CBP2_HORVU
ID CBP2_HORVU Reviewed; 476 AA.
AC P08818; P93177;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Serine carboxypeptidase 2;
DE EC=3.4.16.6;
DE AltName: Full=CP-MII;
DE AltName: Full=Carboxypeptidase D;
DE AltName: Full=Serine carboxypeptidase II;
DE Contains:
DE RecName: Full=Serine carboxypeptidase 2 chain A;
DE AltName: Full=Serine carboxypeptidase II chain A;
DE Contains:
DE RecName: Full=Serine carboxypeptidase 2 chain B;
DE AltName: Full=Serine carboxypeptidase II chain B;
DE Flags: Precursor;
GN Name=CBP2; Synonyms=CXP;2;
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 [GENOMIC DNA].
RC STRAIN=cv. Igri; TISSUE=Etiolated leaf;
RA Rocher A., Lok F., Cameron-Mills V., von Wettstein D.;
RT "The gene family of serine carboxypeptidases in barley.";
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 35-294 AND 314-472, AND GLYCOSYLATION OF VARIANT
RP 351-AT-352.
RA Soerensen S.B., Svendsen I., Breddam K.;
RT "Primary structure of carboxypeptidase II from malted barley.";
RL Carlsberg Res. Commun. 52:285-295(1987).
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=Preferential release of a C-terminal arginine or lysine
CC residue.; EC=3.4.16.6;
CC -!- SUBUNIT: Carboxypeptidase II is a dimer, where each monomer is composed
CC of two chains linked by a disulfide bond.
CC -!- SUBCELLULAR LOCATION: Secreted. Note=Secreted into the endosperm.
CC -!- DEVELOPMENTAL STAGE: Simultaneously present in aleurone and endosperm
CC between 20 and 30 days postanthesis. Accumulates in the developing
CC grain and is stored in its active form in the mature grain. Also found
CC in the roots and shoots of the growing seedling.
CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR EMBL; Y09602; CAA70815.1; -; Genomic_DNA.
DR PIR; T05701; T05701.
DR AlphaFoldDB; P08818; -.
DR SMR; P08818; -.
DR ESTHER; horvu-cbp2; Carboxypeptidase_S10.
DR MEROPS; S10.005; -.
DR ExpressionAtlas; P08818; 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..34
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 35..294
FT /note="Serine carboxypeptidase 2 chain A"
FT /id="PRO_0000004309"
FT PROPEP 295..313
FT /note="Linker peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000004310"
FT CHAIN 314..476
FT /note="Serine carboxypeptidase 2 chain B"
FT /id="PRO_0000004311"
FT ACT_SITE 190
FT /evidence="ECO:0000250"
FT ACT_SITE 390
FT /evidence="ECO:0000250"
FT ACT_SITE 443
FT /evidence="ECO:0000250"
FT MOD_RES 314
FT /note="Blocked amino end (Thr)"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine; partial"
FT CARBOHYD 352
FT /note="O-linked (GalNAc...) threonine; in variant 351-AT-
FT 352"
FT CARBOHYD 472
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 97..353
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000250"
FT DISULFID 254..266
FT /evidence="ECO:0000250"
FT DISULFID 290..320
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000250"
FT VARIANT 351..352
FT /note="TN -> AT"
FT CONFLICT 181
FT /note="Y -> R (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 476 AA; 52625 MW; 18685725B1A6B5E4 CRC64;
MRTTTRRLPP APAAAAVLLA ALTCLLLRPA AVAAAGGHAA DRIVRLPGQP EVDFDMYSGY
ITVDEAAGRS LFYLLQEAPE EAQPAPLVLW LNGGPGCSSV AYGASEELGA FRVMPRGAGL
VLNEYRWNKV ANVLFLDSPA GVGFSYTNTS SDIYTSGDNR TAHDSYAFLA AWFERFPHYK
YREFYVAGES YAGHYVPELS QLVHRSGNPV INLKGFMVGN GLIDDYHDYV GTFEFWWNHG
IVSDDTYRRL KDACLHDSFI HPSPACDAAT DVATAEQGNI DMYSLYTPVC NISSSSSSSS
LSRRRTRGRY PWLTGSYDPC TERYSTAYYN RRDVQTALHA NVTGAMNYTW TNCSDTINTH
WHDAPRSMLP IYRELIAAGL RIWVFSGDTD AVVPLTATRY SIGALGLATT TSWYPWYDDL
QEVGGWSQVY KGLTLVSVRG AGHEVPLHRP RQALILFQQF LQGKPMPGRT TNVTVA
