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Protein

Lectin-C

Gene
N/A
Organism
Phytolacca americana (American pokeweed) (Phytolacca decandra)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

N-acetyl-D-glucosamine binding lectin. Almost no hemagglutinating activity towards human erythrocytes. Low mitogenic activity towards human peripheral blood lymphocytes.2 Publications

GO - Molecular functioni

  • carbohydrate binding Source: UniProtKB-KW
  • chitin binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Mitogen

Keywords - Ligandi

Chitin-binding, Lectin

Protein family/group databases

CAZyiCBM18. Carbohydrate-Binding Module Family 18.

Names & Taxonomyi

Protein namesi
Recommended name:
Lectin-C
Alternative name(s):
PL-C
OrganismiPhytolacca americana (American pokeweed) (Phytolacca decandra)
Taxonomic identifieri3527 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesPhytolaccaceaePhytolacca

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 26Sequence analysisAdd BLAST26
PropeptideiPRO_000000527127 – 44Removed in mature formSequence analysis1 PublicationAdd BLAST18
ChainiPRO_000000527245 – 170Lectin-C1 PublicationAdd BLAST126
PropeptideiPRO_0000005273171 – 194Removed in mature formSequence analysis1 PublicationAdd BLAST24

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi48 ↔ 63PROSITE-ProRule annotation1 Publication
Disulfide bondi57 ↔ 69PROSITE-ProRule annotation1 Publication
Disulfide bondi62 ↔ 76PROSITE-ProRule annotation1 Publication
Disulfide bondi80 ↔ 84PROSITE-ProRule annotation1 Publication
Disulfide bondi89 ↔ 104PROSITE-ProRule annotation1 Publication
Disulfide bondi98 ↔ 110PROSITE-ProRule annotation1 Publication
Disulfide bondi103 ↔ 117PROSITE-ProRule annotation1 Publication
Disulfide bondi121 ↔ 125PROSITE-ProRule annotation1 Publication
Disulfide bondi130 ↔ 145PROSITE-ProRule annotation1 Publication
Disulfide bondi139 ↔ 151PROSITE-ProRule annotation1 Publication
Disulfide bondi144 ↔ 158PROSITE-ProRule annotation1 Publication
Disulfide bondi162 ↔ 166PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer. The homodimers are asymmetric; formed in a 'head-to-tail' fashion via hydrophobic interactions between aromatic residues of the carbohydrate-binding sites of each subunit.1 Publication

Structurei

Secondary structure

1194
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi50 – 52Combined sources3
Helixi58 – 60Combined sources3
Beta strandi69 – 72Combined sources4
Helixi73 – 76Combined sources4
Turni84 – 87Combined sources4
Helixi91 – 93Combined sources3
Helixi99 – 101Combined sources3
Beta strandi108 – 111Combined sources4
Helixi114 – 117Combined sources4
Turni125 – 128Combined sources4
Helixi132 – 134Combined sources3
Beta strandi149 – 152Combined sources4
Helixi155 – 158Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ULKX-ray1.80A/B45-170[»]
ProteinModelPortaliQ9AYP9.
SMRiQ9AYP9.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9AYP9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini45 – 86Chitin-binding type-1 1PROSITE-ProRule annotationAdd BLAST42
Domaini87 – 127Chitin-binding type-1 2PROSITE-ProRule annotationAdd BLAST41
Domaini128 – 168Chitin-binding type-1 3PROSITE-ProRule annotationAdd BLAST41

Sequence similaritiesi

Contains 3 chitin-binding type-1 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3Di3.30.60.10. 3 hits.
InterProiIPR001002. Chitin-bd_1.
IPR018371. Chitin-binding_1_CS.
[Graphical view]
PfamiPF00187. Chitin_bind_1. 3 hits.
[Graphical view]
PRINTSiPR00451. CHITINBINDNG.
ProDomiPD000609. Chitin_bd_1. 3 hits.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00270. ChtBD1. 3 hits.
[Graphical view]
SUPFAMiSSF57016. SSF57016. 3 hits.
PROSITEiPS00026. CHIT_BIND_I_1. 1 hit.
PS50941. CHIT_BIND_I_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9AYP9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRSNSIAVM LVLVLSSLML LLPVEGQGHE GHGVGEILLM GKLGAPVCGV
60 70 80 90 100
RASGRVCPDG YCCSQWGYCG TTEEYCGKGC QSQCDYNRCG KEFGGKECHD
110 120 130 140 150
ELCCSQYGWC GNSDGHCGEG CQSQCSYWRC GKDFGGRLCT EDMCCSQYGW
160 170 180 190
CGLTDDHCED GCQSQCDLPT LLPSPLRRII AIRKLKANLA NMLS
Length:194
Mass (Da):21,042
Last modified:June 1, 2001 - v1
Checksum:i8FA0C697AF82563A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB052963 mRNA. Translation: BAB21577.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB052963 mRNA. Translation: BAB21577.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ULKX-ray1.80A/B45-170[»]
ProteinModelPortaliQ9AYP9.
SMRiQ9AYP9.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM18. Carbohydrate-Binding Module Family 18.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ9AYP9.

Family and domain databases

Gene3Di3.30.60.10. 3 hits.
InterProiIPR001002. Chitin-bd_1.
IPR018371. Chitin-binding_1_CS.
[Graphical view]
PfamiPF00187. Chitin_bind_1. 3 hits.
[Graphical view]
PRINTSiPR00451. CHITINBINDNG.
ProDomiPD000609. Chitin_bd_1. 3 hits.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00270. ChtBD1. 3 hits.
[Graphical view]
SUPFAMiSSF57016. SSF57016. 3 hits.
PROSITEiPS00026. CHIT_BIND_I_1. 1 hit.
PS50941. CHIT_BIND_I_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLECC_PHYAM
AccessioniPrimary (citable) accession number: Q9AYP9
Secondary accession number(s): Q9S9F4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: June 1, 2001
Last modified: November 2, 2016
This is version 66 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

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.