteinase." Liao D.-I., Remington S.J. J. Biol. Chem. 265:6528-6531(1990) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
[4]	"Refined atomic model of wheat serine carboxypeptidase II at 2.2-A resolution." Liao D.-I., Breddam K., Sweet R.M., Bullock T., Remington S.J. Biochemistry 31:9796-9812(1992) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[5]	"Structure of the complex of L-benzylsuccinate with wheat serine carboxypeptidase II at 2.0-A resolution." Bullock T.L., Branchaud B., Remington S.J. Biochemistry 33:11127-11134(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG.
[6]	"Peptide aldehyde complexes with wheat serine carboxypeptidase II: implications for the catalytic mechanism and substrate specificity." Bullock T.L., Breddam K., Remington S.J. J. Mol. Biol. 255:714-725(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ890016 mRNA. Translation: CAI64396.1.

PIR

A29639.

UniGene

Ta.56555.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BCR	X-ray	2.50	A	1-263	[»]
			B	285-444	[»]
1BCS	X-ray	2.08	A	1-263	[»]
			B	285-444	[»]
1WHS	X-ray	2.00	A	6-260	[»]
			B	287-439	[»]
1WHT	X-ray	2.00	A	5-260	[»]
			B	287-439	[»]
3SC2	X-ray	2.20	A	1-259	[»]
			B	287-438	[»]

ProteinModelPortal

P08819.

SMR

P08819. Positions 5-260, 287-439.

ModBase

Search...

Protein family/group databases

MEROPS

S10.005.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

KEGG

dosa:Os05t0268500-01.

Organism-specific databases

Gramene

P08819.

Family and domain databases

InterPro

IPR001563. Peptidase_S10.
IPR018202. Peptidase_S10_AS.
[Graphical view]

PANTHER

PTHR11802. PTHR11802. 1 hit.

Pfam

PF00450. Peptidase_S10. 1 hit.
[Graphical view]

PRINTS

PR00724. CRBOXYPTASEC.

PROSITE

PS00560. CARBOXYPEPT_SER_HIS. 1 hit.
PS00131. CARBOXYPEPT_SER_SER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P08819.

Entry information

Entry name

CBP2_WHEAT

Accession

Primary (citable) accession number: P08819
Secondary accession number(s): Q4W1G1

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	February 6, 2007
Last modified:	April 3, 2013
This is version 99 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program