ID   CBP22_HORVU             Reviewed;         436 AA.
AC   P55748;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Serine carboxypeptidase II-2;
DE            EC=3.4.16.6;
DE   AltName: Full=CP-MII.2;
DE   Contains:
DE     RecName: Full=Serine carboxypeptidase II-2 chain A;
DE   Contains:
DE     RecName: Full=Serine carboxypeptidase II-2 chain B;
DE   Flags: Precursor; Fragment;
GN   Name=CXP;2-2;
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], AND PARTIAL PROTEIN SEQUENCE.
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. Low levels in
CC       the developing aleurone and embryo. Also found in the roots and shoots
CC       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; X78878; CAB59202.1; -; mRNA.
DR   AlphaFoldDB; P55748; -.
DR   SMR; P55748; -.
DR   ESTHER; horvu-cp22; Carboxypeptidase_S10.
DR   MEROPS; S10.A32; -.
DR   ExpressionAtlas; P55748; 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   1: Evidence at protein level;
KW   Carboxypeptidase; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Hydrolase; Protease; Zymogen.
FT   CHAIN           <1..256
FT                   /note="Serine carboxypeptidase II-2 chain A"
FT                   /id="PRO_0000004317"
FT   PROPEP          257..270
FT                   /note="Linker peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000004318"
FT   CHAIN           271..436
FT                   /note="Serine carboxypeptidase II-2 chain B"
FT                   /id="PRO_0000004319"
FT   ACT_SITE        149
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        350
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        403
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        107
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        56..313
FT                   /note="Interchain (between A and B chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        217..229
FT                   /evidence="ECO:0000250"
FT   DISULFID        253..281
FT                   /note="Interchain (between A and B chains)"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   436 AA;  48952 MW;  E0F82D97E0C34DC9 CRC64;
     VPRVPGQAFD ASFAHYAGYV TVSEDRGAAL FYWFFEAAHD PASKPLLLWL NGGPGCSSIA
     FGVGEEVGPF HVNADGKGVH MNPYSWNQVA NILFLDSPVG VGYSYSNTSA DILSNGDERT
     AKDSLVFLTK WLERFPQYKE REFYLTGESY AGHYVPQLAQ AIKRHHEATG DKSINLKGYM
     VGNALTDDFH DHYGIFQYMW TTGLISDQTY KLLNIFCDFE SFVHTSPQCD KILDIASTEA
     GNIDSYSIFT PTCHSSFASS RNKVVKRLRS VGKMGEQYDP CTEKHSIVYF NLHEVQKALH
     VNPVIGKSKW ETCSEVINTN WKDCERSVLH IYHELIQYGL RIWMFSGDTD AVIPVTSTRY
     SIDALKLPTV TPWHAWYDDD GEVGGWTQGY KGLNFVTVRG AGHEVPLHRP KQALTLIKSF
     LAGRPMPVLS DLRSDM