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Alkaline/neutral invertase CINV1 (EC 3.2.1.26) (Alkaline/neutral invertase G) (A/N-INVG) (Cytosolic invertase 1) (AtCYT-INV1)

 CINV1_ARATH             Reviewed;         551 AA.
Q9LQF2;
01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
30-AUG-2017, entry version 111.
RecName: Full=Alkaline/neutral invertase CINV1 {ECO:0000305};
EC=3.2.1.26 {ECO:0000269|PubMed:21441406};
AltName: Full=Alkaline/neutral invertase G {ECO:0000305};
Short=A/N-INVG {ECO:0000303|PubMed:21441406};
AltName: Full=Cytosolic invertase 1 {ECO:0000303|PubMed:17508130};
Short=AtCYT-INV1 {ECO:0000303|PubMed:17508130};
Name=CINV1 {ECO:0000303|PubMed:17508130};
Synonyms=INVG {ECO:0000303|PubMed:21441406};
OrderedLocusNames=At1g35580; ORFNames=F15O4.33;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
INTERACTION WITH PIP5K9, SUBCELLULAR LOCATION, AND DISRUPTION
PHENOTYPE.
STRAIN=cv. Columbia; TISSUE=Root;
PubMed=17220200; DOI=10.1105/tpc.106.045658;
Lou Y., Gou J.Y., Xue H.W.;
"PIP5K9, an Arabidopsis phosphatidylinositol monophosphate kinase,
interacts with a cytosolic invertase to negatively regulate sugar-
mediated root growth.";
Plant Cell 19:163-181(2007).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, INDUCTION
BY MANNITOL, AND DISRUPTION PHENOTYPE.
PubMed=17508130; DOI=10.1007/s11103-007-9177-4;
Qi X., Wu Z., Li J., Mo X., Wu S., Chu J., Wu P.;
"AtCYT-INV1, a neutral invertase, is involved in osmotic stress-
induced inhibition on lateral root growth in Arabidopsis.";
Plant Mol. Biol. 64:575-587(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-14; SER-61;
THR-70 AND SER-547, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Root;
PubMed=18433157; DOI=10.1021/pr8000173;
de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C.,
Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C.,
Hirt H.;
"Site-specific phosphorylation profiling of Arabidopsis proteins by
mass spectrometry and peptide chip analysis.";
J. Proteome Res. 7:2458-2470(2008).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-70, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. Columbia;
PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,
Andreasson E., Rathjen J.P., Peck S.C.;
"Phosphoproteomic analysis of nuclei-enriched fractions from
Arabidopsis thaliana.";
J. Proteomics 72:439-451(2009).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; SER-61 AND THR-70,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19376835; DOI=10.1104/pp.109.138677;
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
Grossmann J., Gruissem W., Baginsky S.;
"Large-scale Arabidopsis phosphoproteome profiling reveals novel
chloroplast kinase substrates and phosphorylation networks.";
Plant Physiol. 150:889-903(2009).
[9]
FUNCTION.
PubMed=19470642; DOI=10.1073/pnas.0900689106;
Barratt D.H., Derbyshire P., Findlay K., Pike M., Wellner N., Lunn J.,
Feil R., Simpson C., Maule A.J., Smith A.M.;
"Normal growth of Arabidopsis requires cytosolic invertase but not
sucrose synthase.";
Proc. Natl. Acad. Sci. U.S.A. 106:13124-13129(2009).
[10]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
SUBCELLULAR LOCATION, INDUCTION BY HYDROGEN PEROXIDE, GENE FAMILY, AND
DISRUPTION PHENOTYPE.
PubMed=21441406; DOI=10.1093/jxb/err069;
Xiang L., Le Roy K., Bolouri-Moghaddam M.R., Vanhaecke M., Lammens W.,
Rolland F., Van den Ende W.;
"Exploring the neutral invertase-oxidative stress defence connection
in Arabidopsis thaliana.";
J. Exp. Bot. 62:3849-3862(2011).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
-!- FUNCTION: Cytosolic invertase that specifically cleaves sucrose
into glucose and fructose and is involved in the regulation of
multiple tissue development including primary root elongation,
root hair growth, leaf and silique development, and floral
transition. Is involved in osmotic stress-induced inhibition on
lateral root growth by controlling the concentration of hexose in
cells. May regulate sugar-mediated root development by controlling
sucrose catabolism in root cells. {ECO:0000269|PubMed:17220200,
ECO:0000269|PubMed:17508130, ECO:0000269|PubMed:19470642,
ECO:0000269|PubMed:21441406}.
