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Serine carboxypeptidase 2 (EC 3.4.16.6) (CPDW-II) (CP-WII) (Carboxypeptidase D) (Serine carboxypeptidase II) [Cleaved into: Serine carboxypeptidase 2 chain A (Serine carboxypeptidase II chain A); Serine carboxypeptidase 2 chain B (Serine carboxypeptidase II chain B)]

 CBP2_WHEAT              Reviewed;         444 AA.
P08819; Q4W1G1;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
06-FEB-2007, sequence version 2.
10-MAY-2017, entry version 123.
RecName: Full=Serine carboxypeptidase 2;
EC=3.4.16.6;
AltName: Full=CPDW-II;
Short=CP-WII;
AltName: Full=Carboxypeptidase D;
AltName: Full=Serine carboxypeptidase II;
Contains:
RecName: Full=Serine carboxypeptidase 2 chain A;
AltName: Full=Serine carboxypeptidase II chain A;
Contains:
RecName: Full=Serine carboxypeptidase 2 chain B;
AltName: Full=Serine carboxypeptidase II chain B;
Flags: Precursor;
Name=CBP2;
Triticum aestivum (Wheat).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade;
Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
NCBI_TaxID=4565;
[1]
PROTEIN SEQUENCE OF 1-263 AND 285-444.
Breddam K., Soerensen S.B., Svendsen I.;
"Primary structure and enzymatic properties of carboxypeptidase II
from wheat bran.";
Carlsberg Res. Commun. 52:297-311(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 187-444, AND ALLERGEN.
STRAIN=cv. Wyuna; TISSUE=Endosperm;
PubMed=16364168; DOI=10.1111/j.1398-9995.2006.00999.x;
Weichel M., Vergoossen N.J., Bonomi S., Scibilia J., Ortolani C.,
Ballmer-Weber B.K., Pastorello E.A., Crameri R.;
"Screening the allergenic repertoires of wheat and maize with sera
from double-blind, placebo-controlled food challenge positive
patients.";
Allergy 61:128-135(2006).
[3]
X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
PubMed=2324088;
Liao D.-I., Remington S.J.;
"Structure of wheat serine carboxypeptidase II at 3.5-A resolution. A
new class of serine proteinase.";
J. Biol. Chem. 265:6528-6531(1990).
[4]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
PubMed=1390755; DOI=10.1021/bi00155a037;
Liao D.-I., Breddam K., Sweet R.M., Bullock T., Remington S.J.;
"Refined atomic model of wheat serine carboxypeptidase II at 2.2-A
resolution.";
Biochemistry 31:9796-9812(1992).
[5]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE
ANALOG.
PubMed=7727364; DOI=10.1021/bi00203a009;
Bullock T.L., Branchaud B., Remington S.J.;
"Structure of the complex of L-benzylsuccinate with wheat serine
carboxypeptidase II at 2.0-A resolution.";
Biochemistry 33:11127-11134(1994).
[6]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH SUBSTRATE
ANALOGS.
PubMed=8636973; DOI=10.1006/jmbi.1996.0058;
Bullock T.L., Breddam K., Remington S.J.;
"Peptide aldehyde complexes with wheat serine carboxypeptidase II:
implications for the catalytic mechanism and substrate specificity.";
J. Mol. Biol. 255:714-725(1996).
-!- CATALYTIC ACTIVITY: Preferential release of a C-terminal arginine
or lysine residue.
-!- SUBUNIT: Carboxypeptidase II is a dimer, where each monomer is
composed of two chains linked by a disulfide bond.
{ECO:0000269|PubMed:7727364, ECO:0000269|PubMed:8636973}.
-!- PTM: N-glycosylated.
-!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE.
{ECO:0000269|PubMed:16364168}.
-!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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EMBL; AJ890016; CAI64396.1; -; mRNA.
PIR; A29639; A29639.
UniGene; Ta.56555; -.
PDB; 1BCR; X-ray; 2.50 A; A=1-263, B=285-444.
PDB; 1BCS; X-ray; 2.08 A; A=1-263, B=285-444.
PDB; 1WHS; X-ray; 2.00 A; A=6-260, B=287-439.
PDB; 1WHT; X-ray; 2.00 A; A=5-260, B=287-439.
PDB; 3SC2; X-ray; 2.20 A; A=1-259, B=287-438.
PDBsum; 1BCR; -.
PDBsum; 1BCS; -.
PDBsum; 1WHS; -.
PDBsum; 1WHT; -.
PDBsum; 3SC2; -.
ProteinModelPortal; P08819; -.
SMR; P08819; -.
ESTHER; wheat-cbp02; Carboxypeptidase_S10.
MEROPS; S10.A43; -.
PRIDE; P08819; -.
EvolutionaryTrace; P08819; -.
Proteomes; UP000019116; Unplaced.
GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR001563; Peptidase_S10.
InterPro; IPR033124; Ser_caboxypep_his_AS.
InterPro; IPR018202; Ser_caboxypep_ser_AS.
PANTHER; PTHR11802; PTHR11802; 1.
