ID   CBP1_HORVU              Reviewed;         499 AA.
AC   P07519; P07520;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 4.
DT   22-FEB-2023, entry version 131.
DE   RecName: Full=Serine carboxypeptidase 1;
DE            EC=3.4.16.5;
DE   AltName: Full=CP-MI;
DE   AltName: Full=Carboxypeptidase C;
DE   AltName: Full=Serine carboxypeptidase I;
DE   Contains:
DE     RecName: Full=Serine carboxypeptidase 1 chain A;
DE     AltName: Full=Serine carboxypeptidase I chain A;
DE   Contains:
DE     RecName: Full=Serine carboxypeptidase 1 chain B;
DE     AltName: Full=Serine carboxypeptidase I chain B;
DE   Flags: Precursor;
GN   Name=CBP1; Synonyms=CXP;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].
RC   TISSUE=Aleurone;
RA   Rocher A., Lok F., Cameron-Mills V., von Wettstein D.;
RL   Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 88-499.
RX   PubMed=3403516; DOI=10.1016/s0021-9258(18)37928-6;
RA   Doan N.P., Fincher G.B.;
RT   "The A- and B-chains of carboxypeptidase I from germinated barley originate
RT   from a single precursor polypeptide.";
RL   J. Biol. Chem. 263:11106-11110(1988).
RN   [3]
RP   PROTEIN SEQUENCE OF 31-296 AND 352-499.
RA   Soerensen S.B., Breddam K., Svendsen I.;
RT   "Primary structure of carboxypeptidase I from malted barley.";
RL   Carlsberg Res. Commun. 51:475-485(1986).
CC   -!- FUNCTION: May be involved in the degradation of small peptides (2-5
CC       residues) or in the degradation of storage proteins in the embryo.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of a C-terminal amino acid with broad specificity.;
CC         EC=3.4.16.5; Evidence={ECO:0000255|PROSITE-ProRule:PRU10074,
CC         ECO:0000255|PROSITE-ProRule:PRU10075};
CC   -!- SUBUNIT: Carboxypeptidase I is a dimer, where each monomer is composed
CC       of two chains linked by disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted. Note=Secreted into the endosperm.
CC   -!- DEVELOPMENTAL STAGE: After one day of germination, mainly found in the
CC       scutellum of the developing grain; barely detectable after four days,
CC       and absent from the mature grain. A lower level of expression is seen
CC       in the aleurone both during development and germination.
CC   -!- PTM: The linker peptide is endoproteolytically excised during enzyme
CC       maturation.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR   EMBL; Y09603; CAA70816.1; -; mRNA.
DR   EMBL; J03897; AAA32940.1; -; mRNA.
DR   PIR; T05367; CPBHS.
DR   AlphaFoldDB; P07519; -.
DR   SMR; P07519; -.
DR   ESTHER; horvu-cbp1; Carboxypeptidase_S10.
DR   MEROPS; S10.004; -.
DR   GlyCosmos; P07519; 3 sites, No reported glycans.
DR   EnsemblPlants; HORVU.MOREX.r2.3HG0261150.1.mrna1; HORVU.MOREX.r2.3HG0261150.1.mrna1; HORVU.MOREX.r2.3HG0261150.1.
DR   Gramene; HORVU.MOREX.r2.3HG0261150.1.mrna1; HORVU.MOREX.r2.3HG0261150.1.mrna1; HORVU.MOREX.r2.3HG0261150.1.
DR   ExpressionAtlas; P07519; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.12670; -; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 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:SF254; SERINE CARBOXYPEPTIDASE-LIKE 20; 1.
DR   PANTHER; PTHR11802; SERINE PROTEASE FAMILY S10 SERINE CARBOXYPEPTIDASE; 1.
DR   Pfam; PF00450; Peptidase_S10; 1.
DR   PRINTS; PR00724; CRBOXYPTASEC.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 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; Secreted; Signal; Zymogen.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..296
FT                   /note="Serine carboxypeptidase 1 chain A"
FT                   /id="PRO_0000004301"
FT   PROPEP          297..351
FT                   /note="Linker peptide"
FT                   /evidence="ECO:0000269|Ref.3"
FT                   /id="PRO_0000004302"
FT   CHAIN           352..499
FT                   /note="Serine carboxypeptidase 1 chain B"
FT                   /id="PRO_0000004303"
FT   MOTIF           497..499
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        188
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        423
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        476
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        148
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   CARBOHYD        262
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   CARBOHYD        407
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   DISULFID        92..388
FT                   /note="Interchain (between A and B chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        256..268
FT                   /evidence="ECO:0000250"
FT   DISULFID        291..355
FT                   /note="Interchain (between A and B chains)"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        102
FT                   /note="H -> P (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   499 AA;  54096 MW;  9C6674B14D9DB9BF CRC64;
     MARCRRRSGC TAGAALLLLL ALALSGGGGA APQGAEVTGL PGFDGALPSK HYAGYVTVDE
     GHGRNLFYYV VESERDPGKD PVVLWLNGGP GCSSFDGFVY EHGPFNFESG GSVKSLPKLH
     LNPYAWSKVS TMIYLDSPAG VGLSYSKNVS DYETGDLKTA TDSHTFLLKW FQLYPEFLSN
     PFYIAGESYA GVYVPTLSHE VVKGIQGGAK PTINFKGYMV GNGVCDTIFD GNALVPFAHG
     MGLISDEIYQ QASTSCHGNY WNATDGKCDT AISKIESLIS GLNIYDILEP CYHSRSIKEV
     NLQNSKLPQS FKDLGTTNKP FPVRTRMLGR AWPLRAPVKA GRVPSWQEVA SGVPCMSDEV
     ATAWLDNAAV RSAIHAQSVS AIGPWLLCTD KLYFVHDAGS MIAYHKNLTS QGYRAIIFSG
     DHDMCVPFTG SEAWTKSLGY GVVDSWRPWI TNGQVSGYTE GYEHGLTFAT IKGAGHTVPE
     YKPQEAFAFY SRWLAGSKL
//