ID   CBP21_HORVU             Reviewed;         324 AA.
AC   P55747;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Serine carboxypeptidase II-1;
DE            EC=3.4.16.6;
DE   AltName: Full=CP-MII.1;
DE   Contains:
DE     RecName: Full=Serine carboxypeptidase II-1 chain A;
DE   Contains:
DE     RecName: Full=Serine carboxypeptidase II-1 chain B;
DE   Flags: Precursor; Fragment;
GN   Name=CXP;2-1;
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; X78876; CAB58992.1; -; mRNA.
DR   AlphaFoldDB; P55747; -.
DR   SMR; P55747; -.
DR   ESTHER; horvu-cp21; Carboxypeptidase_S10.
DR   MEROPS; S10.005; -.
DR   EnsemblPlants; HORVU.MOREX.r2.3HG0201590.1; HORVU.MOREX.r2.3HG0201590.1; HORVU.MOREX.r2.3HG0201590.
DR   EnsemblPlants; HORVU.MOREX.r2.3HG0201590.1.mrna1; HORVU.MOREX.r2.3HG0201590.1.mrna1; HORVU.MOREX.r2.3HG0201590.1.
DR   Gramene; HORVU.MOREX.r2.3HG0201590.1; HORVU.MOREX.r2.3HG0201590.1; HORVU.MOREX.r2.3HG0201590.
DR   Gramene; HORVU.MOREX.r2.3HG0201590.1.mrna1; HORVU.MOREX.r2.3HG0201590.1.mrna1; HORVU.MOREX.r2.3HG0201590.1.
DR   ExpressionAtlas; P55747; 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..149
FT                   /note="Serine carboxypeptidase II-1 chain A"
FT                   /id="PRO_0000004314"
FT   PROPEP          150..162
FT                   /note="Linker peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000004315"
FT   CHAIN           163..324
FT                   /note="Serine carboxypeptidase II-1 chain B"
FT                   /id="PRO_0000004316"
FT   ACT_SITE        41
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        239
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        291
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        10
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        191
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        109..121
FT                   /evidence="ECO:0000250"
FT   DISULFID        145..170
FT                   /note="Interchain (between A and B chains)"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   324 AA;  37408 MW;  70F081D6B9723A60 CRC64;
     GSDLLTPGDN KTAHDSYAFL VNWLERFPQY KYRDFYIAGE SYAGHYVPQL SQLVHRNNKG
     VRKPILNFKG FMVGNAVIDD YHDFVGTFEY WWTHGLISDD TYQKLQLACE FDSAEHESEA
     CNKINNVAEA EEGLIDAYSI YTPTCKKTSL HRRRLIKGRR PWLPRGYDPC TEQYSTKYYN
     LPEVQKAFRA NVTGIPYSWT ACSDVLSDHW KDSPRSMLPI YRELIAAGIR IWVFSGDADS
     VVPLTATRYS IDALYLPTVT NWYPWYDEEE VAGWCQVYKG LTLVTIRGAG HEVPLHRPQQ
     ALKLFEHFLQ DKPMPRPAHS IQSF