CBP2_WHEAT
ID CBP2_WHEAT Reviewed; 444 AA.
AC P08819; Q4W1G1;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Serine carboxypeptidase 2;
DE EC=3.4.16.6;
DE AltName: Full=CPDW-II;
DE Short=CP-WII;
DE AltName: Full=Carboxypeptidase D;
DE AltName: Full=Serine carboxypeptidase II;
DE Contains:
DE RecName: Full=Serine carboxypeptidase 2 chain A;
DE AltName: Full=Serine carboxypeptidase II chain A;
DE Contains:
DE RecName: Full=Serine carboxypeptidase 2 chain B;
DE AltName: Full=Serine carboxypeptidase II chain B;
DE Flags: Precursor;
GN Name=CBP2;
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP PROTEIN SEQUENCE OF 1-263 AND 285-444.
RA Breddam K., Soerensen S.B., Svendsen I.;
RT "Primary structure and enzymatic properties of carboxypeptidase II from
RT wheat bran.";
RL Carlsberg Res. Commun. 52:297-311(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 187-444, AND ALLERGEN.
RC STRAIN=cv. Wyuna; TISSUE=Endosperm;
RX PubMed=16364168; DOI=10.1111/j.1398-9995.2006.00999.x;
RA Weichel M., Vergoossen N.J., Bonomi S., Scibilia J., Ortolani C.,
RA Ballmer-Weber B.K., Pastorello E.A., Crameri R.;
RT "Screening the allergenic repertoires of wheat and maize with sera from
RT double-blind, placebo-controlled food challenge positive patients.";
RL Allergy 61:128-135(2006).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
RX PubMed=2324088; DOI=10.2210/pdb2sc2/pdb;
RA Liao D.-I., Remington S.J.;
RT "Structure of wheat serine carboxypeptidase II at 3.5-A resolution. A new
RT class of serine proteinase.";
RL J. Biol. Chem. 265:6528-6531(1990).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1-259 AND 287-438, GLYCOSYLATION
RP AT ASN-116; ASN-127 AND ASN-312, AND DISULFIDE BONDS.
RX PubMed=1390755; DOI=10.1021/bi00155a037;
RA Liao D.-I., Breddam K., Sweet R.M., Bullock T., Remington S.J.;
RT "Refined atomic model of wheat serine carboxypeptidase II at 2.2-A
RT resolution.";
RL Biochemistry 31:9796-9812(1992).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 6-260 AND 287-439 IN COMPLEX WITH
RP SUBSTRATE ANALOG, GLYCOSYLATION AT ASN-116; ASN-127 AND ASN-312, AND
RP DISULFIDE BONDS.
RX PubMed=7727364; DOI=10.1021/bi00203a009;
RA Bullock T.L., Branchaud B., Remington S.J.;
RT "Structure of the complex of L-benzylsuccinate with wheat serine
RT carboxypeptidase II at 2.0-A resolution.";
RL Biochemistry 33:11127-11134(1994).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 1-263 AND 285-444 IN COMPLEX WITH
RP SUBSTRATE ANALOGS, GLYCOSYLATION AT ASN-116; ASN-127 AND ASN-312, AND
RP DISULFIDE BONDS.
RX PubMed=8636973; DOI=10.1006/jmbi.1996.0058;
RA Bullock T.L., Breddam K., Remington S.J.;
RT "Peptide aldehyde complexes with wheat serine carboxypeptidase II:
RT implications for the catalytic mechanism and substrate specificity.";
RL J. Mol. Biol. 255:714-725(1996).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential release of a C-terminal arginine or lysine
CC residue.; EC=3.4.16.6;
CC -!- SUBUNIT: Carboxypeptidase II is a dimer, where each monomer is composed
CC of two chains linked by a disulfide bond. {ECO:0000269|PubMed:7727364,
CC ECO:0000269|PubMed:8636973}.
CC -!- PTM: N-glycosylated.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE.
CC {ECO:0000269|PubMed:16364168}.
CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR EMBL; AJ890016; CAI64396.1; -; mRNA.
DR PIR; A29639; A29639.
DR PDB; 1BCR; X-ray; 2.50 A; A=1-263, B=285-444.
DR PDB; 1BCS; X-ray; 2.08 A; A=1-263, B=285-444.
DR PDB; 1WHS; X-ray; 2.00 A; A=6-260, B=287-439.
DR PDB; 1WHT; X-ray; 2.00 A; A=5-260, B=287-439.
DR PDB; 3SC2; X-ray; 2.20 A; A=1-259, B=287-438.
