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Reviewed, UniProtKB/Swiss-Prot Q9S8M0 (LECT_SOLTU)

Last modified November 24, 2009. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Chitin-binding lectin 1
Alternative name(s):
    PL-I
OrganismSolanum tuberosum (Potato)
Taxonomic identifier4113 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Solanoideae › Solaneae › Solanum

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Protein attributes

Sequence length323 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

This protein might function as a defense against chitin containing pathogens. Binds to several branched or linear N-acetyllactosamine-containing glycosphingolipids and also to lactosylceramide with sphingosine and non-hydroxy fatty acids.

Subunit structure

Homodimer Probable.

Post-translational modification

Heavily glycosylated with beta-arabinose on hydroxyprolines and with alpha-galactose on serines of the extensin-like domain. As no other sugars could be detected in the native lectin, it is unlikely that the three putative N-glycosylation sites are actually glycosylated. Ref.5

The N-terminus is blocked. The N-terminal sequences proposed in Ref.3 and Ref.4 originate probably from truncated proteins.

Sequence similarities

In the central section; belongs to the extensin family.

Contains 4 chitin-binding type-1 domains.

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Ontologies

Keywords
   Biological processPlant defense
   DomainRepeat
Signal
   LigandChitin-binding
Lectin
   PTMDisulfide bond
Glycoprotein
Hydroxylation
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processdefense response

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionchitin binding

Inferred from electronic annotation. Source: UniProtKB-KW

sugar binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 323301Chitin-binding lectin 1
PRO_0000005274

Regions

Domain58 – 10144Chitin-binding type-1 1
Domain105 – 14945Chitin-binding type-1 2
Repeat151 – 15991
Repeat160 – 16452
Repeat165 – 16733
Repeat168 – 17254
Repeat173 – 18085
Repeat181 – 18556
Repeat186 – 19057
Repeat191 – 19228
Repeat193 – 19869
Repeat200 – 206710
Domain210 – 25344Chitin-binding type-1 3
Domain257 – 30145Chitin-binding type-1 4
Region150 – 21061Extensin-like
Region151 – 2065610 X approximate repeats of S-P-P-P-P

Sites

Binding site781Chitooligosaccharide By similarity
Binding site801Chitooligosaccharide By similarity
Binding site821Chitooligosaccharide By similarity
Binding site891Chitooligosaccharide By similarity
Binding site2301Chitooligosaccharide By similarity
Binding site2321Chitooligosaccharide By similarity
Binding site2341Chitooligosaccharide By similarity
Binding site2411Chitooligosaccharide By similarity