-!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing beta-D-
fructofuranoside residues in beta-D-fructofuranosides.
{ECO:0000269|PubMed:21441406}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=18.4 mM for sucrose {ECO:0000269|PubMed:17220200,
ECO:0000269|PubMed:17508130};
KM=8.4 mM for sucrose {ECO:0000269|PubMed:21441406};
pH dependence:
Optimum pH is 7.0-8.0. {ECO:0000269|PubMed:17220200,
ECO:0000269|PubMed:17508130, ECO:0000269|PubMed:21441406};
-!- SUBUNIT: Interacts with PIP5K9. Interaction with PIP5K9 represses
CINV1 activity. {ECO:0000269|PubMed:17220200}.
-!- INTERACTION:
Q8L850:PIP5K9; NbExp=6; IntAct=EBI-2008033, EBI-2008013;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:21441406}. Nucleus
{ECO:0000269|PubMed:17220200}. Note=Detected in membrane and
nucleus when associated with PIP5K9.
{ECO:0000269|PubMed:17220200}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=A number of isoforms are produced. According to EST
sequences.;
Name=1;
IsoId=Q9LQF2-1; Sequence=Displayed;
-!- TISSUE SPECIFICITY: Expressed in radicle, hypocotyls, root tips
and vascular cylinder, leaf vasculature, shoot stipules,
trichomes, stem, stigma apex and base of siliques.
{ECO:0000269|PubMed:17508130}.
-!- INDUCTION: Induced by mannitol in roots (PubMed:17508130). Induced
by hydrogen peroxide (PubMed:21441406).
{ECO:0000269|PubMed:17508130, ECO:0000269|PubMed:21441406}.
-!- DISRUPTION PHENOTYPE: Reduced primary root length and increased
length and number of lateral roots. Reduced plant growth and early
flowering. Reduced seedling levels of glucose and fructose, but
increased levels of sucrose. {ECO:0000269|PubMed:17220200,
ECO:0000269|PubMed:17508130, ECO:0000269|PubMed:21441406}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 100 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AM230708; CAJ76698.1; -; mRNA.
EMBL; AC007887; AAF79356.1; -; Genomic_DNA.
EMBL; CP002684; AEE31812.1; -; Genomic_DNA.
EMBL; CP002684; AEE31813.1; -; Genomic_DNA.
EMBL; AY065247; AAL38723.1; -; mRNA.
EMBL; AY142662; AAN13200.1; -; mRNA.
PIR; A86477; A86477.
RefSeq; NP_174791.2; NM_103255.2. [Q9LQF2-1]
RefSeq; NP_849750.1; NM_179419.4. [Q9LQF2-1]
UniGene; At.28624; -.
UniGene; At.74775; -.
ProteinModelPortal; Q9LQF2; -.
SMR; Q9LQF2; -.
BioGrid; 25686; 11.
IntAct; Q9LQF2; 3.
STRING; 3702.AT1G35580.1; -.
CAZy; GH100; Glycoside Hydrolase Family 100.
iPTMnet; Q9LQF2; -.
PaxDb; Q9LQF2; -.
PRIDE; Q9LQF2; -.
EnsemblPlants; AT1G35580.1; AT1G35580.1; AT1G35580. [Q9LQF2-1]
EnsemblPlants; AT1G35580.2; AT1G35580.2; AT1G35580. [Q9LQF2-1]
GeneID; 840454; -.
Gramene; AT1G35580.1; AT1G35580.1; AT1G35580.
Gramene; AT1G35580.2; AT1G35580.2; AT1G35580.
KEGG; ath:AT1G35580; -.
