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 10-JUL-2007, entry version 75. DE Serine carboxypeptidase 2 precursor (EC 3.4.16.6) (Serine DE carboxypeptidase II) (Carboxypeptidase D) (CPDW-II) (CP-WII) DE [Contains: Serine carboxypeptidase 2 chain A (Serine carboxypeptidase DE II chain A); Serine carboxypeptidase 2 chain B (Serine DE carboxypeptidase II chain B)]. GN Name=CBP2; OS Triticum aestivum (Wheat). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade; OC Pooideae; Triticeae; 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 RT from wheat bran."; RL Carlsberg Res. Commun. 52:297-311(1987). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 187-444, AND ALLERGENIC PROPERTIES. 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 RT from double-blind, placebo-controlled food challenge positive RT patients."; RL Allergy 61:128-135(2006). RN [3] RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS). RX MEDLINE=90216664; PubMed=2324088; RA Liao D.-I., Remington S.J.; RT "Structure of wheat serine carboxypeptidase II at 3.5-A resolution. A RT new class of serine proteinase."; RL J. Biol. Chem. 265:6528-6531(1990). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). RX MEDLINE=93003139; 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 (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE RP ANALOG. 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 (2.1 ANGSTROMS) IN COMPLEX WITH SUBSTRATE RP ANALOGS. 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: Preferential release of a C-terminal arginine CC or lysine residue. CC -!- SUBUNIT: Carboxypeptidase II is a dimer, where each monomer is CC composed of two chains linked by a disulfide bond. CC -!- PTM: N-glycosylated. CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE. CC -!- SIMILARITY: Belongs to the peptidase S10 family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ890016; CAI64396.1; -; mRNA. DR PIR; A29639; A29639. DR UniGene; Ta.4208; -. DR PDB; 1BCR; X-ray; A=1-263, B=285-444. DR PDB; 1BCS; X-ray; A=1-263, B=285-444. DR PDB; 1WHS; X-ray; A=6-260, B=287-439. DR PDB; 1WHT; X-ray; A=5-260, B=287-439. DR PDB; 3SC2; X-ray; A=1-259, B=287-438. DR MEROPS; S10.005; -. DR Gramene; P08819; -. DR LinkHub; P08819; -. DR GO; GO:0004187; F:carboxypeptidase D activity; IEA:EC. DR InterPro; IPR001563; Peptidase_S10. DR Pfam; PF00450; Peptidase_S10; 1. DR PRINTS; PR00724; CRBOXYPTASEC. DR PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1. DR PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1. KW 3D-structure; Allergen; Carboxypeptidase; Direct protein sequencing; KW Glycoprotein; Hydrolase; Protease; Zymogen. FT CHAIN 1 259 Serine carboxypeptidase 2 chain A. FT /FTId=PRO_0000004312. FT PROPEP 260 286 Linker peptide. FT /FTId=PRO_0000274569. FT CHAIN 287 444 Serine carboxypeptidase 2 chain B. FT /FTId=PRO_0000004313. FT REGION 51 53 Substrate binding. FT REGION 157 159 Substrate binding. FT ACT_SITE 158 158 FT ACT_SITE 361 361 FT ACT_SITE 413 413 FT BINDING 251 251 Substrate. FT BINDING 414 414 Substrate. FT CARBOHYD 116 116 N-linked (GlcNAc...). FT CARBOHYD 127 127 N-linked (GlcNAc...). FT CARBOHYD 259 259 N-linked (GlcNAc...). FT CARBOHYD 312 312 N-linked (GlcNAc...). FT CARBOHYD 318 318 N-linked (GlcNAc...). FT DISULFID 65 324 Interchain (between A and B chains). FT DISULFID 222 234 FT DISULFID 258 291 Interchain (between A and B chains). FT VARIANT 1 3 Missing (in a' chain). FT CONFLICT 209 209 I -> L (in Ref. 3; CAI64396). FT CONFLICT 216 216 R -> Q (in Ref. 3; CAI64396). FT CONFLICT 219 219 K -> R (in Ref. 3; CAI64396). FT CONFLICT 307 307 M -> T (in Ref. 3; CAI64396). FT CONFLICT 322 322 A -> S (in Ref. 3; CAI64396). FT CONFLICT 440 441 TK -> AT (in Ref. 3; CAI64396). FT CONFLICT 444 444 T -> TVA (in Ref. 3; CAI64396). FT STRAND 24 32 FT TURN 33 36 FT STRAND 37 44 FT HELIX 48 50 FT STRAND 55 59 FT TURN 62 64 FT TURN 67 70 FT HELIX 71 74 FT STRAND 75 81 FT HELIX 83 85 FT STRAND 88 90 FT HELIX 95 97 FT STRAND 99 104 FT STRAND 114 117 FT HELIX 118 122 FT HELIX 126 143 FT HELIX 145 147 FT STRAND 151 158 FT HELIX 160 174 FT STRAND 180 189 FT HELIX 193 205 FT TURN 206 208 FT HELIX 212 222 FT STRAND 227 229 FT HELIX 232 245 FT HELIX 271 279 FT HELIX 282 288 FT HELIX 305 309 FT HELIX 319 327 FT STRAND 331 337 FT STRAND 341 343 FT HELIX 345 353 FT STRAND 359 368 FT STRAND 371 379 FT STRAND 382 387 FT HELIX 394 397 FT HELIX 399 411 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 //