CINV2_ARATH
ID CINV2_ARATH Reviewed; 558 AA.
AC Q67XD9; Q08A96; Q9M0P2;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Alkaline/neutral invertase CINV2 {ECO:0000305};
DE EC=3.2.1.26 {ECO:0000269|PubMed:19470642};
DE AltName: Full=Alkaline/neutral invertase I {ECO:0000305};
DE Short=A/N-INVI {ECO:0000303|PubMed:21441406};
DE AltName: Full=Cytosolic invertase 2 {ECO:0000303|PubMed:19470642};
GN Name=CINV2 {ECO:0000303|PubMed:19470642};
GN Synonyms=INVI {ECO:0000303|PubMed:21441406}; OrderedLocusNames=At4g09510;
GN ORFNames=T15G18.70;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Quinitio C., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=19470642; DOI=10.1073/pnas.0900689106;
RA Barratt D.H., Derbyshire P., Findlay K., Pike M., Wellner N., Lunn J.,
RA Feil R., Simpson C., Maule A.J., Smith A.M.;
RT "Normal growth of Arabidopsis requires cytosolic invertase but not sucrose
RT synthase.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:13124-13129(2009).
RN [6]
RP GENE FAMILY.
RX PubMed=21441406; DOI=10.1093/jxb/err069;
RA Xiang L., Le Roy K., Bolouri-Moghaddam M.R., Vanhaecke M., Lammens W.,
RA Rolland F., Van den Ende W.;
RT "Exploring the neutral invertase-oxidative stress defence connection in
RT Arabidopsis thaliana.";
RL J. Exp. Bot. 62:3849-3862(2011).
CC -!- FUNCTION: Cytosolic invertase that may cleave sucrose into glucose and
CC fructose, and that is involved in the regulation of root growth. May
CC regulate sugar-mediated root development by controlling sucrose
CC catabolism in root cells. {ECO:0000269|PubMed:19470642}.
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:0000269|PubMed:19470642};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9LQF2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q67XD9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q67XD9-2; Sequence=VSP_046440, VSP_046441;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 100 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB78074.1; 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; AL161515; CAB78074.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82759.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82760.1; -; Genomic_DNA.
DR EMBL; AK176880; BAD44643.1; -; mRNA.
DR EMBL; BT028983; ABI93892.1; -; mRNA.
DR PIR; A85097; A85097.
DR RefSeq; NP_567347.1; NM_117019.5. [Q67XD9-1]
DR RefSeq; NP_974525.1; NM_202796.2. [Q67XD9-2]
DR AlphaFoldDB; Q67XD9; -.
DR SMR; Q67XD9; -.
DR BioGRID; 11834; 1.
DR STRING; 3702.AT4G09510.1; -.
DR CAZy; GH100; Glycoside Hydrolase Family 100.
DR iPTMnet; Q67XD9; -.
DR PaxDb; Q67XD9; -.
DR PRIDE; Q67XD9; -.
DR ProteomicsDB; 246849; -. [Q67XD9-1]
DR EnsemblPlants; AT4G09510.1; AT4G09510.1; AT4G09510. [Q67XD9-1]
DR EnsemblPlants; AT4G09510.2; AT4G09510.2; AT4G09510. [Q67XD9-2]
DR GeneID; 826535; -.
DR Gramene; AT4G09510.1; AT4G09510.1; AT4G09510. [Q67XD9-1]
DR Gramene; AT4G09510.2; AT4G09510.2; AT4G09510. [Q67XD9-2]
DR KEGG; ath:AT4G09510; -.
DR Araport; AT4G09510; -.
DR TAIR; locus:2133737; AT4G09510.
DR eggNOG; ENOG502QPS0; Eukaryota.
DR HOGENOM; CLU_020846_1_1_1; -.
DR InParanoid; Q67XD9; -.
DR OMA; HALSFHI; -.
DR OrthoDB; 344496at2759; -.
DR PhylomeDB; Q67XD9; -.
DR BioCyc; MetaCyc:AT4G09510-MON; -.
DR PRO; PR:Q67XD9; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q67XD9; baseline and differential.
DR Genevisible; Q67XD9; AT.
DR GO; GO:0009507; C:chloroplast; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; NAS:TAIR.
DR GO; GO:0004564; F:beta-fructofuranosidase activity; IGI:TAIR.
DR GO; GO:0033926; F:glycopeptide alpha-N-acetylgalactosaminidase activity; IEA:InterPro.
DR GO; GO:0004575; F:sucrose alpha-glucosidase activity; IBA:GO_Central.
DR GO; GO:0048364; P:root development; IGI:TAIR.
DR GO; GO:0005987; P:sucrose catabolic process; IGI:TAIR.
DR Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR024746; Glyco_hydro_100.
DR PANTHER; PTHR31916; PTHR31916; 1.
DR Pfam; PF12899; Glyco_hydro_100; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Carbohydrate metabolism; Cytoplasm; Glycosidase;
KW Hydrolase; Phosphoprotein; Reference proteome.
FT CHAIN 1..558
FT /note="Alkaline/neutral invertase CINV2"
FT /id="PRO_0000422135"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LQF2"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LQF2"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LQF2"
FT MOD_RES 79
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9LQF2"
FT MOD_RES 555
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LQF2"
FT VAR_SEQ 461
FT /note="V -> G (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_046440"
FT VAR_SEQ 462..558
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_046441"
SQ SEQUENCE 558 AA; 64233 MW; 9472E6AEB1D3AB8A CRC64;
MEEGHKEPLV LRVEGSHCSL SEMDDFDLTR ALEKPRQLKI ERKRSFDERS MSELSTGYVR
QDSILEMAHS PGSRSMVDTP LSVRNSFEPH PMVAEAWEAL RRSMVFFRGQ PVGTIAAYDH
ASEEVLNYDQ VFVRDFVPSA LAFLMNGEPD IVKNFLLKTL QLQGWEKRVD RFKLGEGVMP
ASFKVLHDPV RKTDTIIADF GESAIGRVAP VDSGFWWIIL LRAYTKSTGD LTLSETPECQ
RGMRLILSLC LSEGFDTFPT LLCADGCSMV DRRMGVYGYP IEIQALFFMA LRCALSMLKP
DEEGRDFIER IVKRLHALSF HMRSYFWLDF QQLNDIYRYK TEEYSHTAVN KFNVMPDSIP
DWVFDFMPLR GGYFVGNVSP ARMDFRWFSL GNCVSILSSL ATPDQSMAIM DLLEHRWEEL
VGEMPLKICY PCIESHEWRI VTGCDPKNTR WSYHNGGSWP VLLWTLTAAC IKTGRPQIAR
RAIDLIESRL HRDCWPEYYD GKQGRYVGKQ ARKYQTWSIA GYLVAKMMLE DPSHIGMISL
EEDKQMKPVI KRSASWTC