DR PDBsum; 1BCR; -.
DR PDBsum; 1BCS; -.
DR PDBsum; 1WHS; -.
DR PDBsum; 1WHT; -.
DR PDBsum; 3SC2; -.
DR AlphaFoldDB; P08819; -.
DR SMR; P08819; -.
DR STRING; 4565.Traes_1BS_FEA181281.1; -.
DR ESTHER; wheat-cbp02; Carboxypeptidase_S10.
DR MEROPS; S10.005; -.
DR MEROPS; S10.A43; -.
DR PRIDE; P08819; -.
DR eggNOG; KOG1282; Eukaryota.
DR EvolutionaryTrace; P08819; -.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; P08819; baseline and differential.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001563; Peptidase_S10.
DR InterPro; IPR033124; Ser_caboxypep_his_AS.
DR InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR PANTHER; PTHR11802; PTHR11802; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR PRINTS; PR00724; CRBOXYPTASEC.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1.
DR PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allergen; Carboxypeptidase; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW Zymogen.
FT CHAIN 1..259
FT /note="Serine carboxypeptidase 2 chain A"
FT /id="PRO_0000004312"
FT PROPEP 260..286
FT /note="Linker peptide"
FT /id="PRO_0000274569"
FT CHAIN 287..444
FT /note="Serine carboxypeptidase 2 chain B"
FT /id="PRO_0000004313"
FT ACT_SITE 158
FT /evidence="ECO:0000269|PubMed:8636973,
FT ECO:0007744|PDB:1BCR"
FT ACT_SITE 361
FT /evidence="ECO:0000269|PubMed:8636973,
FT ECO:0007744|PDB:1BCR"
FT ACT_SITE 413
FT /evidence="ECO:0000269|PubMed:8636973,
FT ECO:0007744|PDB:1BCR"
FT BINDING 60..62
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:7727364,
FT ECO:0000269|PubMed:8636973, ECO:0007744|PDB:1BCR,
FT ECO:0007744|PDB:1BCS, ECO:0007744|PDB:1WHS,
FT ECO:0007744|PDB:1WHT"
FT BINDING 157..159
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:7727364,
FT ECO:0000269|PubMed:8636973, ECO:0007744|PDB:1BCR,
FT ECO:0007744|PDB:1BCS, ECO:0007744|PDB:1WHS,
FT ECO:0007744|PDB:1WHT"
FT BINDING 409..413
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:7727364,
FT ECO:0007744|PDB:1WHT"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:1390755, ECO:0000269|PubMed:7727364,
FT ECO:0000269|PubMed:8636973, ECO:0007744|PDB:1BCR,
FT ECO:0007744|PDB:1WHT, ECO:0007744|PDB:3SC2"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:1390755, ECO:0000269|PubMed:7727364,
FT ECO:0000269|PubMed:8636973, ECO:0007744|PDB:1BCR,
FT ECO:0007744|PDB:1WHT, ECO:0007744|PDB:3SC2"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:1390755, ECO:0000269|PubMed:7727364,
FT ECO:0000269|PubMed:8636973, ECO:0007744|PDB:1BCR,
FT ECO:0007744|PDB:1WHT, ECO:0007744|PDB:3SC2"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 65..324
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000269|PubMed:1390755,
FT ECO:0000269|PubMed:7727364, ECO:0000269|PubMed:8636973,
FT ECO:0007744|PDB:1BCR, ECO:0007744|PDB:1BCS,
FT ECO:0007744|PDB:1WHS, ECO:0007744|PDB:1WHT,
FT ECO:0007744|PDB:3SC2"
FT DISULFID 222..234
FT /evidence="ECO:0000269|PubMed:1390755,
FT ECO:0000269|PubMed:7727364, ECO:0000269|PubMed:8636973,
FT ECO:0007744|PDB:1BCR, ECO:0007744|PDB:1BCS,
FT ECO:0007744|PDB:1WHS, ECO:0007744|PDB:1WHT,
FT ECO:0007744|PDB:3SC2"
FT DISULFID 258..291
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000269|PubMed:1390755,
FT ECO:0000269|PubMed:7727364, ECO:0000269|PubMed:8636973,
FT ECO:0007744|PDB:1BCR, ECO:0007744|PDB:1BCS,
FT ECO:0007744|PDB:1WHS, ECO:0007744|PDB:1WHT,
