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Serine carboxypeptidase 2 (EC 3.4.16.6) (CP-MII) (Carboxypeptidase D) (Serine carboxypeptidase II) [Cleaved into: Serine carboxypeptidase 2 chain A (Serine carboxypeptidase II chain A); Serine carboxypeptidase 2 chain B (Serine carboxypeptidase II chain B)]

 CBP2_HORVU              Reviewed;         476 AA.
P08818; P93177;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
02-MAY-2002, sequence version 2.
05-JUL-2017, entry version 108.
RecName: Full=Serine carboxypeptidase 2;
EC=3.4.16.6;
AltName: Full=CP-MII;
AltName: Full=Carboxypeptidase D;
AltName: Full=Serine carboxypeptidase II;
Contains:
RecName: Full=Serine carboxypeptidase 2 chain A;
AltName: Full=Serine carboxypeptidase II chain A;
Contains:
RecName: Full=Serine carboxypeptidase 2 chain B;
AltName: Full=Serine carboxypeptidase II chain B;
Flags: Precursor;
Name=CBP2; Synonyms=CXP;2;
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 [GENOMIC DNA].
STRAIN=cv. Igri; TISSUE=Etiolated leaf;
Rocher A., Lok F., Cameron-Mills V., von Wettstein D.;
"The gene family of serine carboxypeptidases in barley.";
Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
[2]
PROTEIN SEQUENCE OF 35-294 AND 314-472, AND GLYCOSYLATION OF VARIANT
351-AT-352.
Soerensen S.B., Svendsen I., Breddam K.;
"Primary structure of carboxypeptidase II from malted barley.";
Carlsberg Res. Commun. 52:285-295(1987).
-!- 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: Preferential release of a C-terminal arginine
or lysine residue.
-!- SUBUNIT: Carboxypeptidase II is a dimer, where each monomer is
composed of two chains linked by a disulfide bond.
-!- SUBCELLULAR LOCATION: Secreted. Note=Secreted into the endosperm.
-!- DEVELOPMENTAL STAGE: Simultaneously present in aleurone and
endosperm between 20 and 30 days postanthesis. Accumulates in the
developing grain and is stored in its active form in the mature
grain. Also found in the roots and shoots of the growing seedling.
-!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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EMBL; Y09602; CAA70815.1; -; Genomic_DNA.
PIR; T05701; T05701.
ProteinModelPortal; P08818; -.
SMR; P08818; -.
ESTHER; horvu-cbp2; Carboxypeptidase_S10.
MEROPS; S10.005; -.
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; 1.
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 34 {ECO:0000269|Ref.2}.
CHAIN 35 294 Serine carboxypeptidase 2 chain A.
/FTId=PRO_0000004309.
PROPEP 295 313 Linker peptide. {ECO:0000250}.
/FTId=PRO_0000004310.
CHAIN 314 476 Serine carboxypeptidase 2 chain B.
/FTId=PRO_0000004311.
ACT_SITE 190 190 {ECO:0000250}.
ACT_SITE 390 390 {ECO:0000250}.
ACT_SITE 443 443 {ECO:0000250}.
MOD_RES 314 314 Blocked amino end (Thr).
CARBOHYD 148 148 N-linked (GlcNAc...) asparagine.
CARBOHYD 159 159 N-linked (GlcNAc...) asparagine.
CARBOHYD 291 291 N-linked (GlcNAc...) asparagine.
CARBOHYD 341 341 N-linked (GlcNAc...) asparagine.
CARBOHYD 347 347 N-linked (GlcNAc...) asparagine.
CARBOHYD 352 352 N-linked (GlcNAc...) asparagine; partial.
CARBOHYD 352 352 O-linked (GalNAc...) threonine; in
variant 351-AT-352.
CARBOHYD 472 472 N-linked (GlcNAc...) asparagine.
DISULFID 97 353 Interchain (between A and B chains).
{ECO:0000250}.
DISULFID 254 266 {ECO:0000250}.
DISULFID 290 320 Interchain (between A and B chains).
{ECO:0000250}.
VARIANT 351 352 TN -> AT.
CONFLICT 181 181 Y -> R (in Ref. 2; AA sequence).
{ECO:0000305}.
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


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