Pfam; PF00450; Peptidase_S10; 1.
PRINTS; PR00724; CRBOXYPTASEC.
SUPFAM; SSF53474; SSF53474; 1.
PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1.
PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
1: Evidence at protein level;
3D-structure; Allergen; Carboxypeptidase; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
Protease; Reference proteome; Zymogen.
CHAIN 1 259 Serine carboxypeptidase 2 chain A.
/FTId=PRO_0000004312.
PROPEP 260 286 Linker peptide.
/FTId=PRO_0000274569.
CHAIN 287 444 Serine carboxypeptidase 2 chain B.
/FTId=PRO_0000004313.
REGION 51 53 Substrate binding.
REGION 157 159 Substrate binding.
ACT_SITE 158 158
ACT_SITE 361 361
ACT_SITE 413 413
BINDING 251 251 Substrate.
BINDING 414 414 Substrate.
CARBOHYD 116 116 N-linked (GlcNAc...) asparagine.
CARBOHYD 127 127 N-linked (GlcNAc...) asparagine.
CARBOHYD 259 259 N-linked (GlcNAc...) asparagine.
CARBOHYD 312 312 N-linked (GlcNAc...) asparagine.
CARBOHYD 318 318 N-linked (GlcNAc...) asparagine.
DISULFID 65 324 Interchain (between A and B chains).
DISULFID 222 234
DISULFID 258 291 Interchain (between A and B chains).
VARIANT 1 3 Missing (in a' chain).
CONFLICT 209 209 I -> L (in Ref. 3; CAI64396).
{ECO:0000305}.
CONFLICT 216 216 R -> Q (in Ref. 3; CAI64396).
{ECO:0000305}.
CONFLICT 219 219 K -> R (in Ref. 3; CAI64396).
{ECO:0000305}.
CONFLICT 307 307 M -> T (in Ref. 3; CAI64396).
{ECO:0000305}.
CONFLICT 322 322 A -> S (in Ref. 3; CAI64396).
{ECO:0000305}.
CONFLICT 440 441 TK -> AT (in Ref. 3; CAI64396).
{ECO:0000305}.
CONFLICT 444 444 T -> TVA (in Ref. 3; CAI64396).
{ECO:0000305}.
TURN 7 9 {ECO:0000244|PDB:1WHS}.
STRAND 24 32 {ECO:0000244|PDB:1WHS}.
TURN 33 36 {ECO:0000244|PDB:1WHS}.
STRAND 37 44 {ECO:0000244|PDB:1WHS}.
HELIX 48 50 {ECO:0000244|PDB:1WHS}.
STRAND 55 59 {ECO:0000244|PDB:1WHS}.
TURN 62 64 {ECO:0000244|PDB:1WHS}.
TURN 67 70 {ECO:0000244|PDB:1WHS}.
HELIX 71 74 {ECO:0000244|PDB:1WHS}.
STRAND 75 81 {ECO:0000244|PDB:1WHS}.
HELIX 83 85 {ECO:0000244|PDB:1WHS}.
STRAND 88 90 {ECO:0000244|PDB:1WHS}.
HELIX 95 97 {ECO:0000244|PDB:1WHS}.
STRAND 99 104 {ECO:0000244|PDB:1WHS}.
STRAND 114 117 {ECO:0000244|PDB:1WHS}.
HELIX 118 122 {ECO:0000244|PDB:1WHS}.
HELIX 126 143 {ECO:0000244|PDB:1WHS}.
HELIX 145 147 {ECO:0000244|PDB:1WHS}.
STRAND 151 158 {ECO:0000244|PDB:1WHS}.
HELIX 160 174 {ECO:0000244|PDB:1WHS}.
STRAND 180 189 {ECO:0000244|PDB:1WHS}.
HELIX 193 205 {ECO:0000244|PDB:1WHS}.
TURN 206 208 {ECO:0000244|PDB:1WHS}.
HELIX 212 222 {ECO:0000244|PDB:1WHS}.
STRAND 227 229 {ECO:0000244|PDB:1WHS}.
HELIX 232 245 {ECO:0000244|PDB:1WHS}.
HELIX 292 301 {ECO:0000244|PDB:1WHS}.
HELIX 303 308 {ECO:0000244|PDB:1WHS}.
STRAND 312 315 {ECO:0000244|PDB:1BCR}.
HELIX 326 330 {ECO:0000244|PDB:1WHS}.
HELIX 340 348 {ECO:0000244|PDB:1WHS}.
STRAND 352 358 {ECO:0000244|PDB:1WHS}.
STRAND 362 364 {ECO:0000244|PDB:1WHS}.
HELIX 366 374 {ECO:0000244|PDB:1WHS}.
STRAND 380 389 {ECO:0000244|PDB:1WHS}.
STRAND 392 400 {ECO:0000244|PDB:1WHS}.
STRAND 403 408 {ECO:0000244|PDB:1WHS}.
HELIX 415 418 {ECO:0000244|PDB:1WHS}.
HELIX 420 432 {ECO:0000244|PDB:1WHS}.
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


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