FT ECO:0007744|PDB:3SC2"
FT VARIANT 1..3
FT /note="Missing (in a' chain)"
FT CONFLICT 209
FT /note="I -> L (in Ref. 3; CAI64396)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="R -> Q (in Ref. 3; CAI64396)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="K -> R (in Ref. 3; CAI64396)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="M -> T (in Ref. 3; CAI64396)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="A -> S (in Ref. 3; CAI64396)"
FT /evidence="ECO:0000305"
FT CONFLICT 440..441
FT /note="TK -> AT (in Ref. 3; CAI64396)"
FT /evidence="ECO:0000305"
FT CONFLICT 444
FT /note="T -> TVA (in Ref. 3; CAI64396)"
FT /evidence="ECO:0000305"
FT TURN 7..9
FT /evidence="ECO:0007829|PDB:1WHS"
FT STRAND 24..32
FT /evidence="ECO:0007829|PDB:1WHS"
FT TURN 33..36
FT /evidence="ECO:0007829|PDB:1WHS"
FT STRAND 37..44
FT /evidence="ECO:0007829|PDB:1WHS"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:1WHS"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:1WHS"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:1WHS"
FT TURN 67..70
FT /evidence="ECO:0007829|PDB:1WHS"
FT HELIX 71..74
FT /evidence="ECO:0007829|PDB:1WHS"
FT STRAND 75..81
FT /evidence="ECO:0007829|PDB:1WHS"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:1WHS"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:1WHS"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:1WHS"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:1WHS"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:1WHS"
FT HELIX 118..122
FT /evidence="ECO:0007829|PDB:1WHS"
FT HELIX 126..143
FT /evidence="ECO:0007829|PDB:1WHS"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:1WHS"
FT STRAND 151..158
FT /evidence="ECO:0007829|PDB:1WHS"
FT HELIX 160..174
FT /evidence="ECO:0007829|PDB:1WHS"
FT STRAND 180..189
FT /evidence="ECO:0007829|PDB:1WHS"
FT HELIX 193..205
FT /evidence="ECO:0007829|PDB:1WHS"
FT TURN 206..208
FT /evidence="ECO:0007829|PDB:1WHS"
FT HELIX 212..222
FT /evidence="ECO:0007829|PDB:1WHS"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:1WHS"
FT HELIX 232..245
FT /evidence="ECO:0007829|PDB:1WHS"
FT HELIX 292..301
FT /evidence="ECO:0007829|PDB:1WHS"
FT HELIX 303..308
FT /evidence="ECO:0007829|PDB:1WHS"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:1BCR"
FT HELIX 326..330
FT /evidence="ECO:0007829|PDB:1WHS"
FT HELIX 340..348
FT /evidence="ECO:0007829|PDB:1WHS"
FT STRAND 352..358
FT /evidence="ECO:0007829|PDB:1WHS"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:1WHS"
FT HELIX 366..374
FT /evidence="ECO:0007829|PDB:1WHS"
FT STRAND 380..389
FT /evidence="ECO:0007829|PDB:1WHS"
FT STRAND 392..400
FT /evidence="ECO:0007829|PDB:1WHS"
FT STRAND 403..408
FT /evidence="ECO:0007829|PDB:1WHS"
FT HELIX 415..418
FT /evidence="ECO:0007829|PDB:1WHS"
FT HELIX 420..432
FT /evidence="ECO:0007829|PDB:1WHS"
SQ SEQUENCE 444 AA; 49506 MW; 983B9BCC1C2DECB2 CRC64;
VEPSGHAADR IARLPGQPAV DFDMYSGYIT VDEGAGRSLF YLLQEAPEDA QPAPLVLWLN
GGPGCSSVAY GASEELGAFR VKPRGAGLVL NEYRWNKVAN VLFLDSPAGV GFSYTNTSSD
IYTSGDNRTA HDSYAFLAKW FERFPHYKYR DFYIAGESYA GHYVPELSQL VHRSKNPVIN
LKGFMVGNGL IDDYHDYVGT FEFWWNHGIV SDDTYRRLKE ACLHDSFIHP SPACDAATDV
ATAEQGNIDM YSLYTPVCNI TSSSSSSSSS LSQQRRSRGR YPWLTGSYDP CTERYSTAYY
NRRDVQMALH ANVTGAMNYT WATCSDTINT HWHDAPRSML PIYRELIAAG LRIWVFSGDT
DAVVPLTATR YSIGALGLPT TTSWYPWYDD QEVGGWSQVY KGLTLVSVRG AGHEVPLHRP
RQALVLFQYF LQGKPMPGQT KNAT
