INV2_ARATH
ID INV2_ARATH Reviewed; 590 AA.
AC Q1PEF8; A0MF24; Q38801; Q8GXA3; Q9SVE0;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Beta-fructofuranosidase, insoluble isoenzyme CWINV2;
DE EC=3.2.1.26;
DE AltName: Full=Cell wall beta-fructosidase 2;
DE Short=AtbetaFRUCT2;
DE AltName: Full=Cell wall invertase 2;
DE Short=AtcwINV2;
DE AltName: Full=Sucrose hydrolase 2;
DE Flags: Precursor;
GN Name=CWINV2; Synonyms=BFRUCT2; OrderedLocusNames=At3g52600;
GN ORFNames=F22O6.20, F3C22.4;
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 [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Mercier R.W., Gogarten J.;
RT "A second cell wall invertase encoding gene in Arabidopsis thaliana.";
RL Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [6]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=9951726; DOI=10.1007/s004250050481;
RA Tymowska-Lalanne Z., Kreis M.;
RT "Expression of the Arabidopsis thaliana invertase gene family.";
RL Planta 207:259-265(1998).
RN [7]
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).
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 -!- 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=Q1PEF8-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in flowers, and seeds.
CC {ECO:0000269|PubMed:12508063, ECO:0000269|PubMed:9951726}.
CC -!- INDUCTION: By aeroponic growth condition, darkness, sucrose, glucose
CC and mannitol. {ECO:0000269|PubMed:9951726}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK28599.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB43403.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U11033; AAA63802.1; -; Genomic_DNA.
DR EMBL; AL050300; CAB43403.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE78967.1; -; Genomic_DNA.
DR EMBL; AK118343; BAC42957.1; -; mRNA.
DR EMBL; DQ446760; ABE66012.1; -; mRNA.
DR EMBL; DQ653148; ABK28599.1; ALT_SEQ; mRNA.
DR PIR; T08439; T08439.
DR RefSeq; NP_190828.2; NM_115120.4. [Q1PEF8-1]
DR AlphaFoldDB; Q1PEF8; -.
DR SMR; Q1PEF8; -.
DR STRING; 3702.AT3G52600.1; -.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
DR PaxDb; Q1PEF8; -.
DR PRIDE; Q1PEF8; -.
DR ProteomicsDB; 247177; -. [Q1PEF8-1]
DR EnsemblPlants; AT3G52600.1; AT3G52600.1; AT3G52600. [Q1PEF8-1]
DR GeneID; 824426; -.
DR Gramene; AT3G52600.1; AT3G52600.1; AT3G52600. [Q1PEF8-1]
DR KEGG; ath:AT3G52600; -.
DR Araport; AT3G52600; -.
DR TAIR; locus:2079944; AT3G52600.
DR eggNOG; KOG0228; Eukaryota.
DR InParanoid; Q1PEF8; -.
DR OrthoDB; 405663at2759; -.
DR PhylomeDB; Q1PEF8; -.
DR BioCyc; ARA:AT3G52600-MON; -.
DR PRO; PR:Q1PEF8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q1PEF8; baseline and differential.
DR Genevisible; Q1PEF8; AT.
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:0048481; P:plant ovule development; IMP:TAIR.
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 Alternative splicing; Apoplast; Cell wall; Disulfide bond; Glycoprotein;
KW Glycosidase; Hydrolase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..590
FT /note="Beta-fructofuranosidase, insoluble isoenzyme CWINV2"
FT /id="PRO_0000348348"
FT ACT_SITE 62
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT BINDING 59..62
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 121..122
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 185..186
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 241
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 275
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 564
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 435..483
FT /evidence="ECO:0000250"
FT CONFLICT 256
FT /note="G -> R (in Ref. 1; AAA63802)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="G -> S (in Ref. 4; BAC42957)"
FT /evidence="ECO:0000305"
FT CONFLICT 590
FT /note="K -> KG (in Ref. 5; ABK28599)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 590 AA; 66823 MW; 6B2336244D065E06 CRC64;
MSAPKFGYVL LLIVLINISN NGVDAFHKVF KKLQSKSTSL ESVSPLHRTA YHFQPPRHWI
NDPNAPMLYK GVYHLFYQYN PKGAVWGNIV WAHSVSKDLI NWEALEPAIY PSKWFDINGT
WSGSATHVPG KGPVILYTGI TENQTQIQNY AIPQDLSDPY LKTWIKPDDN PIVKPDNGEN
GSAFRDPTTA WFNKKDGYWR MLVGSKRKNR GIAYMYKSRD FKKWVKSKRP IHSRKKTGMW
ECPDFFPVSV TDKKNGLDFS YDGPNAKHVL KVSLDLTRYE YYTLGTYDTK KDRYRPDGYT
PDGWDGLRFD YGNYYASKTF FDDKTNRRIL WGWANESDTV QDDTVKGWAG IQLIPRTILL
DSSGKQLVFW PIEEIESLRG KNVQMTNQKM EMGQRFEVQG ITPAQVDVDV TFNVGNLEKA
EKFDESFATK PLELCNLKGS NVNGGVGPFG LITLATSDLE EYTPVFFRVF KDAASNKPKV
LMCSDAKPSS LKKDTGTDAK ERMYKPSFAG FVDVGLLDGK ISLRSLIDHS VVESFGAKGK
TVITSRVYPT KAVGEKAHLF VFNNGSQPVT VESLNAWNMQ KPLKMNQGAK
