ID   CBP23_HORVU             Reviewed;         516 AA.
AC   P52711;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Serine carboxypeptidase II-3;
DE            EC=3.4.16.6;
DE   AltName: Full=CP-MII.3;
DE   Contains:
DE     RecName: Full=Serine carboxypeptidase II-3 chain A;
DE   Contains:
DE     RecName: Full=Serine carboxypeptidase II-3 chain B;
DE   Flags: Precursor;
GN   Name=CXP;2-3;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Alexis; TISSUE=Grain;
RX   PubMed=7520177; DOI=10.1073/pnas.91.17.8209;
RA   Dal Degan F., Rocher A., Cameron-Mills V., von Wettstein D.;
RT   "The expression of serine carboxypeptidases during maturation and
RT   germination of the barley grain.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:8209-8213(1994).
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:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the germinating embryo. Also found in
CC       the roots and shoots of the growing seedling.
CC   -!- PTM: The linker peptide is endoproteolytically excised during enzyme
CC       maturation. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR   EMBL; X78877; CAA55478.1; -; mRNA.
DR   PIR; S44191; S44191.
DR   AlphaFoldDB; P52711; -.
DR   SMR; P52711; -.
DR   ESTHER; horvu-cp23; Carboxypeptidase_S10.
DR   MEROPS; S10.A41; -.
DR   ExpressionAtlas; P52711; baseline and differential.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:UniProtKB-EC.
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   2: Evidence at transcript level;
KW   Carboxypeptidase; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW   Signal; Zymogen.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..77
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000004320"
FT   CHAIN           78..341
FT                   /note="Serine carboxypeptidase II-3 chain A"
FT                   /id="PRO_0000004321"
FT   PROPEP          342..352
FT                   /note="Linker peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000004322"
FT   CHAIN           353..516
FT                   /note="Serine carboxypeptidase II-3 chain B"
FT                   /id="PRO_0000004323"
FT   ACT_SITE        236
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        427
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        484
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        194
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        205
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        301
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        380
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        143..391
FT                   /note="Interchain (between A and B chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        300..315
FT                   /evidence="ECO:0000250"
FT   DISULFID        339..359
FT                   /note="Interchain (between A and B chains)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   516 AA;  55914 MW;  D41AA1C56CF8D355 CRC64;
     MKCTVVALVL LVAVQCLVLG AGPAAAAKAR RTRQGDYLNR LRGSPSSRAS WESLAAVEEQ
     TTTKAAGRPA PVAAAVEAGR KEADRVEALP GHPRGVDFAQ YAGYVTVDAA AGRALFYYLA
     EAVGGNGDKT KPLLLWLNGG PGCSSLGYGA MEELGPFRVM SDGKTLYSNP YSWNHAANVL
     FLESPAGVGY SYSNTTADYG RSGDNGTAED AYQFLDNWLE RFPEYKGREF YITGESYAGH
     YVPQLAHAIL RHASPDINLK GIMIGNAVIN DWTDSKGMYD FFWTHALISD ETADGISKNC
     NFTAYGAGVA SNALCDAASD EVGESLADID IYNIYAPNCQ SEKLVTPPIA PSIDNFDPCT
     DYYVEAYLNR PDVQKALHAN VTRLDHPWSA CSDVLTRWVD SAKTVLPIIQ ELMKNSIRVW
     VYSGDTDGRV PVTSSRLSVN QLQLPVAAKW RPWFSSTKGA GEVGGYIVQY KGDLSLVTVR
     GAGHEVPSYQ PRRALVLVQN FLAGKALPDC KECEQD