CBP1_HORVU
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 03-AUG-2022, entry version 129.
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 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; 3.40.50.1820; -; 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; 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
