SCP26_ORYSJ
ID SCP26_ORYSJ Reviewed; 482 AA.
AC Q5W727;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Serine carboxypeptidase-like 26 {ECO:0000305};
DE Short=OsSCP26 {ECO:0000303|PubMed:16895613};
DE EC=3.4.16.- {ECO:0000305};
DE AltName: Full=Protein GRAIN SIZE 5 {ECO:0000303|PubMed:22019783};
DE Flags: Precursor;
GN Name=SCP26 {ECO:0000303|PubMed:16895613};
GN Synonyms=GS5 {ECO:0000303|PubMed:22019783};
GN OrderedLocusNames=Os05g0158500 {ECO:0000312|EMBL:BAF16624.1},
GN LOC_Os05g06660 {ECO:0000305};
GN ORFNames=OsJ_17198 {ECO:0000312|EMBL:EEE62407.1},
GN OSJNBa0017J22.3 {ECO:0000312|EMBL:AAV43913.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16261349; DOI=10.1007/s00438-005-0039-y;
RA Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT "A fine physical map of the rice chromosome 5.";
RL Mol. Genet. Genomics 274:337-345(2005).
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 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).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16895613; DOI=10.1186/1471-2164-7-200;
RA Tripathi L.P., Sowdhamini R.;
RT "Cross genome comparisons of serine proteases in Arabidopsis and rice.";
RL BMC Genomics 7:200-200(2006).
RN [7]
RP FUNCTION.
RX PubMed=22019783; DOI=10.1038/ng.977;
RA Li Y., Fan C., Xing Y., Jiang Y., Luo L., Sun L., Shao D., Xu C., Li X.,
RA Xiao J., He Y., Zhang Q.;
RT "Natural variation in GS5 plays an important role in regulating grain size
RT and yield in rice.";
RL Nat. Genet. 43:1266-1269(2011).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=25711711; DOI=10.1093/jxb/erv058;
RA Xu C., Liu Y., Li Y., Xu X., Xu C., Li X., Xiao J., Zhang Q.;
RT "Differential expression of GS5 regulates grain size in rice.";
RL J. Exp. Bot. 66:2611-2623(2015).
CC -!- FUNCTION: Acts as positive regulator of grain size by controlling grain
CC width, filling and weight. High expression of GS5 in the grain is
CC correlated with large grain size. {ECO:0000269|PubMed:22019783,
CC ECO:0000269|PubMed:25711711}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22019783,
CC ECO:0000269|PubMed:25711711}.
CC -!- INDUCTION: Induced by light. Circadian regulation with a peak of
CC expression at dusk (PubMed:25711711). Down-regulated by abscisic acid
CC (ABA) and brassinosteroid (BR) (PubMed:25711711).
CC {ECO:0000269|PubMed:25711711}.
CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR EMBL; AC119288; AAV43913.1; -; Genomic_DNA.
DR EMBL; AP008211; BAF16624.1; -; Genomic_DNA.
DR EMBL; AP014961; BAS92383.1; -; Genomic_DNA.
DR EMBL; CM000142; EEE62407.1; -; Genomic_DNA.
DR RefSeq; XP_015640559.1; XM_015785073.1.
DR AlphaFoldDB; Q5W727; -.
DR SMR; Q5W727; -.
DR STRING; 4530.OS05T0158500-01; -.
DR ESTHER; orysa-q5w727; Carboxypeptidase_S10.
DR MEROPS; S10.A20; -.
DR PaxDb; Q5W727; -.
DR PRIDE; Q5W727; -.
DR EnsemblPlants; Os05t0158500-01; Os05t0158500-01; Os05g0158500.
DR GeneID; 4337873; -.
DR Gramene; Os05t0158500-01; Os05t0158500-01; Os05g0158500.
DR KEGG; osa:4337873; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_13_0_1; -.
DR InParanoid; Q5W727; -.
DR OMA; DQVYERI; -.
DR OrthoDB; 607679at2759; -.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000007752; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; 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; PS00131; CARBOXYPEPT_SER_SER; 1.
PE 2: Evidence at transcript level;
KW Carboxypeptidase; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..482
FT /note="Serine carboxypeptidase-like 26"
FT /evidence="ECO:0000255"
FT /id="PRO_5010396574"
FT ACT_SITE 194
FT /evidence="ECO:0000250"
FT ACT_SITE 403
FT /evidence="ECO:0000250"
FT ACT_SITE 455
FT /evidence="ECO:0000250"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 101..366
FT /evidence="ECO:0000250"
FT DISULFID 263..274
FT /evidence="ECO:0000250"
FT DISULFID 298..333
FT /evidence="ECO:0000250"
SQ SEQUENCE 482 AA; 53631 MW; AEDD9848A21996EE CRC64;
MAVAAAAAAR RRDVSCLLLL LCFSSSMAAT GGGGGGGEQE ADRVARLPGQ PASPAVSQFA
GYVGVDERHG RALFYWFFEA QASPAPEKKP LLLWLNGGPG CSSIGYGAAS ELGPLRVARQ
GAALEFNQYG WNKEANLLFL ESPVGVGFSY TNTSSDLSNL NDDFVAEDAY SFLVNWFKRF
PQYKDNEFYI SGESYAGHYV PQLADLVYER NKDKRASTYI NLKGFIVGNP LTDDYYDSKG
LAEYAWSHAI VSDQVYERIK KTCNFKNSNW TDDCNAAMNI IFSQYNQIDI YNIYAPKCLL
NSTSASSPDR AFFANNQEQF RWRIKMFSGY DPCYSSYAED YFNKHDVQEA FHANASGLLP
GKWQVCSDQI LNSYNFSVLS ILPIYSKLIK AGLRVWLYSG DADGRVPVIS SRYCVEALGL
PIKTDWQSWY LDKQVAGRFV EYHGMTMVTV RGAGHLVPLN KPAEGLMLIN AFLHGEKLPT
SR
