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Protein

Chitin-binding lectin 1

Gene
N/A
Organism
Solanum tuberosum (Potato)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei78ChitooligosaccharideBy similarity1
Binding sitei80ChitooligosaccharideBy similarity1
Binding sitei82ChitooligosaccharideBy similarity1
Binding sitei89ChitooligosaccharideBy similarity1
Binding sitei230ChitooligosaccharideBy similarity1
Binding sitei232ChitooligosaccharideBy similarity1
Binding sitei234ChitooligosaccharideBy similarity1
Binding sitei241ChitooligosaccharideBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processPlant defense
LigandChitin-binding, Lectin

Names & Taxonomyi

Protein namesi
Recommended name:
Chitin-binding lectin 1
Alternative name(s):
PL-I
OrganismiSolanum tuberosum (Potato)
Taxonomic identifieri4113 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum
Proteomesi
  • UP000011115 Componenti: Unassembled WGS sequence

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Sequence analysisAdd BLAST22
ChainiPRO_000000527423 – 323Chitin-binding lectin 1Add BLAST301

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei504-hydroxyproline1 Publication1
Glycosylationi50O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei514-hydroxyproline1 Publication1
Glycosylationi51O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei534-hydroxyproline1 Publication1
Glycosylationi53O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei554-hydroxyproline1 Publication1
Glycosylationi55O-linked (Ara...) hydroxyproline1 Publication1
Disulfide bondi61 ↔ 77PROSITE-ProRule annotation
Disulfide bondi70 ↔ 83PROSITE-ProRule annotation
Disulfide bondi76 ↔ 90PROSITE-ProRule annotation
Disulfide bondi95 ↔ 99PROSITE-ProRule annotation
Disulfide bondi108 ↔ 125PROSITE-ProRule annotation
Disulfide bondi117 ↔ 131PROSITE-ProRule annotation
Disulfide bondi124 ↔ 138PROSITE-ProRule annotation
Disulfide bondi143 ↔ 147PROSITE-ProRule annotation
Glycosylationi151O-linked (Gal) serine1 Publication1
Modified residuei1524-hydroxyproline1 Publication1 Publication1
Glycosylationi152O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1534-hydroxyproline1 Publication1 Publication1
Glycosylationi153O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1544-hydroxyproline1 Publication1 Publication1
Glycosylationi154O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1554-hydroxyproline1 Publication1 Publication1
Glycosylationi155O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1564-hydroxyproline1 Publication1 Publication1
Glycosylationi156O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1574-hydroxyproline1 Publication1 Publication1
Glycosylationi157O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1584-hydroxyproline1 Publication1
Glycosylationi158O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1594-hydroxyproline1 Publication1 Publication1
Glycosylationi159O-linked (Ara...) hydroxyproline1 Publication1
Glycosylationi160O-linked (Gal) serine1 Publication1
Modified residuei1614-hydroxyproline1 Publication1 Publication1
Glycosylationi161O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1624-hydroxyproline1 Publication1 Publication1
Glycosylationi162O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1634-hydroxyproline1 Publication1 Publication1
Glycosylationi163O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1644-hydroxyproline1 Publication1 Publication1
Glycosylationi164O-linked (Ara...) hydroxyproline1 Publication1
Glycosylationi165O-linked (Gal) serine1 Publication1
Modified residuei1664-hydroxyproline1 Publication1 Publication1
Glycosylationi166O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1674-hydroxyproline1 Publication1 Publication1
Glycosylationi167O-linked (Ara...) hydroxyproline1 Publication1
Glycosylationi168O-linked (Gal) serine1 Publication1
Modified residuei1694-hydroxyproline1 Publication1 Publication1
Glycosylationi169O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1704-hydroxyproline1 Publication1 Publication1
Glycosylationi170O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1714-hydroxyproline1 Publication1 Publication1
