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P08819

- CBP2_WHEAT

UniProt

P08819 - CBP2_WHEAT

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Protein

Serine carboxypeptidase 2

Gene

CBP2

Organism
Triticum aestivum (Wheat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

Preferential release of a C-terminal arginine or lysine residue.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei158 – 1581
Binding sitei251 – 2511Substrate
Active sitei361 – 3611
Active sitei413 – 4131
Binding sitei414 – 4141Substrate

GO - Molecular functioni

  1. serine-type carboxypeptidase activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Protease

Protein family/group databases

MEROPSiS10.005.

Names & Taxonomyi

Protein namesi
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:
Alternative name(s):
Serine carboxypeptidase II chain A
Alternative name(s):
Serine carboxypeptidase II chain B
Gene namesi
Name:CBP2
OrganismiTriticum aestivum (Wheat)
Taxonomic identifieri4565 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeTriticum
ProteomesiUP000019116: Unplaced

Organism-specific databases

GrameneiP08819.

Pathology & Biotechi

Allergenic propertiesi

Causes an allergic reaction in human. Binds to IgE.1 Publication

Keywords - Diseasei

Allergen

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 259259Serine carboxypeptidase 2 chain APRO_0000004312Add
BLAST
Propeptidei260 – 28627Linker peptidePRO_0000274569Add
BLAST
Chaini287 – 444158Serine carboxypeptidase 2 chain BPRO_0000004313Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi65 ↔ 324Interchain (between A and B chains)
Glycosylationi116 – 1161N-linked (GlcNAc...)
Glycosylationi127 – 1271N-linked (GlcNAc...)
Disulfide bondi222 ↔ 234
Disulfide bondi258 ↔ 291Interchain (between A and B chains)
Glycosylationi259 – 2591N-linked (GlcNAc...)
Glycosylationi312 – 3121N-linked (GlcNAc...)
Glycosylationi318 – 3181N-linked (GlcNAc...)

Post-translational modificationi

N-glycosylated.

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PRIDEiP08819.

Interactioni

Subunit structurei

Carboxypeptidase II is a dimer, where each monomer is composed of two chains linked by a disulfide bond.2 Publications

Structurei

Secondary structure

1
444
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni7 – 93
Beta strandi24 – 329
Turni33 – 364
Beta strandi37 – 448
Helixi48 – 503
Beta strandi55 – 595
Turni62 – 643
Turni67 – 704
Helixi71 – 744
Beta strandi75 – 817
Helixi83 – 853
Beta strandi88 – 903
Helixi95 – 973
Beta strandi99 – 1046
Beta strandi114 – 1174
Helixi118 – 1225
Helixi126 – 14318
Helixi145 – 1473
Beta strandi151 – 1588
Helixi160 – 17415
Beta strandi180 – 18910
Helixi193 – 20513
Turni206 – 2083
Helixi212 – 22211
Beta strandi227 – 2293
Helixi232 – 24514
Helixi292 – 30110
Helixi303 – 3086
Beta strandi312 – 3154
Helixi326 – 3305
Helixi340 – 3489
Beta strandi352 – 3587
Beta strandi362 – 3643
Helixi366 – 3749
Beta strandi380 – 38910
Beta strandi392 – 4009
Beta strandi403 – 4086
Helixi415 – 4184
Helixi420 – 43213

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BCRX-ray2.50A1-263[»]
B285-444[»]
1BCSX-ray2.08A1-263[»]
B285-444[»]
1WHSX-ray2.00A6-260[»]
B287-439[»]
1WHTX-ray2.00A5-260[»]
B287-439[»]
3SC2X-ray2.20A1-259[»]
B287-438[»]
ProteinModelPortaliP08819.
SMRiP08819. Positions 5-260, 287-439.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08819.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni51 – 533Substrate binding
Regioni157 – 1593Substrate binding

Sequence similaritiesi

Belongs to the peptidase S10 family.Curated

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR001563. Peptidase_S10.
IPR018202. Peptidase_S10_AS.
[Graphical view]
PANTHERiPTHR11802. PTHR11802. 1 hit.
PfamiPF00450. Peptidase_S10. 1 hit.
[Graphical view]
PRINTSiPR00724. CRBOXYPTASEC.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00560. CARBOXYPEPT_SER_HIS. 1 hit.
PS00131. CARBOXYPEPT_SER_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P08819-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
VEPSGHAADR IARLPGQPAV DFDMYSGYIT VDEGAGRSLF YLLQEAPEDA
60 70 80 90 100
QPAPLVLWLN GGPGCSSVAY GASEELGAFR VKPRGAGLVL NEYRWNKVAN
110 120 130 140 150
VLFLDSPAGV GFSYTNTSSD IYTSGDNRTA HDSYAFLAKW FERFPHYKYR
160 170 180 190 200
DFYIAGESYA GHYVPELSQL VHRSKNPVIN LKGFMVGNGL IDDYHDYVGT
210 220 230 240 250
FEFWWNHGIV SDDTYRRLKE ACLHDSFIHP SPACDAATDV ATAEQGNIDM
260 270 280 290 300
YSLYTPVCNI TSSSSSSSSS LSQQRRSRGR YPWLTGSYDP CTERYSTAYY
310 320 330 340 350
NRRDVQMALH ANVTGAMNYT WATCSDTINT HWHDAPRSML PIYRELIAAG
360 370 380 390 400
LRIWVFSGDT DAVVPLTATR YSIGALGLPT TTSWYPWYDD QEVGGWSQVY
410 420 430 440
KGLTLVSVRG AGHEVPLHRP RQALVLFQYF LQGKPMPGQT KNAT
Length:444
Mass (Da):49,506
Last modified:February 6, 2007 - v2
Checksum:i983B9BCC1C2DECB2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti209 – 2091I → L in CAI64396. (PubMed:2324088)Curated
Sequence conflicti216 – 2161R → Q in CAI64396. (PubMed:2324088)Curated
Sequence conflicti219 – 2191K → R in CAI64396. (PubMed:2324088)Curated
Sequence conflicti307 – 3071M → T in CAI64396. (PubMed:2324088)Curated
Sequence conflicti322 – 3221A → S in CAI64396. (PubMed:2324088)Curated
Sequence conflicti440 – 4412TK → AT in CAI64396. (PubMed:2324088)Curated
Sequence conflicti444 – 4441T → TVA in CAI64396. (PubMed:2324088)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1 – 33Missing in a' chain.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ890016 mRNA. Translation: CAI64396.1.
PIRiA29639.
UniGeneiTa.56555.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ890016 mRNA. Translation: CAI64396.1 .
PIRi A29639.
UniGenei Ta.56555.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P08819.
SMRi P08819. Positions 5-260, 287-439.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi S10.005.

Proteomic databases

PRIDEi P08819.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

Gramenei P08819.

Miscellaneous databases

EvolutionaryTracei P08819.

Family and domain databases

Gene3Di 3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR001563. Peptidase_S10.
IPR018202. Peptidase_S10_AS.
[Graphical view ]
PANTHERi PTHR11802. PTHR11802. 1 hit.
Pfami PF00450. Peptidase_S10. 1 hit.
[Graphical view ]
PRINTSi PR00724. CRBOXYPTASEC.
SUPFAMi SSF53474. SSF53474. 1 hit.
PROSITEi PS00560. CARBOXYPEPT_SER_HIS. 1 hit.
PS00131. CARBOXYPEPT_SER_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiCBP2_WHEAT
AccessioniPrimary (citable) accession number: P08819
Secondary accession number(s): Q4W1G1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: February 6, 2007
Last modified: October 1, 2014
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3