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P08819

- CBP2_WHEAT

UniProt

P08819 - CBP2_WHEAT

Protein

Serine carboxypeptidase 2

Gene

CBP2

Organism
Triticum aestivum (Wheat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 2 (06 Feb 2007)
      Previous versions | rss
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    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

    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

    VEPSGHAADR IARLPGQPAV DFDMYSGYIT VDEGAGRSLF YLLQEAPEDA    50
    QPAPLVLWLN GGPGCSSVAY GASEELGAFR VKPRGAGLVL NEYRWNKVAN 100
    VLFLDSPAGV GFSYTNTSSD IYTSGDNRTA HDSYAFLAKW FERFPHYKYR 150
    DFYIAGESYA GHYVPELSQL VHRSKNPVIN LKGFMVGNGL IDDYHDYVGT 200
    FEFWWNHGIV SDDTYRRLKE ACLHDSFIHP SPACDAATDV ATAEQGNIDM 250
    YSLYTPVCNI TSSSSSSSSS LSQQRRSRGR YPWLTGSYDP CTERYSTAYY 300
    NRRDVQMALH ANVTGAMNYT WATCSDTINT HWHDAPRSML PIYRELIAAG 350
    LRIWVFSGDT DAVVPLTATR YSIGALGLPT TTSWYPWYDD QEVGGWSQVY 400
    KGLTLVSVRG AGHEVPLHRP RQALVLFQYF LQGKPMPGQT KNAT 444
    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