Glycosylationi171O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1724-hydroxyproline1 Publication1 Publication1
Glycosylationi172O-linked (Ara...) hydroxyproline1 Publication1
Glycosylationi173O-linked (Gal) serine1 Publication1
Modified residuei1744-hydroxyproline1 Publication1 Publication1
Glycosylationi174O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1754-hydroxyproline1 Publication1 Publication1
Glycosylationi175O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1764-hydroxyproline1 Publication1
Glycosylationi176O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1774-hydroxyproline1 Publication1 Publication1
Glycosylationi177O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1784-hydroxyproline1 Publication1
Glycosylationi178O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1794-hydroxyproline1 Publication1
Glycosylationi179O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1804-hydroxyproline1 Publication1
Glycosylationi180O-linked (Ara...) hydroxyproline1 Publication1
Glycosylationi181O-linked (Gal) serine1 Publication1
Modified residuei1824-hydroxyproline1 Publication1
Glycosylationi182O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1834-hydroxyproline1 Publication1
Glycosylationi183O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1844-hydroxyproline1 Publication1
Glycosylationi184O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1854-hydroxyproline1 Publication1
Glycosylationi185O-linked (Ara...) hydroxyproline1 Publication1
Glycosylationi186O-linked (Gal) serine1 Publication1
Modified residuei1874-hydroxyproline1 Publication1
Glycosylationi187O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1884-hydroxyproline1 Publication1
Glycosylationi188O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1894-hydroxyproline1 Publication1
Glycosylationi189O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1904-hydroxyproline1 Publication1
Glycosylationi190O-linked (Ara...) hydroxyproline1 Publication1
Glycosylationi191O-linked (Gal) serine1 Publication1
Modified residuei1924-hydroxyproline1 Publication1
Glycosylationi192O-linked (Ara...) hydroxyproline1 Publication1
Glycosylationi193O-linked (Gal) serine1 Publication1
Modified residuei1944-hydroxyproline1 Publication1
Glycosylationi194O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1954-hydroxyproline1 Publication1
Glycosylationi195O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1964-hydroxyproline1 Publication1
Glycosylationi196O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1974-hydroxyproline1 Publication1
Glycosylationi197O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1984-hydroxyproline1 Publication1
Glycosylationi198O-linked (Ara...) hydroxyproline1 Publication1
Glycosylationi200O-linked (Gal) serine1 Publication1
Modified residuei2014-hydroxyproline1 Publication1
Glycosylationi201O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei2024-hydroxyproline1 Publication1
Glycosylationi202O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei2034-hydroxyproline1 Publication1
Glycosylationi203O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei2044-hydroxyproline1 Publication1
Glycosylationi204O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei2054-hydroxyproline1 Publication1
Glycosylationi205O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei2064-hydroxyproline1 Publication1
Glycosylationi206O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei2094-hydroxyproline1 Publication1
Glycosylationi209O-linked (Ara...) hydroxyproline1 Publication1
Disulfide bondi213 ↔ 229PROSITE-ProRule annotation
Disulfide bondi222 ↔ 235PROSITE-ProRule annotation
Disulfide bondi228 ↔ 242PROSITE-ProRule annotation
Disulfide bondi247 ↔ 251PROSITE-ProRule annotation
Disulfide bondi260 ↔ 277PROSITE-ProRule annotation
Disulfide bondi269 ↔ 283PROSITE-ProRule annotation
Disulfide bondi276 ↔ 290PROSITE-ProRule annotation
Disulfide bondi295 ↔ 299PROSITE-ProRule annotation

Post-translational modificationi

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.1 Publication
The N-terminus is blocked. The N-terminal sequences proposed in PubMed:9022287 and PubMed:11056399 originate probably from truncated proteins.

