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CBP3_ORYSJ
ID   CBP3_ORYSJ              Reviewed;         500 AA.
AC   P37891; Q0E4K7; Q6Z7C2;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Serine carboxypeptidase 3;
DE            EC=3.4.16.5;
DE   AltName: Full=Serine carboxypeptidase III;
DE   Flags: Precursor;
GN   Name=CBP3; OrderedLocusNames=Os02g0114200, LOC_Os02g02320;
GN   ORFNames=OJ1399_H05.34, OsJ_05092 {ECO:0000312|EMBL:EAZ21483.1},
GN   P0036E06.13;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Yukihikari; TISSUE=Seed;
RX   PubMed=1627776; DOI=10.1007/bf00026789;
RA   Washio K., Ishikawa K.;
RT   "Structure and expression during the germination of rice seeds of the gene
RT   for a carboxypeptidase.";
RL   Plant Mol. Biol. 19:631-640(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
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   -!- SUBUNIT: Monomer. {ECO:0000305}.
CC   -!- INDUCTION: By gibberellic acid (GA). Inhibited by abscisic acid (ABA).
CC   -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR   EMBL; D10985; BAA01757.1; -; Genomic_DNA.
DR   EMBL; AP004090; BAD07648.1; -; Genomic_DNA.
DR   EMBL; AP004867; BAD07926.1; -; Genomic_DNA.
DR   EMBL; AP008208; BAF07581.1; -; Genomic_DNA.
DR   EMBL; AP014958; BAS76637.1; -; Genomic_DNA.
DR   EMBL; CM000139; EAZ21483.1; -; Genomic_DNA.
DR   EMBL; AK061078; BAG87715.1; -; mRNA.
DR   PIR; S22530; S22530.
DR   RefSeq; XP_015626272.1; XM_015770786.1.
DR   AlphaFoldDB; P37891; -.
DR   SMR; P37891; -.
DR   STRING; 4530.OS02T0114200-01; -.
DR   ESTHER; orysa-cbp3; Carboxypeptidase_S10.
DR   MEROPS; S10.009; -.
DR   PaxDb; P37891; -.
DR   PRIDE; P37891; -.
DR   EnsemblPlants; Os02t0114200-01; Os02t0114200-01; Os02g0114200.
DR   GeneID; 4328060; -.
DR   Gramene; Os02t0114200-01; Os02t0114200-01; Os02g0114200.
DR   KEGG; osa:4328060; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_10_1_1; -.
DR   InParanoid; P37891; -.
DR   OMA; PDAFCDP; -.
DR   OrthoDB; 625787at2759; -.
DR   Proteomes; UP000000763; Chromosome 2.
DR   Proteomes; UP000007752; Chromosome 2.
DR   Proteomes; UP000059680; Chromosome 2.
DR   ExpressionAtlas; P37891; baseline and differential.
DR   Genevisible; P37891; OS.
DR   GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Carboxypeptidase; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW   Reference proteome; Signal; Zymogen.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..73
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000004327"
FT   CHAIN           74..484
FT                   /note="Serine carboxypeptidase 3"
FT                   /id="PRO_0000004328"
FT   PROPEP          485..500
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000004329"
FT   ACT_SITE        216
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        404
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        461
FT                   /evidence="ECO:0000250"
FT   BINDING         407
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        144
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        126..366
FT                   /evidence="ECO:0000250"
FT   DISULFID        294..309
FT                   /evidence="ECO:0000250"
FT   DISULFID        332..337
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   500 AA;  55446 MW;  AE455E2780147DB8 CRC64;
     MATARVSLIL LVVVLAASAC AEGLRLPRDA KFPAAQAERL IRSLNLLPKE AGPTGAGDVP
     SVAPGELLER RVTLPGLPQG VGDLGHHAGY YRLPNTHDAR MFYFLFESRG KKEDPVVIWL
     TGGPGCSSEL AVFYENGPFT ISNNMSLAWN KFGWDTISNI IFVDQPTGTG FSYSSDDRDT
     RHDETGVSND LYSFLQVFFK KHPEFAKNDF FITGESYAGH YIPAFASRVH QGNKANEGIH
     INLKGFAIGN GLTDPAIQYK AYTDYALDMN LIKKSDYDRI NKFIPPCEFA IKLCGTNGKA
     SCMAAYMVCN SIFSSIMKLV GTKNYYDVRK ECEGKLCYDF SNLEKFFGDK AVKEAIGVGD
     LEFVSCSTTV YQAMLTDWMR NLEVGIPALL EDGINVLIYA GEYDLICNWL GNSRWVHSME
     WSGQKDFVSS HESPFVVDGA EAGVLKSHGP LSFLKVHNAG HMVPMDQPKA SLEMLRRFTQ
     GKLKEEWLAE LPEQPMYAAM
 
 
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