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INV7_ORYSJ
ID   INV7_ORYSJ              Reviewed;         596 AA.
AC   Q0J360; A0A0P0XL00; Q56UC9; Q56UM5; Q6K311; Q9XGV7;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Beta-fructofuranosidase, insoluble isoenzyme 7;
DE            EC=3.2.1.26;
DE   AltName: Full=Cell wall beta-fructosidase 7;
DE   AltName: Full=Invertase 7;
DE   AltName: Full=OsCIN7;
DE   AltName: Full=Sucrose hydrolase 7;
DE   Flags: Precursor;
GN   Name=CIN7; Synonyms=INV1; OrderedLocusNames=Os09g0255000, LOC_Os09g08072;
GN   ORFNames=OSJNBb0066C12.30;
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;
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=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   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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   [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.
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   -!- 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 15 days after flowering.
CC       {ECO:0000269|PubMed:11978873, ECO:0000269|PubMed:15701658,
CC       ECO:0000269|PubMed:15759120}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
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DR   EMBL; AY578164; AAT84407.1; -; mRNA.
DR   EMBL; AP005738; BAD23559.1; -; Genomic_DNA.
DR   EMBL; AP008215; BAF24605.1; -; Genomic_DNA.
DR   EMBL; AP014965; BAT07071.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0J360; -.
DR   SMR; Q0J360; -.
DR   STRING; 4530.OS09T0255000-01; -.
DR   CAZy; GH32; Glycoside Hydrolase Family 32.
DR   PaxDb; Q0J360; -.
DR   PRIDE; Q0J360; -.
DR   EnsemblPlants; Os09t0255000-01; Os09t0255000-01; Os09g0255000.
DR   Gramene; Os09t0255000-01; Os09t0255000-01; Os09g0255000.
DR   eggNOG; KOG0228; Eukaryota.
DR   HOGENOM; CLU_001528_6_0_1; -.
DR   InParanoid; Q0J360; -.
DR   OMA; MYYNGMY; -.
DR   PlantReactome; R-OSA-1119626; Fructan degradation.
DR   Proteomes; UP000000763; Chromosome 9.
DR   Proteomes; UP000059680; Chromosome 9.
DR   Genevisible; Q0J360; 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; 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.
PE   2: Evidence at transcript level;
KW   Apoplast; Cell wall; Disulfide bond; Glycoprotein; Glycosidase; Hydrolase;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..596
FT                   /note="Beta-fructofuranosidase, insoluble isoenzyme 7"
FT                   /id="PRO_0000033384"
FT   ACT_SITE        54
FT                   /evidence="ECO:0000250"
FT   BINDING         51..54
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         70
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         78
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         115..116
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         179..180
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         234
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        82
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        330
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        552
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        432..478
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   596 AA;  65490 MW;  27F11888D23A1CE1 CRC64;
     MARLGLAVCA ASFHLFLLLA STSSLRRAPT EADTANHARR TAYHFQPAKN WQNDPNGPMY
     HNGMYHLFYQ YNPHSALWDI GNLSWGHSVS GDLLNWAALD TALDPTSPFD ANGCWSGSAT
     ILPGALPAIL YTGIDASKEQ VQNVAFAKNP SDPLLREWEK PAYNPVIALP ADVPGDKFRD
     PSTAWLGRDG LWRIAVSAEV DGVASTLVYR SKDFVRWERN AAPLHASRAA GMVECPDLFP
     VAERGEDGLD TSANGAGGVR HVLKLSVMDT LQDYYMVGTY DDAADAFSPA EPERGDDCRS
     WRRLDYGHVY ASKSFFDVRK NRRVLWAWAN ESDSQADDVA RGWSGVQTFP RKMWLAKDGK
     QLLQWPIEEI KTLRRKRAGL WQGTRLGAGA VQEIVGVASS QADVEVVFKI PSLEEAERVD
     DPNRLLDPQK LCGEKGAAVR GGVGPFGLLV MASGDLHEHT AVFFRVFRHH DKYKLLMCTD
     LTKSSTRAGV YKPAYGGFVD MDIDDHKTIS LRTLIDHSVV ESFGGGGRAC ITARVYPEHV
     ATSSSHLYVF NNGSDAVKVA KLEAWDLATA TVNVVVGDHH GLVAPALELE PTRTTQ
 
 
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