Araport; AT1G35580; -.
TAIR; locus:2014676; AT1G35580.
eggNOG; ENOG410IVHI; Eukaryota.
eggNOG; ENOG410XPYN; LUCA.
HOGENOM; HOG000232531; -.
InParanoid; Q9LQF2; -.
OMA; IRETDNI; -.
OrthoDB; EOG0936057R; -.
PhylomeDB; Q9LQF2; -.
PRO; PR:Q9LQF2; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q9LQF2; baseline and differential.
Genevisible; Q9LQF2; AT.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0016020; C:membrane; IDA:TAIR.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0004564; F:beta-fructofuranosidase activity; IDA:TAIR.
GO; GO:0033926; F:glycopeptide alpha-N-acetylgalactosaminidase activity; IEA:InterPro.
GO; GO:0004575; F:sucrose alpha-glucosidase activity; IDA:TAIR.
GO; GO:0005975; P:carbohydrate metabolic process; IMP:TAIR.
GO; GO:0006520; P:cellular amino acid metabolic process; IMP:TAIR.
GO; GO:0042542; P:response to hydrogen peroxide; IEP:TAIR.
GO; GO:0048364; P:root development; IMP:TAIR.
GO; GO:0005987; P:sucrose catabolic process; IDA:TAIR.
InterPro; IPR008928; 6-hairpin_glycosidase-like.
InterPro; IPR024746; Glyco_hydro_100.
Pfam; PF12899; Glyco_hydro_100; 1.
SUPFAM; SSF48208; SSF48208; 2.
1: Evidence at protein level;
Acetylation; Alternative splicing; Carbohydrate metabolism;
Complete proteome; Cytoplasm; Glycosidase; Hydrolase; Nucleus;
Phosphoprotein; Reference proteome.
CHAIN 1 551 Alkaline/neutral invertase CINV1.
/FTId=PRO_0000422134.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22223895}.
MOD_RES 11 11 Phosphoserine.
{ECO:0000244|PubMed:18433157}.
MOD_RES 14 14 Phosphoserine.
{ECO:0000244|PubMed:18433157}.
MOD_RES 44 44 Phosphoserine.
{ECO:0000244|PubMed:19376835}.
MOD_RES 61 61 Phosphoserine.
{ECO:0000244|PubMed:18433157,
ECO:0000244|PubMed:19376835}.
MOD_RES 70 70 Phosphothreonine.
{ECO:0000244|PubMed:18433157,
ECO:0000244|PubMed:19245862,
ECO:0000244|PubMed:19376835}.
MOD_RES 547 547 Phosphoserine.
{ECO:0000244|PubMed:18433157}.
SEQUENCE 551 AA; 62834 MW; 8FE2EF4BC4DFC91F CRC64;
MEGVGLRAVG SHCSLSEMDD LDLTRALDKP RLKIERKRSF DERSMSELST GYSRHDGIHD
SPRGRSVLDT PLSSARNSFE PHPMMAEAWE ALRRSMVFFR GQPVGTLAAV DNTTDEVLNY
DQVFVRDFVP SALAFLMNGE PDIVKHFLLK TLQLQGWEKR VDRFKLGEGV MPASFKVLHD
PIRETDNIVA DFGESAIGRV APVDSGFWWI ILLRAYTKST GDLTLSETPE CQKGMKLILS
LCLAEGFDTF PTLLCADGCS MIDRRMGVYG YPIEIQALFF MALRSALSML KPDGDGREVI
ERIVKRLHAL SFHMRNYFWL DHQNLNDIYR FKTEEYSHTA VNKFNVMPDS IPEWVFDFMP
LRGGYFVGNV GPAHMDFRWF ALGNCVSILS SLATPDQSMA IMDLLEHRWA ELVGEMPLKI
CYPCLEGHEW RIVTGCDPKN TRWSYHNGGS WPVLLWQLTA ACIKTGRPQI ARRAVDLIES
RLHRDCWPEY YDGKLGRYVG KQARKYQTWS IAGYLVAKML LEDPSHIGMI SLEEDKLMKP
VIKRSASWPQ L


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