Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 96 (11 Dec 2019)
Sequence version 2 (11 Jan 2001)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Beta-fructofuranosidase, soluble isoenzyme I

Gene

INV*DC4

Organism
Daucus carota (Wild carrot)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

May participate in the regulation of the hexose level in mature tissues and in the utilization of sucrose stored in vacuoles.

Miscellaneous

There are at least three isozymes of beta-fructofuranosidase in carrot: one insoluble and two soluble ones.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • Hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides.PROSITE-ProRule annotation EC:3.2.1.26

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei145PROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei161SubstrateBy similarity1
Binding sitei169SubstrateBy similarity1
Binding sitei323SubstrateBy similarity1
Binding sitei356SubstrateBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionGlycosidase, Hydrolase

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
GH32 Glycoside Hydrolase Family 32

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Beta-fructofuranosidase, soluble isoenzyme I (EC:3.2.1.26)
Alternative name(s):
Invertase
Saccharase
Sucrose hydrolase
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:INV*DC4
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiDaucus carota (Wild carrot)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri4039 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaeudicotyledonsGunneridaePentapetalaeasteridscampanulidsApialesApiaceaeApioideaeScandiceaeDaucinaeDaucusDaucus sect. Daucus

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 44CytoplasmicCuratedAdd BLAST44
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei45 – 65Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini66 – 661LumenalCuratedAdd BLAST596

Keywords - Cellular componenti

Membrane, Vacuole

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_00000333721 – 115Removed in mature form1 PublicationAdd BLAST115
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000033373116 – 661Beta-fructofuranosidase, soluble isoenzyme IAdd BLAST546

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi171N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi238N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi290N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi512N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi513 ↔ 561By similarity
Glycosylationi633N-linked (GlcNAc...) asparagineSequence analysis1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

N-glycosylated; high-mannose and high-xylose complex glycans.

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P80065

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer (PubMed:1541302). May be present in two forms, a 70 kDa monomer and a heterodimer of the 30 kDa and 38 kDa subunits (By similarity). The ratio of the levels of the two forms within cells appears to be regulated developmentally (By similarity).

By similarity1 Publication

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P80065

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni142 – 145Substrate bindingBy similarity4
Regioni204 – 205Substrate bindingBy similarity2
Regioni268 – 269Substrate bindingBy similarity2

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the glycosyl hydrolase 32 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.115.10.20, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR021792 Beta-fructofuranosidase
IPR013320 ConA-like_dom_sf
IPR001362 Glyco_hydro_32
IPR018053 Glyco_hydro_32_AS
IPR013189 Glyco_hydro_32_C
IPR013148 Glyco_hydro_32_N
IPR023296 Glyco_hydro_beta-prop_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF11837 DUF3357, 1 hit
PF08244 Glyco_hydro_32C, 1 hit
PF00251 Glyco_hydro_32N, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00640 Glyco_32, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49899 SSF49899, 1 hit
SSF75005 SSF75005, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00609 GLYCOSYL_HYDROL_F32, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P80065-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDTYHFLPSR DLEHASSYTP RPDSPETRHE PDPDRSKTNR RPIKIVSSVL
60 70 80 90 100
LSTLILSFVI FLLVNPNVQQ VVRKKVSKNS NGEDRNKASK SPEMLGPPSR
110 120 130 140 150
GVSQGVSEKS FRQATAEPSY PWTNDMLSWQ RTSFHFQPQE NWMNDPNGPL
160 170 180 190 200
FHMGWYHLFY QYNPDSAIWG NITWGHAISR DLINWLHLPF AMQPDQWYDI
210 220 230 240 250
NGVWTGSATV LPDGKIVMLY TGDTDDLVQV QNLAYPANLS DPLLLDWIKY
260 270 280 290 300
PDNPVMFPPP GIGSTDFRDP TTAWIGRDGK WRITIGSKVN KTGISLMYKT
310 320 330 340 350
TDFITYELLD NLLHAVPGTG MWECVDFYPV SVTGSNGLDT SVNGPGVKHV
360 370 380 390 400
LKSSLDDDRH DYYALGTYDP INDKWTPDNP ELDVGIGLRL DYGKYYASKT
410 420 430 440 450
FYDQDKERRL LWGWIGETDS ESADLLKGWA SVQSIPRTVV FDKKTGTNIL
460 470 480 490 500
QWPVKEVESL RSRSYEIDDV ELKPGSLVPL KISSAAQLDI VASFEVDEEA
510 520 530 540 550
FKGTYEADAS YNCTASEGAA GRGILGPFGI LVLADDPLSE LTPVYFYIAK
560 570 580 590 600
GVDGNAKTYF CADQSRSSTA SDVDKEVYGS DVPVLHGESL SMRLLVDHSI
610 620 630 640 650
VESFAQGGRT VITSRVYPTR AIYSAARVFL FNNATGVSVT ASVKAWQMAS
660
ATLKPFPFDQ L
Length:661
Mass (Da):73,864
Last modified:January 11, 2001 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iED534C08D61745EA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti422S → P AA sequence (PubMed:1541302).Curated1
Sequence conflicti425L → V AA sequence (PubMed:1541302).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti21R → L in class 3. 1
Natural varianti52S → A in class 3. 1
Natural varianti56L → F in class 3. 1
Natural varianti85R → H in class 3. 1
Natural varianti210V → I in class 2 and class 3. 1
Natural varianti277R → P in class 2 and class 3. 1
Natural varianti334G → V in class 2. 1
Natural varianti418 – 423TDSESA → SDNEST in class 2 and class 3. 6
Natural varianti468D → N in class 2 and class 3. 1
Natural varianti503G → R in class 2. 1
Natural varianti586H → P in class 2 and class 3. 1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X75351 mRNA Translation: CAA53097.1
X75352 mRNA Translation: CAA53098.1
X75353 mRNA Translation: CAA53099.1
Y18707 Genomic DNA Translation: CAA77267.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S37590
S37591
S37592

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75351 mRNA Translation: CAA53097.1
X75352 mRNA Translation: CAA53098.1
X75353 mRNA Translation: CAA53099.1
Y18707 Genomic DNA Translation: CAA77267.1
PIRiS37590
S37591
S37592

3D structure databases

SMRiP80065
ModBaseiSearch...

Protein family/group databases

CAZyiGH32 Glycoside Hydrolase Family 32

Proteomic databases

PRIDEiP80065

Family and domain databases

Gene3Di2.115.10.20, 1 hit
InterProiView protein in InterPro
IPR021792 Beta-fructofuranosidase
IPR013320 ConA-like_dom_sf
IPR001362 Glyco_hydro_32
IPR018053 Glyco_hydro_32_AS
IPR013189 Glyco_hydro_32_C
IPR013148 Glyco_hydro_32_N
IPR023296 Glyco_hydro_beta-prop_sf
PfamiView protein in Pfam
PF11837 DUF3357, 1 hit
PF08244 Glyco_hydro_32C, 1 hit
PF00251 Glyco_hydro_32N, 1 hit
SMARTiView protein in SMART
SM00640 Glyco_32, 1 hit
SUPFAMiSSF49899 SSF49899, 1 hit
SSF75005 SSF75005, 1 hit
PROSITEiView protein in PROSITE
PS00609 GLYCOSYL_HYDROL_F32, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiINVB_DAUCA
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P80065
Secondary accession number(s): Q42719, Q42720, Q42721
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 11, 2001
Last modified: December 11, 2019
This is version 96 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again