ID   CBPX_PEA                Reviewed;         286 AA.
AC   Q41005;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Serine carboxypeptidase-like;
DE            EC=3.4.16.-;
DE   Flags: Fragment;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Feltham First;
RX   PubMed=8654403; DOI=10.1111/j.1432-1033.1996.00574.x;
RA   Jones C.G., Lycett G.W., Tucker G.A.;
RT   "Protease inhibitor studies and cloning of a serine carboxypeptidase cDNA
RT   from germinating seeds of pea (Pisum sativum L.).";
RL   Eur. J. Biochem. 235:574-578(1996).
CC   -!- FUNCTION: Involved in degradation of small peptides.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR   EMBL; Z68130; CAA92216.1; -; mRNA.
DR   PIR; S62370; S62370.
DR   AlphaFoldDB; Q41005; -.
DR   SMR; Q41005; -.
DR   MEROPS; S10.009; -.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
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   PANTHER; PTHR11802; PTHR11802; 1.
DR   Pfam; PF00450; Peptidase_S10; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1.
PE   2: Evidence at transcript level;
KW   Carboxypeptidase; Disulfide bond; Glycoprotein; Hydrolase; Protease.
FT   CHAIN           <1..286
FT                   /note="Serine carboxypeptidase-like"
FT                   /id="PRO_0000120566"
FT   ACT_SITE        4
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        193
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        250
FT                   /evidence="ECO:0000250"
FT   BINDING         196
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        227
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        83..98
FT                   /evidence="ECO:0000250"
FT   DISULFID        121..126
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   286 AA;  31343 MW;  91D6A3F7E944EA6D CRC64;
     TGESYAGHYI PALASRIHQG NQANEGIHIN LKGLAIGNGL TNPAIQYKGY PDYALDMGII
     TQTTHDLLGK VLVPACELAI KLCGTNGKVS CLTANVACNL IFSDIMLHAG GVNYYDIRKK
     CEGSLCYDFS NMEKFLNQES VRDSLGVGKI RFVSCSTEVY MAMLVDWMRN LEVGIPLLLE
     DGINLLIYAG EYDLICNWLG NSRWVHAMKW SGQKEFVASS DVPFVVNGSQ AGLLKSYGPL
     SFLKVHDAGH MVPMDQPKAA LEMVKQWTRG TLAESIDGEE KLVADM