INV4_ARATH
ID INV4_ARATH Reviewed; 591 AA.
AC Q8W413; Q8L5V2; Q9SJN5;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Beta-fructofuranosidase, insoluble isoenzyme CWINV4;
DE EC=3.2.1.26;
DE AltName: Full=Beta-fructofuranosidase 6;
DE Short=AtFruct6;
DE AltName: Full=Cell wall beta-fructosidase 4;
DE AltName: Full=Cell wall invertase 4;
DE Short=AtcwINV4;
DE AltName: Full=Sucrose hydrolase 4;
DE Flags: Precursor;
GN Name=CWINV4; Synonyms=FRUCT6; OrderedLocusNames=At2g36190;
GN ORFNames=F9C22.8;
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].
RA Toyomasu T., Sasaki S., Mitsuhasi W.;
RT "acid invertase gene No. 6 from Arabidopsis.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) 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).
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 flowers, and seeds, and, to a lower
CC extent, in seedlings. {ECO:0000269|PubMed:12508063}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
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DR EMBL; AB049617; BAB83031.1; -; mRNA.
DR EMBL; AC006921; AAD21446.2; -; Genomic_DNA.
DR EMBL; AC007135; AAM15406.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09214.1; -; Genomic_DNA.
DR EMBL; AY084792; AAM61359.1; -; mRNA.
DR PIR; G84777; G84777.
DR RefSeq; NP_565837.1; NM_129177.3.
DR AlphaFoldDB; Q8W413; -.
DR SMR; Q8W413; -.
DR STRING; 3702.AT2G36190.1; -.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
DR PaxDb; Q8W413; -.
DR PRIDE; Q8W413; -.
DR ProteomicsDB; 248510; -.
DR EnsemblPlants; AT2G36190.1; AT2G36190.1; AT2G36190.
DR GeneID; 818191; -.
DR Gramene; AT2G36190.1; AT2G36190.1; AT2G36190.
DR KEGG; ath:AT2G36190; -.
DR Araport; AT2G36190; -.
DR TAIR; locus:2049445; AT2G36190.
DR eggNOG; KOG0228; Eukaryota.
DR HOGENOM; CLU_001528_6_0_1; -.
DR InParanoid; Q8W413; -.
DR OMA; TPKMNAP; -.
DR OrthoDB; 405663at2759; -.
DR PhylomeDB; Q8W413; -.
DR BRENDA; 3.2.1.26; 399.
DR PRO; PR:Q8W413; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8W413; baseline and differential.
DR Genevisible; Q8W413; AT.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0004575; F:sucrose alpha-glucosidase activity; IMP:TAIR.
DR GO; GO:0071836; P:nectar secretion; IMP:TAIR.
DR GO; GO:0048481; P:plant ovule development; IMP:TAIR.
DR GO; GO:0005982; P:starch metabolic process; IMP:TAIR.
DR GO; GO:0005987; P:sucrose catabolic process; 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 Apoplast; Cell wall; Disulfide bond; Glycoprotein; Glycosidase; Hydrolase;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..591
FT /note="Beta-fructofuranosidase, insoluble isoenzyme CWINV4"
FT /id="PRO_0000348350"
FT ACT_SITE 64
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT BINDING 61..64
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 123..124
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 187..188
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 242
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 276
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 472
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 436..484
FT /evidence="ECO:0000250"
FT CONFLICT 134
FT /note="G -> V (in Ref. 4; AAM61359)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="P -> R (in Ref. 4; AAM61359)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 591 AA; 67413 MW; 2886EE8BC024E511 CRC64;
MAISNVISVL LLLLVLINLS NQNIKGIDAF HQIYEELQSE SVESVNHLHR PSFHFQPPKH
WINDPNGPVY YKGLYHLFYQ YNTKGAVWGN IIWAHSVSKD LVNWEALEPA LSPSKWFDIG
GTWSGSITIV PGKGPIILYT GVNQNETQLQ NYAIPEDPSD PYLRKWIKPD DNPIAIPDYT
MNGSAFRDPT TAWFSKDGHW RTVVGSKRKR RGIAYIYRSR DFKHWVKAKH PVHSKQSTGM
WECPDFFPVS LTDFRNGLDL DYVGPNTKHV LKVSLDITRY EYYTLGKYDL KKDRYIPDGN
TPDGWEGLRF DYGNFYASKT FFDYKKNRRI LWGWANESDT VEDDILKGWA GLQVIPRTVL
LDSSKKQLVF WPVEEIESLR GNYVRMNNHD IKMGQRIEVK GITPAQADVE VTFYVGSLEK
AEIFDPSFTW KPLELCNIKG SNVRGGVGPF GLITLATPDL EEYTPVFFRV FNDTKTHKPK
VLMCSDARPS SLKQDTGLLA KDRMYKPSFA GFVDVDMADG RISLRSLIDH SVVESFGALG
KTVITSRVYP VKAVKENAHL YVFNNGTQTV TIESLNAWNM DRPLQMNDGA L
