ID CBP2_WHEAT STANDARD; PRT; 423 AA. AC P08819; DT 01-NOV-1988 (Rel. 09, Created) DT 01-NOV-1988 (Rel. 09, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Serine carboxypeptidase II chains A and B (EC 3.4.16.6) DE (Carboxypeptidase D) (CPDW-II) (CP-WII). GN CBP2. OS Triticum aestivum (Wheat). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; Pooideae; OC Triticeae; Triticum. OX NCBI_TaxID=4565; RN [1] RP SEQUENCE. 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 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 [3] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). RX MEDLINE=93003139; PubMed=1390755; 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). 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 -!- SIMILARITY: Belongs to peptidase family S10. 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 PIR; A29639; A29639. DR PDB; 3SC2; 31-OCT-93. DR PDB; 1WHS; 22-JUN-94. DR PDB; 1WHT; 22-JUN-94. DR PDB; 1BCR; 08-MAR-96. DR PDB; 1BCS; 08-MAR-96. DR MEROPS; S10.005; -. DR InterPro; IPR001563; Peptidase_S10. DR InterPro; IPR000379; Ser_estrs. DR PRINTS; PR00724; CRBOXYPTASEC. DR ProDom; PD001189; Serine_carbpept; 1. DR PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1. DR PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1. KW Hydrolase; Carboxypeptidase; Glycoprotein; Zymogen; 3D-structure. FT CHAIN 1 263 Serine carboxypeptidase II chain A. FT NON_CONS 263 264 FT CHAIN 264 423 Serine carboxypeptidase II chain B. FT ACT_SITE 158 158 FT ACT_SITE 340 340 FT ACT_SITE 392 392 FT DISULFID 65 303 Interchain. FT DISULFID 222 234 FT DISULFID 258 270 FT CARBOHYD 116 116 N-linked (GlcNAc...). FT CARBOHYD 127 127 N-linked (GlcNAc...). FT CARBOHYD 259 259 N-linked (GlcNAc...). FT CARBOHYD 291 291 N-linked (GlcNAc...). FT CARBOHYD 297 297 N-linked (GlcNAc...). FT CARBOHYD 421 421 N-linked (GlcNAc...). FT VARIANT 1 3 Missing (in a' chain). FT HELIX 6 9 FT STRAND 10 10 FT TURN 15 16 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 STRAND 65 65 FT TURN 67 70 FT HELIX 71 74 FT STRAND 79 81 FT HELIX 83 85 FT STRAND 88 90 FT TURN 92 93 FT HELIX 95 97 FT TURN 98 98 FT STRAND 100 104 FT TURN 108 109 FT TURN 111 112 FT STRAND 114 115 FT HELIX 118 122 FT HELIX 126 143 FT HELIX 145 147 FT TURN 148 149 FT STRAND 151 157 FT TURN 158 159 FT HELIX 160 174 FT TURN 175 175 FT TURN 177 178 FT STRAND 180 187 FT STRAND 192 192 FT HELIX 193 205 FT TURN 206 208 FT HELIX 212 222 FT TURN 223 224 FT HELIX 232 245 FT TURN 250 251 FT TURN 253 254 FT TURN 269 270 FT HELIX 271 279 FT TURN 280 280 FT HELIX 282 288 FT TURN 289 289 FT TURN 292 293 FT STRAND 303 303 FT HELIX 305 309 FT TURN 310 310 FT STRAND 317 317 FT HELIX 319 327 FT TURN 328 329 FT STRAND 331 337 FT TURN 338 339 FT HELIX 345 353 FT TURN 354 356 FT STRAND 359 368 FT TURN 369 370 FT STRAND 371 379 FT TURN 380 381 FT STRAND 382 387 FT TURN 388 389 FT HELIX 394 397 FT HELIX 399 411 FT TURN 412 412 SQ SEQUENCE 423 AA; 47111 MW; C64815BFF62B085C 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 TSSTGSYDPC TERYSTAYYN RRDVQMALHA NVTGAMNYTW ATCSDTINTH WHDAPRSMLP IYRELIAAGL RIWVFSGDTD AVVPLTATRY SIGALGLPTT TSWYPWYDDQ EVGGWSQVYK GLTLVSVRGA GHEVPLHRPR QALVLFQYFL QGKPMPGQTK NAT //