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 23-FEB-2022, entry version 137. 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 (2.2 ANGSTROMS). 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 (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE 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 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: 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}. 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 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 SMR; P08819; -. DR STRING; 4565.Traes_1BS_FEA181281.1; -. DR ESTHER; wheat-cbp02; Carboxypeptidase_S10. 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 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 REGION 51..53 FT /note="Substrate binding" FT REGION 157..159 FT /note="Substrate binding" FT ACT_SITE 158 FT ACT_SITE 361 FT ACT_SITE 413 FT BINDING 251 FT /note="Substrate" FT BINDING 414 FT /note="Substrate" FT CARBOHYD 116 FT /note="N-linked (GlcNAc...) asparagine" FT CARBOHYD 127 FT /note="N-linked (GlcNAc...) asparagine" FT CARBOHYD 259 FT /note="N-linked (GlcNAc...) asparagine" FT CARBOHYD 312 FT /note="N-linked (GlcNAc...) asparagine" FT CARBOHYD 318 FT /note="N-linked (GlcNAc...) asparagine" FT DISULFID 65..324 FT /note="Interchain (between A and B chains)" FT DISULFID 222..234 FT DISULFID 258..291 FT /note="Interchain (between A and B chains)" 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 //