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

PRIDEiQ9S8M0

PTM databases

iPTMnetiQ9S8M0

Expressioni

Gene expression databases

ExpressionAtlasiQ9S8M0 baseline and differential

Interactioni

Subunit structurei

Homodimer.Curated

Structurei

3D structure databases

ProteinModelPortaliQ9S8M0
SMRiQ9S8M0
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini58 – 101Chitin-binding type-1 1PROSITE-ProRule annotationAdd BLAST44
Domaini105 – 149Chitin-binding type-1 2PROSITE-ProRule annotationAdd BLAST45
Repeati151 – 15919
Repeati160 – 16425
Repeati165 – 16733
Repeati168 – 17245
Repeati173 – 18058
Repeati181 – 18565
Repeati186 – 19075
Repeati191 – 19282
Repeati193 – 19896
Repeati200 – 206107
Domaini210 – 253Chitin-binding type-1 3PROSITE-ProRule annotationAdd BLAST44
Domaini257 – 301Chitin-binding type-1 4PROSITE-ProRule annotationAdd BLAST45

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni150 – 210Extensin-likeAdd BLAST61
Regioni151 – 20610 X approximate repeats of S-P-P-P-PAdd BLAST56

Sequence similaritiesi

In the central section; belongs to the extensin family.Curated

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3Di3.30.60.10, 4 hits
InterProiView protein in InterPro
IPR001002 Chitin-bd_1
IPR036861 Endochitinase-like_sf
PfamiView protein in Pfam
PF00187 Chitin_bind_1, 4 hits
ProDomiView protein in ProDom or Entries sharing at least one domain
PD000609 Chitin_bd_1, 4 hits
SMARTiView protein in SMART
SM00270 ChtBD1, 4 hits
SUPFAMiSSF57016 SSF57016, 4 hits
PROSITEiView protein in PROSITE
PS00026 CHIT_BIND_I_1, 2 hits
PS50941 CHIT_BIND_I_2, 4 hits

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9S8M0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKETAISVLA LLTLFLLEVV SANELSLPFH LPINETIGLE VFQGINNASP
60 70 80 90 100
PSPSPLPYPQ CGMKKGGGKC IKTGECCSIW GWCGTTNAYC SPGYCQKQCP
110 120 130 140 150
GPYPEGRCGW QANGKSCPTG TGQCCSNGGW CGTTSDYCAS KNCQSQCKLP
160 170 180 190 200
SPPPPPPPPS PPPPSPPSPP PPSPPPPPPP SPPPPSPPPP SPSPPPPPAS
210 220 230 240 250
PPPPPPALPY PQCGIKKGGG KCIKTGECCS IWGWCGTTNA YCSPGYCQKQ
260 270 280 290 300
CPGPYPEGRC GWQANGKSCP TGTGHCCSNA GWCGTTSDYC APVNCQAQCN
310 320
TTTLTSPIKN RMRGIESFML NVV
Length:323
Mass (Da):33,554
Last modified:April 13, 2004 - v2
Checksum:i2E415620F8C7FC40
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti50P → T AA sequence (PubMed:9022287).Curated1
Sequence conflicti50P → T AA sequence (PubMed:11056399).Curated1
Sequence conflicti54S → P AA sequence (PubMed:9022287).Curated1
Sequence conflicti54S → P AA sequence (PubMed:11056399).Curated1
Sequence conflicti59 – 61PQC → LQY AA sequence (PubMed:11056399).Curated3
Sequence conflicti63M → L AA sequence (PubMed:9022287).Curated1
Sequence conflicti63M → L AA sequence (PubMed:11056399).Curated1
Sequence conflicti66G → P AA sequence (PubMed:9022287).Curated1
Sequence conflicti73T → G AA sequence (PubMed:11056399).Curated1
Sequence conflicti158P → H AA sequence (PubMed:8054990).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BG350800 mRNA No translation available.

Similar proteinsi

Entry informationi

Entry nameiLECT_SOLTU
AccessioniPrimary (citable) accession number: Q9S8M0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: April 13, 2004
Last modified: May 23, 2018
This is version 74 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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