ID INV6_ARATH Reviewed; 550 AA.
AC Q8W4S6; A8MQQ0; Q9LYI1;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 132.
DE RecName: Full=Beta-fructofuranosidase, insoluble isoenzyme CWINV6;
DE AltName: Full=6 and 1-fructan exohydrolase;
DE Short=6&1-FEH;
DE EC=3.2.1.80;
DE AltName: Full=Cell wall beta-fructosidase 6;
DE AltName: Full=Cell wall invertase 6;
DE Short=AtcwINV6;
DE AltName: Full=Sucrose hydrolase 6;
DE Flags: Precursor;
GN Name=CWINV6; OrderedLocusNames=At5g11920; ORFNames=F14F18.90;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
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 [5]
RP 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).
CC -!- FUNCTION: 6 and 1-fructan exohydrolase that can degrade both inulin and
CC levan-type fructans, such as phlein, levan, neokestose, levanbiose, 6-
CC kestose, 1-kestose, inulin, and 1,1-nystose. {ECO:0000269|Ref.5}.
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=2;
CC Name=1;
CC IsoId=Q8W4S6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8W4S6-2; Sequence=VSP_035148;
CC -!- TISSUE SPECIFICITY: Expressed in seedlings and leaves, and, to a lower
CC extent, in flowers and seeds. {ECO:0000269|PubMed:12508063}.
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=CAB87665.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL163812; CAB87665.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91739.1; -; Genomic_DNA.
DR EMBL; AY060553; AAL31183.1; -; mRNA.
DR EMBL; AY141991; AAM98255.1; -; mRNA.
DR PIR; T48551; T48551.
DR RefSeq; NP_568254.1; NM_121230.3. [Q8W4S6-1]
DR AlphaFoldDB; Q8W4S6; -.
DR SMR; Q8W4S6; -.
DR IntAct; Q8W4S6; 1.
DR STRING; 3702.Q8W4S6; -.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
DR GlyCosmos; Q8W4S6; 2 sites, No reported glycans.
DR PaxDb; 3702-AT5G11920-1; -.
DR EnsemblPlants; AT5G11920.1; AT5G11920.1; AT5G11920. [Q8W4S6-1]
DR GeneID; 831065; -.
DR Gramene; AT5G11920.1; AT5G11920.1; AT5G11920. [Q8W4S6-1]
DR KEGG; ath:AT5G11920; -.
DR Araport; AT5G11920; -.
DR TAIR; AT5G11920; CWINV6.
DR eggNOG; KOG0228; Eukaryota.
DR HOGENOM; CLU_001528_6_0_1; -.
DR InParanoid; Q8W4S6; -.
DR OMA; PEISPCP; -.
DR OrthoDB; 315037at2759; -.
DR PhylomeDB; Q8W4S6; -.
DR BioCyc; ARA:AT5G11920-MONOMER; -.
DR PRO; PR:Q8W4S6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8W4S6; baseline and differential.
DR Genevisible; Q8W4S6; AT.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0051669; F:fructan beta-fructosidase 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; BETA-FRUCTOFURANOSIDASE, INSOLUBLE ISOENZYME CWINV1-RELATED; 1.
DR PANTHER; PTHR31953:SF66; BETA-FRUCTOFURANOSIDASE, INSOLUBLE ISOENZYME CWINV6; 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.
PE 2: Evidence at transcript level;
KW Alternative splicing; Apoplast; Cell wall; Glycoprotein; Glycosidase;
KW Hydrolase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..?
FT /evidence="ECO:0000255"
FT CHAIN ?..550
FT /note="Beta-fructofuranosidase, insoluble isoenzyme CWINV6"
FT /id="PRO_0000348352"
FT ACT_SITE 31
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT BINDING 28..31
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 92..93
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 157..158
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 408..549
FT /note="RDSSVGCVYGPFGLLALASSDLSEQTAIFFKVIRRGNGYAVVMCSSEKRSSL
FT RDNIKKSSHGAFLDIDPRHEKISLRCLIDHSIIESYGVGGKTVITSRVYPKLAIGEAAK
FT LYVFNDGENGVIMTSLEAWSMRNAQINSNPT -> HRSLDYRELRSRRKNCDNI (in
FT isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_035148"
SQ SEQUENCE 550 AA; 62098 MW; E4CE7626CB8922BB CRC64;
MADVMEQNLL QTAVLNRTSF HFQPQRNWLN DPNAPMYYKG FYHLFYQNNP LAPEFSRTRI
IWGHSVSQDM VNWIQLEPAL VPSESFDINS CWSGSATILP DGRPVILYTG LDVNNKQQVT
VVAEPKDVSD PLLREWVKPK YNPVMVPPSN VPFNCFRDPT EAWKGQDGKW RVLIGAKEKD
TEKGMAILYR SDDFVQWTKY PVPLLESEGT GMWECPDFFP VSITGKEGVD TSVNNASVRH
VLKASFGGND CYVIGKYSSE TEDFSADYEF TNTSADLRYD HGTFYASKAF FDSVKNRRIN
WGWVIETDSK EDDFKKGWAG LMTLPREIWM DTSGKKLMQW PIEEINNLRT KSVSLDDCYE
FKTGSTFEIS GITAAQADVE VTFNLPFLEN NPEILDADQV DDATLFDRDS SVGCVYGPFG
LLALASSDLS EQTAIFFKVI RRGNGYAVVM CSSEKRSSLR DNIKKSSHGA FLDIDPRHEK
ISLRCLIDHS IIESYGVGGK TVITSRVYPK LAIGEAAKLY VFNDGENGVI MTSLEAWSMR
NAQINSNPTY
//
