ID   CBP3_HORVU              Reviewed;         508 AA.
AC   P21529;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   27-MAR-2024, entry version 120.
DE   RecName: Full=Serine carboxypeptidase 3;
DE            EC=3.4.16.5;
DE   AltName: Full=CP-MIII;
DE   AltName: Full=Serine carboxypeptidase III;
DE   Flags: Precursor;
GN   Name=CBP3; Synonyms=CXP;3;
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   STRAIN=cv. Himalaya; 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   PROTEIN SEQUENCE OF 81-491.
RC   STRAIN=cv. Gula;
RX   PubMed=2639682; DOI=10.1007/bf02904473;
RA   Soerensen S.B., Svendsen I., Breddam K.;
RT   "Primary structure of carboxypeptidase III from malted barley.";
RL   Carlsberg Res. Commun. 54:193-202(1989).
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   -!- ACTIVITY REGULATION: Inhibited by mercuric ions.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Secreted. Note=Secreted into the endosperm.
CC   -!- DEVELOPMENTAL STAGE: Expressed mainly in the aleurone and, to a lesser
CC       extent in the embryo, throughout the 5-days germination period
CC       exclusively, with a maximal level at 3 days. Also found in the roots
CC       and shoots of the growing seedling.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR   EMBL; Y09604; CAA70817.1; -; mRNA.
DR   PIR; A35275; A35275.
DR   AlphaFoldDB; P21529; -.
DR   SMR; P21529; -.
DR   ESTHER; horvu-cbp3; Carboxypeptidase_S10.
DR   MEROPS; S10.009; -.
DR   GlyCosmos; P21529; 1 site, No reported glycans.
DR   ExpressionAtlas; P21529; 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; 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:SF259; SERINE CARBOXYPEPTIDASE 3; 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..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..80
FT                   /evidence="ECO:0000269|PubMed:2639682"
FT                   /id="PRO_0000004324"
FT   CHAIN           81..491
FT                   /note="Serine carboxypeptidase 3"
FT                   /id="PRO_0000004325"
FT   PROPEP          492..508
FT                   /id="PRO_0000004326"
FT   REGION          48..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        223
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        411
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        468
FT                   /evidence="ECO:0000250"
FT   BINDING         414
FT                   /ligand="substrate"
FT   MOD_RES         81
FT                   /note="Blocked amino end (Leu)"
FT   CARBOHYD        151
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   DISULFID        133..373
FT                   /evidence="ECO:0000250"
FT   DISULFID        301..316
FT                   /evidence="ECO:0000250"
FT   DISULFID        339..344
FT                   /evidence="ECO:0000250"
FT   VARIANT         265
FT                   /note="Q -> V"
SQ   SEQUENCE   508 AA;  56362 MW;  70C6751D78D40AB6 CRC64;
     MVTTPRLVSL LLLLALCAAA AGALRLPPDA SFPGAQAERL IRALNLLPKD SSSSSGRHGA
     RVGEGNEDVA PGQLLERRVT LPGLPEGVAD LGHHAGYYRL PNTHDARMFY FFFESRGKKE
     DPVVIWLTGG PGCSSELAVF YENGPFTIAN NMSLVWNKFG WDKISNIIFV DQPTGTGFSY
     SSDDRDTRHD ETGVSNDLYD FLQVFFKKHP EFIKNDFFIT GESYAGHYIP AFASRVHQGN
     KKNEGTHINL KGFAIGNGLT DPAIQYKAYT DYALEMNLIQ KADYERINKF IPPCEFAIKL
     CGTNGKASCM AAYMVCNTIF NSIMKLVGTK NYYDVRKECE GKLCYDFSNL EKFFGDKAVR
     QAIGVGDIEF VSCSTSVYQA MLTDWMRNLE VGIPALLEDG INVLIYAGEY DLICNWLGNS
     RWVHSMEWSG QKDFAKTAES SFLVDDAQAG VLKSHGALSF LKVHNAGHMV PMDQPKAALE
     MLRRFTQGKL KEAVPEEESS TTSFYAAM
//