ID   INV4_ORYSJ              Reviewed;         590 AA.
AC   Q5JJV0; Q0JFR0; Q75SP0;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   24-JAN-2024, entry version 105.
DE   RecName: Full=Beta-fructofuranosidase, insoluble isoenzyme 4;
DE            EC=3.2.1.26;
DE   AltName: Full=Cell wall beta-fructosidase 4;
DE   AltName: Full=Invertase 4;
DE   AltName: Full=OsCIN4;
DE   AltName: Full=Sucrose hydrolase 4;
DE   Flags: Precursor;
GN   Name=CIN4; OrderedLocusNames=Os01g0966700, LOC_Os01g73580;
GN   ORFNames=OsJ_04889 {ECO:0000312|EMBL:EEE56070.1}, P0458E05.32;
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 [MRNA].
RC   STRAIN=cv. Nipponbare; TISSUE=Panicle;
RA   Hirose T., Terao T.;
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12447438; DOI=10.1038/nature01184;
RA   Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA   Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA   Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA   Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA   Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA   Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA   Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA   Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA   Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA   Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA   Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA   Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA   Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT   "The genome sequence and structure of rice chromosome 1.";
RL   Nature 420:312-316(2002).
RN   [4]
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   [5]
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   [6]
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   [7]
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   [8]
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   [9]
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 leaves. Expressed at moderate levels
CC       in roots and flowers, and weakly in seeds.
CC       {ECO:0000269|PubMed:15759120}.
CC   -!- DEVELOPMENTAL STAGE: Expressed from 1 to 10 days after flowering.
CC       {ECO:0000269|PubMed:15701658, ECO:0000269|PubMed:15759120}.
CC   -!- INDUCTION: By rice blast fungus (M.grisea) 12 hours after infection.
CC       {ECO:0000269|PubMed:15759120}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
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DR   EMBL; AY578161; AAT84404.1; -; mRNA.
DR   EMBL; AB154521; BAD05180.1; -; mRNA.
DR   EMBL; AP004365; BAD88258.1; -; Genomic_DNA.
DR   EMBL; AP008207; BAF07418.1; -; Genomic_DNA.
DR   EMBL; AP014957; BAS76386.1; -; Genomic_DNA.
DR   EMBL; CM000138; EEE56070.1; -; Genomic_DNA.
DR   EMBL; AK067444; BAG90423.1; -; mRNA.
DR   RefSeq; XP_015622113.1; XM_015766627.1.
DR   AlphaFoldDB; Q5JJV0; -.
DR   SMR; Q5JJV0; -.
DR   STRING; 39947.Q5JJV0; -.
DR   CAZy; GH32; Glycoside Hydrolase Family 32.
DR   GlyCosmos; Q5JJV0; 5 sites, No reported glycans.
DR   PaxDb; 39947-Q5JJV0; -.
DR   EnsemblPlants; Os01t0966700-01; Os01t0966700-01; Os01g0966700.
DR   GeneID; 4324001; -.
DR   Gramene; Os01t0966700-01; Os01t0966700-01; Os01g0966700.
DR   KEGG; osa:4324001; -.
DR   eggNOG; KOG0228; Eukaryota.
DR   HOGENOM; CLU_001528_6_0_1; -.
DR   InParanoid; Q5JJV0; -.
DR   OMA; GGRACIM; -.
DR   OrthoDB; 315037at2759; -.
DR   PlantReactome; R-OSA-1119626; Fructan degradation.
DR   Proteomes; UP000000763; Chromosome 1.
DR   Proteomes; UP000007752; Chromosome 1.
DR   Proteomes; UP000059680; Chromosome 1.
DR   ExpressionAtlas; Q5JJV0; baseline and 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   CDD; cd18624; GH32_Fruct1-like; 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   PANTHER; PTHR31953:SF68; BETA-FRUCTOFURANOSIDASE, INSOLUBLE ISOENZYME 4; 1.
DR   PANTHER; PTHR31953; BETA-FRUCTOFURANOSIDASE, INSOLUBLE ISOENZYME CWINV1-RELATED; 1.
DR   Pfam; PF08244; Glyco_hydro_32C; 1.
DR   Pfam; PF00251; Glyco_hydro_32N; 1.
DR   SMART; SM00640; Glyco_32; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS00609; GLYCOSYL_HYDROL_F32; 1.
DR   Genevisible; Q5JJV0; OS.
PE   2: Evidence at transcript level;
KW   Apoplast; Cell wall; Disulfide bond; Glycoprotein; Glycosidase; Hydrolase;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..590
FT                   /note="Beta-fructofuranosidase, insoluble isoenzyme 4"
FT                   /id="PRO_0000033382"
FT   ACT_SITE        74
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT   BINDING         71..74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         90
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         98
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         133..134
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         198..199
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         253
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         287
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        94
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        167
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        247
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        345
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        565
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        445..491
FT                   /evidence="ECO:0000250"
FT   CONFLICT        226
FT                   /note="L -> P (in Ref. 2; BAD05180)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   590 AA;  66610 MW;  4999F60849A679E4 CRC64;
     MVMAPIPQPW HQWPFLILFF LVLFSCESNL PCRNGVEATQ RVFLYPQSPK VSSIVSKGYR
     TGYHFQPPKN WINDPNGPMY YNGIYHEFYQ YNPNGSVWGN IVWGHSVSTD LINWIRLEPA
     IEGNTPSDIN GCWTGSATIL TGDQPVIIYT GADTEKRQVQ NIVLPKNRSD PYLREWTKPK
     NNPLIEPVGP GLNSNQFRDP TTGWIGPDGL WRIAVGAELN GYSAALLYKS KDFMQWTRVD
     HPLYSSNASN MWECPDFFAV LPGKNNGLDL SAAIPNGAKH VLKMSLDSCD KYMIGVYDLK
     HDMFVPDTVL DDRRLWLRID YGNYYASKSF FDSKKGRRII WGWTNETDST SDDVAKGWAG
     IHAIPRTIWL DGDGKRLLQW PIEEVESLRR NEVSHQGLEL KKGDLFEIKG TDTLQADVEI
     DFELTSIDAA DPFDPSWLLD TEKHCREADA SVHGGLGPFG LVVLASDNMD EHTTVHFRVY
     KSEQKYMVLL CSDLRRSSLR PGLYTPAYGG FFEYDLEKEK KISLRTLIDR SAVESFGGGG
     RACIMARVYP AAVVDGATHM YAFNNGSSTV KVSQLKAWSM TRAQVNVRKG
//