INV2_ORYSI
ID INV2_ORYSI Reviewed; 598 AA.
AC Q01IS7; A2XT83; Q56UD4; Q6VGJ3; Q7XVJ4;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Beta-fructofuranosidase, insoluble isoenzyme 2;
DE EC=3.2.1.26;
DE AltName: Full=Cell wall beta-fructosidase 2;
DE AltName: Full=Invertase 2;
DE AltName: Full=OsCIN2;
DE AltName: Full=Sucrose hydrolase 2;
DE Flags: Precursor;
GN Name=CIN2; ORFNames=OsI_015276, OSIGBa0134P10.9;
OS Oryza sativa subsp. indica (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=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Minghui 86;
RA Wang Y.-Q., Zhu Z.;
RT "Characterization of three rice cell wall invertase genes.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Guang-Lu-Ai No.4;
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. 93-11;
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).
CC -!- FUNCTION: May play a role in sucrose partitioning during seed
CC development. {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAH67363.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY340072; AAQ24868.1; -; mRNA.
DR EMBL; CR855194; CAH67363.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CM000129; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; Q01IS7; -.
DR SMR; Q01IS7; -.
DR STRING; 39946.Q01IS7; -.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
DR EnsemblPlants; BGIOSGA016364-TA; BGIOSGA016364-PA; BGIOSGA016364.
DR Gramene; BGIOSGA016364-TA; BGIOSGA016364-PA; BGIOSGA016364.
DR HOGENOM; CLU_001528_6_0_1; -.
DR OMA; YYAGEYH; -.
DR BRENDA; 3.2.1.26; 4460.
DR Proteomes; UP000007015; Chromosome 4.
DR ExpressionAtlas; Q01IS7; differential.
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 GO; GO:0052576; P:carbohydrate storage; IEA:EnsemblPlants.
DR GO; GO:0042742; P:defense response to bacterium; IEA:EnsemblPlants.
DR GO; GO:0050832; P:defense response to fungus; IEA:EnsemblPlants.
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..25
FT /evidence="ECO:0000255"
FT CHAIN 26..598
FT /note="Beta-fructofuranosidase, insoluble isoenzyme 2"
FT /id="PRO_0000303011"
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"
FT CONFLICT 40
FT /note="A -> T (in Ref. 1; AAQ24868)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="M -> V (in Ref. 1; AAQ24868)"
FT /evidence="ECO:0000305"
FT CONFLICT 501
FT /note="C -> R (in Ref. 1; AAQ24868)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 598 AA; 66233 MW; 9F1AF7F8AFA19D82 CRC64;
MGVLGSRVAW AWLVQLLLLQ QLAGASHVVY DDLELQAAAA 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