Amino acid modifications

Modified residue5014-hydroxyproline Probable
Modified residue5314-hydroxyproline Probable
Modified residue5514-hydroxyproline Probable
Modified residue15014-hydroxyproline Probable
Modified residue15214-hydroxyproline Probable
Modified residue15314-hydroxyproline Probable
Modified residue15414-hydroxyproline Probable
Modified residue15514-hydroxyproline Probable
Modified residue15614-hydroxyproline Probable
Modified residue15714-hydroxyproline Probable
Modified residue15814-hydroxyproline Probable
Modified residue15914-hydroxyproline Probable
Modified residue16114-hydroxyproline Probable
Modified residue16214-hydroxyproline Probable
Modified residue16314-hydroxyproline Probable
Modified residue16414-hydroxyproline Probable
Modified residue16614-hydroxyproline Probable
Modified residue16714-hydroxyproline Probable
Modified residue16914-hydroxyproline Probable
Modified residue17014-hydroxyproline Probable
Modified residue17114-hydroxyproline Probable
Modified residue17214-hydroxyproline Probable
Modified residue17414-hydroxyproline Probable
Modified residue17514-hydroxyproline Probable
Modified residue17614-hydroxyproline Probable
Modified residue17714-hydroxyproline Probable
Modified residue17814-hydroxyproline Probable
Modified residue17914-hydroxyproline Probable
Modified residue18014-hydroxyproline Probable
Modified residue18214-hydroxyproline Probable
Modified residue18314-hydroxyproline Probable
Modified residue18414-hydroxyproline Probable
Modified residue18514-hydroxyproline Probable
Modified residue18714-hydroxyproline Probable
Modified residue18814-hydroxyproline Probable
Modified residue18914-hydroxyproline Probable
Modified residue19014-hydroxyproline Probable
Modified residue19214-hydroxyproline Probable
Modified residue19414-hydroxyproline Probable
Modified residue19514-hydroxyproline Probable
Modified residue19614-hydroxyproline Probable
Modified residue19714-hydroxyproline Probable
Modified residue19814-hydroxyproline Probable
Modified residue20114-hydroxyproline Probable
Modified residue20214-hydroxyproline Probable
Modified residue20314-hydroxyproline Probable
Modified residue20414-hydroxyproline Probable
Modified residue20514-hydroxyproline Probable
Modified residue20614-hydroxyproline Probable
Modified residue20914-hydroxyproline Probable
Glycosylation501O-linked (Ara...) Probable
Glycosylation531O-linked (Ara...) Probable
Glycosylation551O-linked (Ara...) Probable
Glycosylation1501O-linked (Ara...) Probable
Glycosylation1511O-linked (Gal) Probable
Glycosylation1521O-linked (Ara...) Probable
Glycosylation1531O-linked (Ara...) Probable
Glycosylation1541O-linked (Ara...) Probable
Glycosylation1551O-linked (Ara...) Probable
Glycosylation1561O-linked (Ara...) Probable
Glycosylation1571O-linked (Ara...) Probable
Glycosylation1581O-linked (Ara...) Probable
Glycosylation1591O-linked (Ara...) Probable
Glycosylation1601O-linked (Gal) Probable
Glycosylation1611O-linked (Ara...) Probable
Glycosylation1621O-linked (Ara...) Probable
Glycosylation1631O-linked (Ara...) Probable
Glycosylation1641O-linked (Ara...) Probable
Glycosylation1651O-linked (Gal) Probable
Glycosylation1661O-linked (Ara...) Probable
Glycosylation1671O-linked (Ara...) Probable
Glycosylation1681O-linked (Gal) Probable
Glycosylation1691O-linked (Ara...) Probable
Glycosylation1701O-linked (Ara...) Probable
Glycosylation1711O-linked (Ara...) Probable
Glycosylation1721O-linked (Ara...) Probable
Glycosylation1731O-linked (Gal) Probable
Glycosylation1741O-linked (Ara...) Probable
Glycosylation1751O-linked (Ara...) Probable
Glycosylation1761O-linked (Ara...) Probable
Glycosylation1771O-linked (Ara...) Probable
Glycosylation1781O-linked (Ara...) Probable
Glycosylation1791O-linked (Ara...) Probable
Glycosylation1801O-linked (Ara...) Probable
Glycosylation1811O-linked (Gal) Probable
Glycosylation1821O-linked (Ara...) Probable
Glycosylation1831O-linked (Ara...) Probable
Glycosylation1841O-linked (Ara...) Probable
Glycosylation1851O-linked (Ara...) Probable
Glycosylation1861O-linked (Gal) Probable
Glycosylation1871O-linked (Ara...) Probable
Glycosylation1881O-linked (Ara...) Probable
Glycosylation1891O-linked (Ara...) Probable
Glycosylation1901O-linked (Ara...) Probable
Glycosylation1911O-linked (Gal) Probable
Glycosylation1921O-linked (Ara...) Probable
Glycosylation1931O-linked (Gal) Probable
Glycosylation1941O-linked (Ara...) Probable
Glycosylation1951O-linked (Ara...) Probable
Glycosylation1961O-linked (Ara...) Probable
Glycosylation1971O-linked (Ara...) Probable
Glycosylation1981O-linked (Ara...) Probable
Glycosylation2001O-linked (Gal) Probable
Glycosylation2011O-linked (Ara...) Probable
Glycosylation2021O-linked (Ara...) Probable
Glycosylation2031O-linked (Ara...) Probable
Glycosylation2041O-linked (Ara...) Probable
Glycosylation2051O-linked (Ara...) Probable
Glycosylation2061O-linked (Ara...) Probable
Glycosylation2091O-linked (Ara...) Probable
Disulfide bond61 ↔ 77 By similarity
Disulfide bond70 ↔ 83 By similarity
Disulfide bond76 ↔ 90 By similarity
Disulfide bond95 ↔ 99 By similarity
Disulfide bond108 ↔ 125 By similarity
Disulfide bond117 ↔ 131 By similarity
Disulfide bond124 ↔ 138 By similarity
Disulfide bond143 ↔ 147 By similarity
Disulfide bond213 ↔ 229 By similarity
Disulfide bond222 ↔ 235 By similarity
Disulfide bond228 ↔ 242 By similarity
Disulfide bond247 ↔ 251 By similarity
Disulfide bond260 ↔ 277 By similarity
Disulfide bond269 ↔ 283 By similarity
Disulfide bond276 ↔ 290 By similarity
Disulfide bond295 ↔ 299 By similarity

Experimental info

Sequence conflict501P → T AA sequence Ref.3
Sequence conflict501P → T AA sequence Ref.4
Sequence conflict541S → P AA sequence Ref.3
Sequence conflict541S → P AA sequence Ref.4
Sequence conflict59 – 613PQC → LQY AA sequence Ref.4
Sequence conflict631M → L AA sequence Ref.3
Sequence conflict631M → L AA sequence Ref.4
Sequence conflict661G → P AA sequence Ref.3
Sequence conflict731T → G AA sequence Ref.4
Sequence conflict1581P → H AA sequence Ref.2

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Sequences

Sequence LengthMass (Da)Tools
Q9S8M0-1 [UniParc].

