CBPX_ORYSJ
ID CBPX_ORYSJ Reviewed; 429 AA.
AC P52712; Q8GVT1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Serine carboxypeptidase-like;
DE EC=3.4.16.-;
DE Flags: Precursor;
GN Name=CBP31; OrderedLocusNames=Os07g0479300, LOC_Os07g29620;
GN ORFNames=P0434A03.108-1, P0640E12.147-1;
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 [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Yukihikari;
RX PubMed=7972496; DOI=10.1104/pp.105.4.1275;
RA Washio K., Ishikawa K.;
RT "Organ-specific and hormone-dependent expression of genes for serine
RT carboxypeptidases during development and following germination of rice
RT grains.";
RL Plant Physiol. 105:1275-1280(1994).
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=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 [4]
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 -!- TISSUE SPECIFICITY: Abundant in germinated embryos composed of leaf,
CC root, and scutellum. {ECO:0000269|PubMed:7972496}.
CC -!- DEVELOPMENTAL STAGE: Expressed in immature grains. Decreases during
CC maturation and then increases again during germination.
CC {ECO:0000269|PubMed:7972496}.
CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK120117; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D17587; BAA04511.1; -; mRNA.
DR EMBL; AP004299; BAC45113.1; -; Genomic_DNA.
DR EMBL; AP005261; BAD31260.1; -; Genomic_DNA.
DR EMBL; AP014963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK120117; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; T03607; T03607.
DR AlphaFoldDB; P52712; -.
DR SMR; P52712; -.
DR STRING; 4530.OS07T0479300-01; -.
DR ESTHER; orysa-cbpx; Carboxypeptidase_S10.
DR MEROPS; S10.009; -.
DR PaxDb; P52712; -.
DR PRIDE; P52712; -.
DR eggNOG; KOG1282; Eukaryota.
DR InParanoid; P52712; -.
DR Proteomes; UP000000763; Chromosome 7.
DR Proteomes; UP000059680; Chromosome 7.
DR Genevisible; P52712; OS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:Gramene.
DR GO; GO:0005777; C:peroxisome; ISS:Gramene.
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.
FT SIGNAL 1..?
FT /evidence="ECO:0000255"
FT CHAIN ?..429
FT /note="Serine carboxypeptidase-like"
FT /id="PRO_0000004335"
FT ACT_SITE 148
FT /evidence="ECO:0000250"
FT ACT_SITE 336
FT /evidence="ECO:0000250"
FT ACT_SITE 393
FT /evidence="ECO:0000250"
FT BINDING 339
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 414
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 58..298
FT /evidence="ECO:0000250"
FT DISULFID 226..241
FT /evidence="ECO:0000250"
FT DISULFID 264..269
FT /evidence="ECO:0000250"
FT CONFLICT 245
FT /note="F -> C (in Ref. 1; BAA04511)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 429 AA; 47790 MW; 1F2F64F236475BB4 CRC64;
MATGKSGGSS AEDLGHHAGY YRLPNTHDAR LFYFFFESRG SKGEDDPVVI WLTGGPGCSS
ELALFYENGP FHIADNMSLV WNDFGWDQES NLIYVDQPTG TGFSYSSNPR DTRHDEAGVS
NDLYAFLQAF FTEHPNFAKN DFYITGESYA GHYIPAFASR VYKGNKNSEG IHINLKGFAI
GNGLTDPAIQ YKAYTDYSLD MGLITKSQFN RINKIVPTCE LAIKLCGTSG TISCLGAYVV
CNLIFSSIET IIGKKNYYDI RKPCVGSLCY DLSNMEKFLQ LKSVRESLGV GDIQFVSCSP
TVYQAMLLDW MRNLEVGIPE LLENDIKVLI YAGEYDLICN WLGNSRWVNS MEWSGKEAFV
SSSEEPFTVD GKEAGILKSY GPLSFLKVHD AGHMVPMDQP KVALEMLMRW TSGNLSNASS
SFQRLDFTM
