INV3_ARATH
ID INV3_ARATH Reviewed; 594 AA.
AC Q67XZ3; Q9C721; Q9SLS5;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Beta-fructofuranosidase, insoluble isoenzyme CWINV3;
DE AltName: Full=6-fructan exohydrolase;
DE Short=6-FEH;
DE EC=3.2.1.80;
DE AltName: Full=Beta-fructofuranosidase 5;
DE Short=AtFruct5;
DE AltName: Full=Cell wall beta-fructosidase 3;
DE AltName: Full=Cell wall invertase 3;
DE Short=AtcwINV3;
DE AltName: Full=Sucrose hydrolase 3;
DE Flags: Precursor;
GN Name=CWINV3; Synonyms=FRUCT5; OrderedLocusNames=At1g55120;
GN ORFNames=T7N22.6;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Landsberg erecta;
RA Toyomasu T., Mitsuhashi W., Sasaki S.;
RT "Arabidopsis acid-invertase, cell wall type.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12508063; DOI=10.1093/jxb/erg055;
RA Sherson S.M., Alford H.L., Forbes S.M., Wallace G., Smith S.M.;
RT "Roles of cell-wall invertases and monosaccharide transporters in the
RT growth and development of Arabidopsis.";
RL J. Exp. Bot. 54:525-531(2003).
RN [6]
RP PROTEIN SEQUENCE OF 40-48; 155-177; 180-211; 266-283; 313-320; 341-350;
RP 374-381; 414-426; 514-529 AND 536-553, AND FUNCTION.
RX DOI=10.1111/j.1365-3040.2004.01281.x;
RA de Coninck B., Le Roy K., Francis I., Clerens S., Vergauwen R.,
RA Halliday A.M., Smith S.M., Van Laere A., Van Den Ende W.;
RT "Arabidopsis AtcwINV3 and 6 are not invertases but are fructan
RT exohydrolases (FEHs) with different substrate specificities.";
RL Plant Cell Environ. 28:432-443(2005).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=16339783; DOI=10.1093/jxb/erj039;
RA Quilliam R.S., Swarbrick P.J., Scholes J.D., Rolfe S.A.;
RT "Imaging photosynthesis in wounded leaves of Arabidopsis thaliana.";
RL J. Exp. Bot. 57:55-69(2006).
CC -!- FUNCTION: 6-fructan exohydrolase that can use phlein, levan,
CC neokestose, levanbiose, 6-kestose, and 1-kestose as substrates.
CC {ECO:0000269|Ref.6}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing (2->1)- and (2->6)-linked
CC beta-D-fructofuranose residues in fructans.; EC=3.2.1.80;
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q67XZ3-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, leaves, flowers, and seeds.
CC {ECO:0000269|PubMed:12508063, ECO:0000269|PubMed:16339783}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
CC -!- CAUTION: Seems to not have any beta-fructofuranosidase activity.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG50837.1; 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; AB029310; BAA89048.1; -; mRNA.
DR EMBL; AC073944; AAG50837.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33186.1; -; Genomic_DNA.
DR EMBL; AK176675; BAD44438.1; -; mRNA.
DR PIR; G96592; G96592.
DR RefSeq; NP_564676.1; NM_104385.4. [Q67XZ3-1]
DR AlphaFoldDB; Q67XZ3; -.
DR SMR; Q67XZ3; -.
DR STRING; 3702.AT1G55120.1; -.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
DR PaxDb; Q67XZ3; -.
DR PRIDE; Q67XZ3; -.
DR ProteomicsDB; 248470; -. [Q67XZ3-1]
DR EnsemblPlants; AT1G55120.1; AT1G55120.1; AT1G55120. [Q67XZ3-1]
DR GeneID; 841955; -.
DR Gramene; AT1G55120.1; AT1G55120.1; AT1G55120. [Q67XZ3-1]
DR KEGG; ath:AT1G55120; -.
DR Araport; AT1G55120; -.
DR TAIR; locus:2205677; AT1G55120.
DR eggNOG; KOG0228; Eukaryota.
DR HOGENOM; CLU_001528_6_0_1; -.
DR InParanoid; Q67XZ3; -.
DR OrthoDB; 405663at2759; -.
DR PhylomeDB; Q67XZ3; -.
DR BioCyc; ARA:AT1G55120-MON; -.
DR BRENDA; 3.2.1.80; 399.
DR PRO; PR:Q67XZ3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q67XZ3; baseline and differential.
DR Genevisible; Q67XZ3; AT.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0051669; F:fructan beta-fructosidase 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 1: Evidence at protein level;
KW Alternative splicing; Apoplast; Cell wall; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..594
FT /note="Beta-fructofuranosidase, insoluble isoenzyme CWINV3"
FT /id="PRO_0000348349"
FT ACT_SITE 53
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT BINDING 50..53
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 113..114
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 179..180
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 428..480
FT /evidence="ECO:0000250"
FT CONFLICT 418..423
FT /note="EPSWTD -> GPELDPI (in Ref. 1; BAA89048)"
FT /evidence="ECO:0000305"
FT CONFLICT 427
FT /note="I -> V (in Ref. 4; BAD44438)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 594 AA; 67068 MW; 813988E1E239FE86 CRC64;
MAKLNRSNIG LSLLLSMFLA NFITDLEASS HQDLNQPYRT GYHFQPLKNW MNDPNGPMIY
KGIYHLFYQY NPYGAVWDVR IVWGHSTSVD LVNWISQPPA FNPSQPSDIN GCWSGSVTIL
PNGKPVILYT GIDQNKGQVQ NVAVPVNISD PYLREWSKPP QNPLMTTNAV NGINPDRFRD
PTTAWLGRDG EWRVIVGSST DDRRGLAILY KSRDFFNWTQ SMKPLHYEDL TGMWECPDFF
PVSITGSDGV ETSSVGENGI KHVLKVSLIE TLHDYYTIGS YDREKDVYVP DLGFVQNESA
PRLDYGKYYA SKTFYDDVKK RRILWGWVNE SSPAKDDIEK GWSGLQSFPR KIWLDESGKE
LLQWPIEEIE TLRGQQVNWQ KKVLKAGSTL QVHGVTAAQA DVEVSFKVKE LEKADVIEPS
WTDPQKICSQ GDLSVMSGLG PFGLMVLASN DMEEYTSVYF RIFKSNDDTN KKTKYVVLMC
SDQSRSSLND ENDKSTFGAF VAIDPSHQTI SLRTLIDHSI VESYGGGGRT CITSRVYPKL
AIGENANLFV FNKGTQSVDI LTLSAWSLKS AQINGDLMSP FIEREESRSP NHQF
