INV2_ORYSJ
ID INV2_ORYSJ Reviewed; 598 AA.
AC Q0JDC5; A3ATP3; Q56UD4; Q6VGJ3; Q7XVJ4;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Beta-fructofuranosidase, insoluble isoenzyme 2;
DE EC=3.2.1.26 {ECO:0000269|PubMed:18820698, ECO:0000269|PubMed:20416079};
DE AltName: Full=Cell wall beta-fructosidase 2;
DE AltName: Full=Invertase 2;
DE AltName: Full=OsCIN2;
DE AltName: Full=Protein GRAIN INCOMPLETE FILLING 1 {ECO:0000303|PubMed:15685292};
DE AltName: Full=Sucrose hydrolase 2;
DE Flags: Precursor;
GN Name=CIN2; Synonyms=GIF1 {ECO:0000303|PubMed:15685292};
GN OrderedLocusNames=Os04g0413500, LOC_Os04g33740;
GN ORFNames=OJ000126_13.8, OsJ_014165;
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, DEVELOPMENTAL STAGE, AND
RP INDUCTION.
RC STRAIN=cv. Nipponbare;
RX PubMed=15759120; DOI=10.1007/s00299-004-0910-z;
RA Cho J.-I., Lee S.-K., Ko S., Kim H.-K., Jun S.-H., Lee Y.-H., Bhoo S.H.,
RA Lee K.-W., An G., Hahn T.-R., Jeon J.-S.;
RT "Molecular cloning and expression analysis of the cell-wall invertase gene
RT family in rice (Oryza sativa L.).";
RL Plant Cell Rep. 24:225-236(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
RN [3]
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 [4]
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 [5]
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 [6]
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 [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP BIOTECHNOLOGY, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Zhonghua 11;
RX PubMed=18820698; DOI=10.1038/ng.220;
RA Wang E., Wang J., Zhu X., Hao W., Wang L., Li Q., Zhang L., He W., Lu B.,
RA Lin H., Ma H., Zhang G., He Z.;
RT "Control of rice grain-filling and yield by a gene with a potential
RT signature of domestication.";
RL Nat. Genet. 40:1370-1374(2008).
RN [8]
RP CATALYTIC ACTIVITY.
RX PubMed=20416079; DOI=10.1186/1471-2148-10-108;
RA Wang E., Xu X., Zhang L., Zhang H., Lin L., Wang Q., Li Q., Ge S., Lu B.R.,
RA Wang W., He Z.;
RT "Duplication and independent selection of cell-wall invertase genes GIF1
RT and OsCIN1 during rice evolution and domestication.";
RL BMC Evol. Biol. 10:108-108(2010).
RN [9]
RP FUNCTION.
RX PubMed=24118770; DOI=10.1111/mpp.12078;
RA Sun L., Yang D.L., Kong Y., Chen Y., Li X.Z., Zeng L.J., Li Q., Wang E.T.,
RA He Z.H.;
RT "Sugar homeostasis mediated by cell wall invertase GRAIN INCOMPLETE FILLING
RT 1 (GIF1) plays a role in pre-existing and induced defence in rice.";
RL Mol. Plant Pathol. 15:161-173(2014).
CC -!- FUNCTION: Cell wall-associated invertase that cleaves sucrose into
CC glucose and fructose and is required for assimilated carbon
CC partitioning during early grain-filling. May be involved in sucrose
CC unloaded in the ovular and stylar vascular tissues for the stimulation
CC of starch synthesis in the developing endosperm during grain-filling
CC (PubMed:18820698). Sugar homeostasis mediated by CIN2/GIF1 plays an
CC important role in constitutive and induced physical and chemical
CC defense against pathogens (PubMed:24118770).
CC {ECO:0000269|PubMed:18820698, ECO:0000269|PubMed:24118770}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing beta-D-fructofuranoside
CC residues in beta-D-fructofuranosides.; EC=3.2.1.26;
CC Evidence={ECO:0000269|PubMed:18820698, ECO:0000269|PubMed:20416079};
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305}.
CC Note=Associated with the cell wall. {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves and flowers. Weakly expressed
CC in seeds (PubMed:15759120). Expressed in growing roots, node and the
CC rapidly elongating zone of the internode (PubMed:18820698).
CC {ECO:0000269|PubMed:15759120, ECO:0000269|PubMed:18820698}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout flowering, with higher
CC expression from 1 to 6 days after flowering (PubMed:15759120). During
CC early grain-filling, expressed in the ovular vascular and lateral
CC stylar vascular traces (PubMed:18820698). {ECO:0000269|PubMed:15759120,
CC ECO:0000269|PubMed:18820698}.
