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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

  • positive regulation of mitotic nuclear division Source: UniProtKB
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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence analysisAdd
BLAST
Propeptidei27 – 4418Removed in mature formSequence analysis1 PublicationPRO_0000005271Add
BLAST
Chaini45 – 170126Lectin-C1 PublicationPRO_0000005272Add
BLAST
Propeptidei171 – 19424Removed in mature formSequence analysis1 PublicationPRO_0000005273Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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

1
194
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi50 – 523Combined sources
Helixi58 – 603Combined sources
Beta strandi69 – 724Combined sources
Helixi73 – 764Combined sources
Turni84 – 874Combined sources
Helixi91 – 933Combined sources
Helixi99 – 1013Combined sources
Beta strandi108 – 1114Combined sources
Helixi114 – 1174Combined sources
Turni125 – 1284Combined sources
Helixi132 – 1343Combined sources
Beta strandi149 – 1524Combined sources
Helixi155 – 1584Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ULKX-ray1.80A/B45-170[»]
ProteinModelPortaliQ9AYP9.
SMRiQ9AYP9. Positions 45-170.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9AYP9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini45 – 8642Chitin-binding type-1 1PROSITE-ProRule annotationAdd
BLAST
Domaini87 – 12741Chitin-binding type-1 2PROSITE-ProRule annotationAdd
BLAST
Domaini128 – 16841Chitin-binding type-1 3PROSITE-ProRule annotationAdd
BLAST

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1ULKX-ray1.80A/B45-170[»]
ProteinModelPortaliQ9AYP9.
SMRiQ9AYP9. Positions 45-170.
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: October 14, 2015
This is version 64 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.