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Serine carboxypeptidase 1 (EC 3.4.16.5) (CP-MI) (Carboxypeptidase C) (Serine carboxypeptidase I) [Cleaved into: Serine carboxypeptidase 1 chain A (Serine carboxypeptidase I chain A); Serine carboxypeptidase 1 chain B (Serine carboxypeptidase I chain B)]

 CBP1_HORVU              Reviewed;         499 AA.
P07519; P07520;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 4.
05-JUL-2017, entry version 114.
RecName: Full=Serine carboxypeptidase 1;
EC=3.4.16.5;
AltName: Full=CP-MI;
AltName: Full=Carboxypeptidase C;
AltName: Full=Serine carboxypeptidase I;
Contains:
RecName: Full=Serine carboxypeptidase 1 chain A;
AltName: Full=Serine carboxypeptidase I chain A;
Contains:
RecName: Full=Serine carboxypeptidase 1 chain B;
AltName: Full=Serine carboxypeptidase I chain B;
Flags: Precursor;
Name=CBP1; Synonyms=CXP;1;
Hordeum vulgare (Barley).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade;
Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
NCBI_TaxID=4513;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Aleurone;
Rocher A., Lok F., Cameron-Mills V., von Wettstein D.;
Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 88-499.
PubMed=3403516;
Doan N.P., Fincher G.B.;
"The A- and B-chains of carboxypeptidase I from germinated barley
originate from a single precursor polypeptide.";
J. Biol. Chem. 263:11106-11110(1988).
[3]
PROTEIN SEQUENCE OF 31-296 AND 352-499.
Soerensen S.B., Breddam K., Svendsen I.;
"Primary structure of carboxypeptidase I from malted barley.";
Carlsberg Res. Commun. 51:475-485(1986).
-!- FUNCTION: May be involved in the degradation of small peptides (2-
5 residues) or in the degradation of storage proteins in the
embryo.
-!- CATALYTIC ACTIVITY: Release of a C-terminal amino acid with broad
specificity. {ECO:0000255|PROSITE-ProRule:PRU10074,
ECO:0000255|PROSITE-ProRule:PRU10075}.
-!- SUBUNIT: Carboxypeptidase I is a dimer, where each monomer is
composed of two chains linked by disulfide bonds.
-!- SUBCELLULAR LOCATION: Secreted. Note=Secreted into the endosperm.
-!- DEVELOPMENTAL STAGE: After one day of germination, mainly found in
the scutellum of the developing grain; barely detectable after
four days, and absent from the mature grain. A lower level of
expression is seen in the aleurone both during development and
germination.
-!- PTM: The linker peptide is endoproteolytically excised during
enzyme maturation.
-!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Y09603; CAA70816.1; -; mRNA.
EMBL; J03897; AAA32940.1; -; mRNA.
PIR; T05367; CPBHS.
UniGene; Hv.12403; -.
ProteinModelPortal; P07519; -.
SMR; P07519; -.
ESTHER; horvu-cbp1; Carboxypeptidase_S10.
MEROPS; S10.004; -.
eggNOG; KOG1282; Eukaryota.
eggNOG; COG2939; LUCA.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR001563; Peptidase_S10.
InterPro; IPR033124; Ser_caboxypep_his_AS.
InterPro; IPR018202; Ser_caboxypep_ser_AS.
PANTHER; PTHR11802; PTHR11802; 1.
Pfam; PF00450; Peptidase_S10; 1.
PRINTS; PR00724; CRBOXYPTASEC.
SUPFAM; SSF53474; SSF53474; 2.
PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1.
PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
1: Evidence at protein level;
Carboxypeptidase; Direct protein sequencing; Disulfide bond;
Glycoprotein; Hydrolase; Protease; Secreted; Signal; Zymogen.
SIGNAL 1 30 {ECO:0000255}.
CHAIN 31 296 Serine carboxypeptidase 1 chain A.
/FTId=PRO_0000004301.
PROPEP 297 351 Linker peptide. {ECO:0000269|Ref.3}.
/FTId=PRO_0000004302.
CHAIN 352 499 Serine carboxypeptidase 1 chain B.
/FTId=PRO_0000004303.
MOTIF 497 499 Microbody targeting signal.
{ECO:0000255}.
ACT_SITE 188 188 {ECO:0000250}.
ACT_SITE 423 423 {ECO:0000250}.
ACT_SITE 476 476 {ECO:0000250}.
CARBOHYD 148 148 N-linked (GlcNAc...) asparagine.
CARBOHYD 262 262 N-linked (GlcNAc...) asparagine.
CARBOHYD 407 407 N-linked (GlcNAc...) asparagine.
DISULFID 92 388 Interchain (between A and B chains).
{ECO:0000250}.
DISULFID 256 268 {ECO:0000250}.
DISULFID 291 355 Interchain (between A and B chains).
{ECO:0000250}.
CONFLICT 102 102 H -> P (in Ref. 3; AA sequence).
{ECO:0000305}.
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


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