INV1_ORYSJ
ID INV1_ORYSJ Reviewed; 577 AA.
AC Q0E0P0; A0A0P0VK46; Q6EU76; Q6VEF4; Q8S922;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Beta-fructofuranosidase, insoluble isoenzyme 1;
DE EC=3.2.1.26;
DE AltName: Full=Cell wall beta-fructosidase 1;
DE AltName: Full=Invertase 1;
DE AltName: Full=OsCIN1;
DE AltName: Full=Sucrose hydrolase 1;
DE Flags: Precursor;
GN Name=CIN1; OrderedLocusNames=Os02g0534400, LOC_Os02g33110;
GN ORFNames=B1136H02.14, OJ1112_G07.1;
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. Nipponbare; TISSUE=Panicle;
RX PubMed=11978873; DOI=10.1093/pcp/pcf055;
RA Hirose T., Takano M., Terao T.;
RT "Cell wall invertase in developing rice caryopsis: molecular cloning of
RT OsCIN1 and analysis of its expression in relation to its role in grain
RT filling.";
RL Plant Cell Physiol. 43:452-459(2002).
RN [2]
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 [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 DEVELOPMENTAL STAGE.
RX PubMed=15701658; DOI=10.1093/pcp/pci066;
RA Ishimaru T., Hirose T., Matsuda T., Goto A., Takahashi K., Sasaki H.,
RA Terao T., Ishii R., Ohsugi R., Yamagishi T.;
RT "Expression patterns of genes encoding carbohydrate-metabolizing enzymes
RT and their relationship to grain filling in rice (Oryza sativa L.):
RT comparison of caryopses located at different positions in a panicle.";
RL Plant Cell Physiol. 46:620-628(2005).
CC -!- FUNCTION: May play a role in sucrose partitioning during seed
CC development and in stress response.
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:0000255|PROSITE-ProRule:PRU10067};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000305}. Secreted, cell wall {ECO:0000305}. Note=Associated to
CC the cell wall. {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves and flowers. Weakly
CC expressed in seeds. {ECO:0000269|PubMed:11978873,
CC ECO:0000269|PubMed:15759120}.
CC -!- DEVELOPMENTAL STAGE: Expressed from 1 to 3 days after flowering mainly
CC in the maternal tissues of the developing caryopsis, corresponding to
CC the early grain filling stage. {ECO:0000269|PubMed:11978873,
CC ECO:0000269|PubMed:15701658, ECO:0000269|PubMed:15759120}.
CC -!- INDUCTION: By sugar in excised leaves. By rice blast fungus (M.grisea)
CC 4 hours after infection. {ECO:0000269|PubMed:15759120}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
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DR EMBL; AB073749; BAB90855.1; -; mRNA.
DR EMBL; AY578158; AAT84401.1; -; mRNA.
DR EMBL; AP004156; BAD27793.1; -; Genomic_DNA.
DR EMBL; AP005798; BAD29294.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF08948.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS79053.1; -; Genomic_DNA.
DR RefSeq; XP_015625273.1; XM_015769787.1.
DR AlphaFoldDB; Q0E0P0; -.
DR SMR; Q0E0P0; -.
DR STRING; 4530.OS02T0534400-01; -.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
DR PaxDb; Q0E0P0; -.
DR PRIDE; Q0E0P0; -.
DR EnsemblPlants; Os02t0534400-01; Os02t0534400-01; Os02g0534400.
DR GeneID; 4329561; -.
DR Gramene; Os02t0534400-01; Os02t0534400-01; Os02g0534400.
DR KEGG; osa:4329561; -.
DR eggNOG; KOG0228; Eukaryota.
DR HOGENOM; CLU_001528_6_0_1; -.
DR InParanoid; Q0E0P0; -.
DR OMA; PEPGMNA; -.
DR OrthoDB; 405663at2759; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR Genevisible; Q0E0P0; OS.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0004564; F:beta-fructofuranosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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 2: Evidence at transcript level;
KW Apoplast; Cell wall; Glycoprotein; Glycosidase; Hydrolase;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..577
FT /note="Beta-fructofuranosidase, insoluble isoenzyme 1"
FT /id="PRO_0000033379"
FT ACT_SITE 63
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 428
FT /note="D -> N (in Ref. 1; BAB90855)"
FT /evidence="ECO:0000305"
FT CONFLICT 475
FT /note="K -> E (in Ref. 1; BAB90855)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 577 AA; 63984 MW; 2A39D555E834529C CRC64;
MGTRLLALAP WLLLLLLQLA GASHVVHRSL EAEQAPSSVP ASIVSPLLRT GYHFQPPMNW
INDPNGPLYY KGWYHLFYQY NPKGAVWGNI VWAHSVSQDL INWIALEPAI KPDIPSDQYG
CWSGSATILP DGTPAILYTG IDRPNINYQV QNIAFPKNAS DPLLREWVKP AYNPVATPEP
GMNATQFRDP TTAWYADGHW RMLVGGLKGA RLGLAYLYRS RDFKTWVRAK HPLHSALTGM
WECPDFFPLQ APGLQAGLDT SVPSSKYVLK NSLDLTRYDY YTVGIYNKVT ERYVPDNPAG
DYHRLRYDYG NFYASKTFFD PVKHRRILLG WANESDSVTY DKAKGWAGIH AIPRKVWLDP
SGKQLLQWPI EELETLRGKS VSVFDKVVKP GEHFQVTGLG TYQADVEVSL EVSGLEKAEA
LDPAFGDDAE RLCGAKGADV RGGVVFGLWV LASAGLEEKT AVFFRVFKPA GHGAKPVVLM
CTDPTKSSLS PDLYKPTFAG FVDTDISSGK ISLRSLIDRS VVESFGAGGK TCILSRVYPS
MAIGDKAHLY VFNNGEADIK ISHLKAWEMK KPLMNGA
