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1158  structures 944  species 0  interactions 65241  sequences 2238  architectures

Family: Lectin_C (PF00059)

Summary: Lectin C-type domain

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This is the Wikipedia entry entitled "C-type lectin". More...

C-type lectin Edit Wikipedia article

Lectin C-type domain
PDB 1jzn EBI.jpg
Pentameric structure of rattlesnake venom lectin which is a galactose binding lectin.[1] [2]

A C-type lectin (CLEC) is a type of carbohydrate-binding protein domain known as a lectin.[3] The C-type designation is from their requirement for calcium for binding.[4] Proteins that contain C-type lectin domains have a diverse range of functions including cell-cell adhesion, immune response to pathogens and apoptosis.[5][6]


Drickamer et al. classified C-type lectins into 7 subgroups (I to VII) based on the order of the various protein domains in each protein.[7] This classification was subsequently updated in 2002, leading to seven additional groups (VIII to XIV).[8] Most recently, three further subgroups were added (XV to XVII).[3]

Group Name Associated domains
I Lecticans EGF, Sushi, Ig and Link domains
II Asialoglycoprotein and DC receptors None
III Collectins None
IV Selectins Sushi and EGF domains
V NK - cell receptors None
VI Multi-CTLD endocytic receptors FnII and Ricin domains
VII Reg group None
VIII Chondrolectin, Layilin None
IX Tetranectin None
X Polycystin WSC, REJ, PKD domains
XI Attractin (ATRN) PSI, EGF and CUB domains
XII Eosinophil major basic protein (EMBP) None
XIV Thrombomodulin, CD93, CD248, CLEC14A EGF domains [9]
XV Bimlec None
XVI SEEC SCP and EGF domains
XVII CBCP/Frem1/QBRICK CSPG repeats and CalX-beta domains

CLECs include:

The "NK Cell lectin-like receptors" are a very closely related group:[10]

Additional proteins containing this domain include:


  1. ^ Walker JR, Nagar B, Young NM, Hirama T, Rini JM (April 2004). "X-ray crystal structure of a galactose-specific C-type lectin possessing a novel decameric quaternary structure". Biochemistry. 43 (13): 3783–92. doi:10.1021/bi035871a. PMID 15049685.
  2. ^ Mahla RS, Reddy MC, Prasad DV, Kumar H (September 2013). "Sweeten PAMPs: Role of Sugar Complexed PAMPs in Innate Immunity and Vaccine Biology". Frontiers in Immunology. 4: 248. doi:10.3389/fimmu.2013.00248. PMC 3759294. PMID 24032031.
  3. ^ a b Zelensky AN, Gready JE (December 2005). "The C-type lectin-like domain superfamily". FEBS J. 272 (24): 6179–217. doi:10.1111/j.1742-4658.2005.05031.x. PMID 16336259.
  4. ^ C-Type+Lectin at the US National Library of Medicine Medical Subject Headings (MeSH)
  5. ^ Drickamer K (October 1999). "C-type lectin-like domains". Curr. Opin. Struct. Biol. 9 (5): 585–90. doi:10.1016/S0959-440X(99)00009-3. PMID 10508765.
  6. ^ Cambi A, Figdor C (May 2009). "Necrosis: C-type lectins sense cell death". Curr. Biol. 19 (9): R375–8. doi:10.1016/j.cub.2009.03.032. PMID 19439262.
  7. ^ Drickamer K (1993). "Evolution of Ca(2+)-dependent animal lectins". Prog. Nucleic Acid Res. Mol. Biol. Progress in Nucleic Acid Research and Molecular Biology. 45: 207–32. doi:10.1016/S0079-6603(08)60870-3. ISBN 978-0-12-540045-9. PMID 8341801.
  8. ^ Drickamer K, Fadden AJ (2002). "Genomic analysis of C-type lectins". Biochem. Soc. Symp. (69): 59–72. PMID 12655774.
  9. ^ "C-type lectin domain group 14 proteins in vascular biology, cancer and inflammation". FEBS Journal. PMID 31287944.
  10. ^ NK+Cell+Lectin-Like+Receptors at the US National Library of Medicine Medical Subject Headings (MeSH)

External links

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Lectin C-type domain Provide feedback

This family includes both long and short form C-type

Literature references

  1. Hakansson K, Lim NK, Hoppe HJ, Reid KB; , Structure Fold Des 1999;7:255-264.: Crystal structure of the trimeric alpha-helical coiled-coil and the three lectin domains of human lung surfactant protein D. PUBMED:10368295 EPMC:10368295

Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR001304

A number of different families of proteins share a conserved domain which was first characterised in some animal lectins and which seem to function as a calcium-dependent carbohydrate-recognition domain [ PUBMED:3290208 , PUBMED:8341801 ]. This domain, which is known as the C-type lectin domain (CTL) or as the carbohydrate-recognition domain (CRD), consists of about 110 to 130 residues. There are four cysteines which are perfectly conserved and involved in two disulphide bonds.