Last modified April 13, 2004. Version 2.
Checksum: 2E415620F8C7FC40

FASTA32333,554
        10         20         30         40         50         60 
MKETAISVLA LLTLFLLEVV SANELSLPFH LPINETIGLE VFQGINNASP PSPSPLPYPQ 

        70         80         90        100        110        120 
CGMKKGGGKC IKTGECCSIW GWCGTTNAYC SPGYCQKQCP GPYPEGRCGW QANGKSCPTG 

       130        140        150        160        170        180 
TGQCCSNGGW CGTTSDYCAS KNCQSQCKLP SPPPPPPPPS PPPPSPPSPP PPSPPPPPPP 

       190        200        210        220        230        240 
SPPPPSPPPP SPSPPPPPAS PPPPPPALPY PQCGIKKGGG KCIKTGECCS IWGWCGTTNA 

       250        260        270        280        290        300 
YCSPGYCQKQ CPGPYPEGRC GWQANGKSCP TGTGHCCSNA GWCGTTSDYC APVNCQAQCN 

       310        320 
TTTLTSPIKN RMRGIESFML NVV

« Hide

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References

[1]"Potato lectin: an updated model of a unique chimeric plant protein."
Van Damme E.J., Barre A., Rouge P., Peumans W.J.
Plant J. 37:34-45(2004) [PubMed: 14675430] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], DOMAIN MODELING.
Tissue: Venom gland.
[2]"Potato lectin: a modular protein sharing sequence similarities with the extensin family, the hevein lectin family, and snake venom disintegrins (platelet aggregation inhibitors)."
Kieliszewski M.J., Showalter A.M., Leykam J.F.
Plant J. 5:849-861(1994) [PubMed: 8054990] [Abstract]
Cited for: PROTEIN SEQUENCE OF 73-79; 90-94; 131-137 AND 149-175.
Tissue: Venom.
[3]"Potato lectin: a three-domain glycoprotein with novel hydroxyproline-containing sequences and sequence similarities to wheat-germ agglutinin."
Allen A.K., Bolwell G.P., Brown D.S., Sidebottom C., Slabas A.R.
Int. J. Biochem. Cell Biol. 28:1285-1291(1996) [PubMed: 9022287] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, MASS SPECTROMETRY, DOMAIN ORGANIZATION.
Tissue: Venom.
[4]"Isolectins from Solanum tuberosum with different detailed carbohydrate binding specificities: unexpected recognition of lactosylceramide by N-acetyllactosamine-binding lectins."
Ciopraga J., Aangstroem J., Bergstroem J., Larsson T., Karlsson N., Motas C., Gozia O., Teneberg S.
J. Biochem. 128:855-867(2000) [PubMed: 11056399] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, BINDING SPECIFICITIES.
Tissue: Venom.
[5]"Properties of potato lectin and the nature of its glycoprotein linkages."
Allen A.K., Desai N.N., Neuberger A., Creeth J.M.
Biochem. J. 171:665-674(1978) [PubMed: 666730] [Abstract]
Cited for: CARBOHYDRATE CONTENT ANALYSIS.

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Cross-references

Sequence databases

BG350800 mRNA. No translation available.

3D structure databases

ModBaseSearch...

Family and domain databases

InterProIPR001002. Chitin_bd_1.
[Graphical view]
Gene3DG3DSA:3.30.60.10. Chitin_bd_1. 4 hits.
PfamPF00187. Chitin_bind_1. 4 hits.
[Graphical view]
ProDomPD000609. Chitin_bd_1. 4 hits.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00270. ChtBD1. 4 hits.
[Graphical view]
PROSITEPS00026. CHIT_BIND_I_1. 2 hits.
PS50941. CHIT_BIND_I_2. 4 hits.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameLECT_SOLTU
AccessionPrimary (citable) accession number: Q9S8M0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: April 13, 2004
Last modified: November 24, 2009
This is version 47 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents