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Protein

Alkaline/neutral invertase CINV2

Gene

CINV2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Cytosolic invertase that may cleave sucrose into glucose and fructose, and that is involved in the regulation of root growth. May regulate sugar-mediated root development by controlling sucrose catabolism in root cells.1 Publication

Catalytic activityi

Hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides.1 Publication

GO - Molecular functioni

  • beta-fructofuranosidase activity Source: TAIR
  • glycopeptide alpha-N-acetylgalactosaminidase activity Source: InterPro
  • sucrose alpha-glucosidase activity Source: UniProtKB-EC

GO - Biological processi

  • root development Source: TAIR
  • sucrose catabolic process Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Enzyme and pathway databases

BioCyciMetaCyc:AT4G09510-MONOMER.

Protein family/group databases

CAZyiGH100. Glycoside Hydrolase Family 100.

Names & Taxonomyi

Protein namesi
Recommended name:
Alkaline/neutral invertase CINV2Curated (EC:3.2.1.261 Publication)
Alternative name(s):
Alkaline/neutral invertase ICurated
Short name:
A/N-INVI1 Publication
Cytosolic invertase 21 Publication
Gene namesi
Name:CINV21 Publication
Synonyms:INVI1 Publication
Ordered Locus Names:At4g09510
ORF Names:T15G18.70
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G09510.

Subcellular locationi

  • Cytoplasmcytosol By similarity

GO - Cellular componenti

  • cytosol Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 558558Alkaline/neutral invertase CINV2PRO_0000422135Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei16 – 161PhosphoserineBy similarity
Modified residuei19 – 191PhosphoserineBy similarity
Modified residuei50 – 501PhosphoserineBy similarity
Modified residuei79 – 791PhosphothreonineBy similarity
Modified residuei555 – 5551PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ67XD9.
PRIDEiQ67XD9.

PTM databases

iPTMnetiQ67XD9.

Expressioni

Gene expression databases

GenevisibleiQ67XD9. AT.

Interactioni

Protein-protein interaction databases

BioGridi11834. 1 interaction.
STRINGi3702.AT4G09510.1.

Structurei

3D structure databases

ProteinModelPortaliQ67XD9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 100 family.Curated

Phylogenomic databases

eggNOGiENOG410IVHI. Eukaryota.
ENOG410XPYN. LUCA.
HOGENOMiHOG000232531.
InParanoidiQ67XD9.
OMAiCIESHEW.
PhylomeDBiQ67XD9.

Family and domain databases

InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR024746. Glyco_hydro_100.
[Graphical view]
PfamiPF12899. Glyco_hydro_100. 1 hit.
[Graphical view]
SUPFAMiSSF48208. SSF48208. 2 hits.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q67XD9-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEEGHKEPLV LRVEGSHCSL SEMDDFDLTR ALEKPRQLKI ERKRSFDERS
60 70 80 90 100
MSELSTGYVR QDSILEMAHS PGSRSMVDTP LSVRNSFEPH PMVAEAWEAL
110 120 130 140 150
RRSMVFFRGQ PVGTIAAYDH ASEEVLNYDQ VFVRDFVPSA LAFLMNGEPD
160 170 180 190 200
IVKNFLLKTL QLQGWEKRVD RFKLGEGVMP ASFKVLHDPV RKTDTIIADF
210 220 230 240 250
GESAIGRVAP VDSGFWWIIL LRAYTKSTGD LTLSETPECQ RGMRLILSLC
260 270 280 290 300
LSEGFDTFPT LLCADGCSMV DRRMGVYGYP IEIQALFFMA LRCALSMLKP
310 320 330 340 350
DEEGRDFIER IVKRLHALSF HMRSYFWLDF QQLNDIYRYK TEEYSHTAVN
360 370 380 390 400
KFNVMPDSIP DWVFDFMPLR GGYFVGNVSP ARMDFRWFSL GNCVSILSSL
410 420 430 440 450
ATPDQSMAIM DLLEHRWEEL VGEMPLKICY PCIESHEWRI VTGCDPKNTR
460 470 480 490 500
WSYHNGGSWP VLLWTLTAAC IKTGRPQIAR RAIDLIESRL HRDCWPEYYD
510 520 530 540 550
GKQGRYVGKQ ARKYQTWSIA GYLVAKMMLE DPSHIGMISL EEDKQMKPVI

KRSASWTC
Length:558
Mass (Da):64,233
Last modified:October 11, 2004 - v1
Checksum:i9472E6AEB1D3AB8A
GO
Isoform 2 (identifier: Q67XD9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     461-461: V → G
     462-558: Missing.

Note: No experimental confirmation available.
Show »
Length:461
Mass (Da):52,950
Checksum:iD09A81D8F986D417
GO

Sequence cautioni

The sequence CAB78074.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei461 – 4611V → G in isoform 2. 1 PublicationVSP_046440
Alternative sequencei462 – 55897Missing in isoform 2. 1 PublicationVSP_046441Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL161515 Genomic DNA. Translation: CAB78074.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE82759.1.
CP002687 Genomic DNA. Translation: AEE82760.1.
AK176880 mRNA. Translation: BAD44643.1.
BT028983 mRNA. Translation: ABI93892.1.
PIRiA85097.
RefSeqiNP_567347.1. NM_117019.4. [Q67XD9-1]
NP_974525.1. NM_202796.2. [Q67XD9-2]
UniGeneiAt.33690.

Genome annotation databases

EnsemblPlantsiAT4G09510.1; AT4G09510.1; AT4G09510. [Q67XD9-1]
GeneIDi826535.
KEGGiath:AT4G09510.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL161515 Genomic DNA. Translation: CAB78074.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE82759.1.
CP002687 Genomic DNA. Translation: AEE82760.1.
AK176880 mRNA. Translation: BAD44643.1.
BT028983 mRNA. Translation: ABI93892.1.
PIRiA85097.
RefSeqiNP_567347.1. NM_117019.4. [Q67XD9-1]
NP_974525.1. NM_202796.2. [Q67XD9-2]
UniGeneiAt.33690.

3D structure databases

ProteinModelPortaliQ67XD9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi11834. 1 interaction.
STRINGi3702.AT4G09510.1.

Protein family/group databases

CAZyiGH100. Glycoside Hydrolase Family 100.

PTM databases

iPTMnetiQ67XD9.

Proteomic databases

PaxDbiQ67XD9.
PRIDEiQ67XD9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G09510.1; AT4G09510.1; AT4G09510. [Q67XD9-1]
GeneIDi826535.
KEGGiath:AT4G09510.

Organism-specific databases

TAIRiAT4G09510.

Phylogenomic databases

eggNOGiENOG410IVHI. Eukaryota.
ENOG410XPYN. LUCA.
HOGENOMiHOG000232531.
InParanoidiQ67XD9.
OMAiCIESHEW.
PhylomeDBiQ67XD9.

Enzyme and pathway databases

BioCyciMetaCyc:AT4G09510-MONOMER.

Miscellaneous databases

PROiQ67XD9.

Gene expression databases

GenevisibleiQ67XD9. AT.

Family and domain databases

InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR024746. Glyco_hydro_100.
[Graphical view]
PfamiPF12899. Glyco_hydro_100. 1 hit.
[Graphical view]
SUPFAMiSSF48208. SSF48208. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: cv. Columbia.
  4. "Arabidopsis ORF clones."
    Kim C.J., Chen H., Quinitio C., Shinn P., Ecker J.R.
    Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Strain: cv. Columbia.
  5. Cited for: FUNCTION, CATALYTIC ACTIVITY.
  6. "Exploring the neutral invertase-oxidative stress defence connection in Arabidopsis thaliana."
    Xiang L., Le Roy K., Bolouri-Moghaddam M.R., Vanhaecke M., Lammens W., Rolland F., Van den Ende W.
    J. Exp. Bot. 62:3849-3862(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY.

Entry informationi

Entry nameiCINV2_ARATH
AccessioniPrimary (citable) accession number: Q67XD9
Secondary accession number(s): Q08A96, Q9M0P2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2013
Last sequence update: October 11, 2004
Last modified: January 20, 2016
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.