There are proteins with modules similar in overall structure to CRDs that serve functions other than sugar binding. Therefore, a more general term C-type lectin-like domain was introduced to refer to such domains, although both terms C-type lectin and C-type lectin-like are sometimes used interchangeably [ PUBMED:16336259 ].

C-type lectins can be further divided into seven subgroups based on additional non-lectin domains and gene structure: (I) hyalectans, (II) asialoglycoprotein receptors, (III) collectins, (IV) selectins, (V) NK group transmembrane receptors, (VI) macrophage mannose receptors, and (VII) simple (single domain) lectins [ PUBMED:15476922 ]. Lectins are a diverse group of proteins, both in terms of structure and activity. Carbohydrate binding ability may have evolved independently and sporadically in numerous unrelated families, where each evolved a structure that was conserved to fulfil some other activity and function. In general, animal lectins act as recognition molecules within the immune system, their functions involving defence against pathogens, cell trafficking, immune regulation and the prevention of autoimmunity [ PUBMED:14519388 ].

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan C_Lectin (CL0056), which has the following description:

This clan contains domains that have a C-type lectin fold. Many of these are known or expected to mediate interactions with sugars.

The clan contains the following 13 members:

APT C4 Chordopox_A33R DUF1554 DUF5075 Endostatin FGE-sulfatase Intimin_C InvE_AD Lectin_C Ly49 UL45 Xlink


We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

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Representative proteomes UniProt

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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

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HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...


This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

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Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Swissprot_feature_table
Previous IDs: lectin_c;
Type: Domain
Sequence Ontology: SO:0000417
Author: Sonnhammer ELL , Griffiths-Jones SR , Eberhardt R
Number in seed: 53
Number in full: 65241
Average length of the domain: 107.30 aa
Average identity of full alignment: 21 %
Average coverage of the sequence by the domain: 29.76 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 22.6 22.6
Trusted cut-off 22.6 22.6
Noise cut-off 22.5 22.5
Model length: 109
Family (HMM) version: 24
Download: download the raw HMM for this family

Species distribution

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Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence


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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Lectin_C domain has been found. There are 1158 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A0A061AD52 View 3D Structure Click here
A0A096QLV7 View 3D Structure Click here
A0A0G2JU13 View 3D Structure Click here
A0A0G2JUK7 View 3D Structure Click here
A0A0G2JUX8 View 3D Structure Click here
A0A0G2JVR1 View 3D Structure Click here
A0A0G2JZA8 View 3D Structure Click here
A0A0G2K0S4 View 3D Structure Click here
A0A0G2K1B9 View 3D Structure Click here
A0A0G2K314 View 3D Structure Click here
A0A0G2K361 View 3D Structure Click here
A0A0G2K381 View 3D Structure Click here
A0A0G2K3B3 View 3D Structure Click here
A0A0G2K4Q7 View 3D Structure Click here
A0A0G2K5R6 View 3D Structure Click here
A0A0G2K5S8 View 3D Structure Click here
A0A0G2K6C6 View 3D Structure Click here
A0A0G2K9W0 View 3D Structure Click here
A0A0G2KAD3 View 3D Structure Click here
A0A0G2KAZ0 View 3D Structure Click here
A0A0G2KFD2 View 3D Structure Click here
A0A0G2KJW0 View 3D Structure Click here
A0A0G2KNH3 View 3D Structure Click here
A0A0G2KYA2 View 3D Structure Click here
A0A0G2KYS0 View 3D Structure Click here
A0A0G2L593 View 3D Structure Click here
A0A0G2L7J2 View 3D Structure Click here
A0A0G2LA17 View 3D Structure Click here
A0A0G2QC32 View 3D Structure Click here
A0A0R4INM0 View 3D Structure Click here
A0A0R4IQE2 View 3D Structure Click here
A0A0R4IRD4 View 3D Structure Click here
A0A0R4IRN4 View 3D Structure Click here
A0A0R4IWK4 View 3D Structure Click here
A0A0R4IXT8 View 3D Structure Click here
A0A0R4IY99 View 3D Structure Click here
A0A131MBU3 View 3D Structure Click here
A0A140LFQ6 View 3D Structure Click here
A0A140LFS0 View 3D Structure Click here
A0A140LFY4 View 3D Structure Click here