CC -!- INDUCTION: By sucrose in caryopsis from 1 to 2 and from 9 to 10 days
CC after flowering. {ECO:0000269|PubMed:15759120}.
CC -!- DISRUPTION PHENOTYPE: Slow grain-filling resulting in reduced weight of
CC grains containinf loosely packed starch granules and reduced levels of
CC amylose and amylopectin. {ECO:0000269|PubMed:18820698}.
CC -!- BIOTECHNOLOGY: CIN2/GIF1 is a potential domestication-selected gene
CC that controls grain filling and yield, and could be used for further
CC crop improvement. {ECO:0000303|PubMed:18820698}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD40589.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY578159; AAT84402.1; -; mRNA.
DR EMBL; AL662945; CAD40589.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008210; BAF14662.1; -; Genomic_DNA.
DR EMBL; AP014960; BAS89136.1; -; Genomic_DNA.
DR EMBL; CM000141; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015633534.1; XM_015778048.1.
DR AlphaFoldDB; Q0JDC5; -.
DR SMR; Q0JDC5; -.
DR STRING; 4530.OS04T0413500-01; -.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
DR PaxDb; Q0JDC5; -.
DR PRIDE; Q0JDC5; -.
DR EnsemblPlants; Os04t0413500-01; Os04t0413500-01; Os04g0413500.
DR GeneID; 4335790; -.
DR Gramene; Os04t0413500-01; Os04t0413500-01; Os04g0413500.
DR KEGG; osa:4335790; -.
DR eggNOG; KOG0228; Eukaryota.
DR HOGENOM; CLU_001528_6_0_1; -.
DR InParanoid; Q0JDC5; -.
DR OMA; YYAGEYH; -.
DR OrthoDB; 405663at2759; -.
DR PlantReactome; R-OSA-9035605; Regulation of seed size.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000007752; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR ExpressionAtlas; Q0JDC5; baseline and differential.
DR Genevisible; Q0JDC5; OS.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004564; F:beta-fructofuranosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0052576; P:carbohydrate storage; IMP:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
DR Gene3D; 2.115.10.20; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001362; Glyco_hydro_32.
DR InterPro; IPR018053; Glyco_hydro_32_AS.
DR InterPro; IPR013189; Glyco_hydro_32_C.
DR InterPro; IPR013148; Glyco_hydro_32_N.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR Pfam; PF08244; Glyco_hydro_32C; 1.
DR Pfam; PF00251; Glyco_hydro_32N; 1.
DR SMART; SM00640; Glyco_32; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF75005; SSF75005; 1.
DR PROSITE; PS00609; GLYCOSYL_HYDROL_F32; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cell wall; Glycoprotein; Glycosidase; Hydrolase;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..598
FT /note="Beta-fructofuranosidase, insoluble isoenzyme 2"
FT /id="PRO_0000033380"
FT ACT_SITE 69
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 598 AA; 66263 MW; DFAE59481FA19A4F CRC64;
MGVLGSRVAW AWLVQLLLLQ QLAGASHVVY DDLELQAAAT TADGVPPSIV DSELRTGYHF
QPPKNWINDP NAPMYYKGWY HLFYQYNPKG AVWGNIVWAH SVSRDLINWV ALKPAIEPSI
RADKYGCWSG SATMMADGTP VIMYTGVNRP DVNYQVQNVA LPRNGSDPLL REWVKPGHNP
VIVPEGGINA TQFRDPTTAW RGADGHWRLL VGSLAGQSRG VAYVYRSRDF RRWTRAAQPL
HSAPTGMWEC PDFYPVTADG RREGVDTSSA VVDAAASARV KYVLKNSLDL RRYDYYTVGT
YDRKAERYVP DDPAGDEHHI RYDYGNFYAS KTFYDPAKRR RILWGWANES DTAADDVAKG
WAGIQAIPRK VWLDPSGKQL LQWPIEEVER LRGKWPVILK DRVVKPGEHV EVTGLQTAQA
DVEVSFEVGS LEAAERLDPA MAYDAQRLCS ARGADARGGV GPFGLWVLAS AGLEEKTAVF
FRVFRPAARG GGAGKPVVLM CTDPTKSSRN PNMYQPTFAG FVDTDITNGK ISLRSLIDRS
VVESFGAGGK ACILSRVYPS LAIGKNARLY VFNNGKAEIK VSQLTAWEMK KPVMMNGA
