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20  structures 367  species 0  interactions 2827  sequences 48  architectures

Family: CD36 (PF01130)

Summary: CD36 family

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

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Aliases CD36, BDPLT10, CHDS7, FAT, GP3B, GP4, GPIV, PASIV, SCARB3, CD36 molecule
External IDs OMIM: 173510 MGI: 107899 HomoloGene: 73871 GeneCards: CD36
Gene location (Human)
Chromosome 7 (human)
Chr. Chromosome 7 (human)[1]
Chromosome 7 (human)
Genomic location for CD36
Genomic location for CD36
Band 7q21.11 Start 80,369,575 bp[1]
End 80,679,277 bp[1]
RNA expression pattern
PBB GE CD36 206488 s at fs.png
More reference expression data
Species Human Mouse
RefSeq (mRNA)


RefSeq (protein)


Location (UCSC) Chr 7: 80.37 – 80.68 Mb Chr 5: 17.78 – 17.89 Mb
PubMed search [3] [4]
View/Edit Human View/Edit Mouse

CD36 (cluster of differentiation 36), also known as platelet glycoprotein 4, fatty acid translocase (FAT), scavenger receptor class B member 3 (SCARB3), and glycoproteins 88 (GP88), IIIb (GPIIIB), or IV (GPIV) is a protein that in humans is encoded by the CD36 gene. The CD36 antigen is an integral membrane protein found on the surface of many cell types in vertebrate animals. It imports fatty acids inside cells and is a member of the class B scavenger receptor family of cell surface proteins. CD36 binds many ligands including collagen,[5] thrombospondin,[6] erythrocytes parasitized with Plasmodium falciparum,[7] oxidized low density lipoprotein,[8][9] native lipoproteins,[10] oxidized phospholipids,[11] and long-chain fatty acids.[12]

Work in genetically modified rodents suggest a role for CD36 in fatty acid metabolism,[13][14] heart disease,[15] taste,[16][17][18] and dietary fat processing in the intestine.[19] It may be involved in glucose intolerance, atherosclerosis, arterial hypertension, diabetes, cardiomyopathy and Alzheimer's disease.[20]



In humans, rats and mice, CD36 consists of 472 amino acids with a predicted molecular weight of approximately 53,000 Da. However, CD36 is extensively glycosylated and has an apparent molecular weight of 88,000 Da as determined by SDS polyacrylamide gel electrophoresis.[21]


Using Kyte-Doolittle analysis,[22] the amino acid sequence of CD36 predicts a hydrophobic region near each end of the protein large enough to span cellular membranes. Based on this notion and the observation that CD36 is found on the surface of cells, CD36 is thought to have a 'hairpin-like' structure with α-helices at the C- and N- termini projecting through the membrane and a larger extracellular loop (Fig. 1). This topology is supported by transfection experiments in cultured cells using deletion mutants of CD36.[23][24]

Based on the crystal structure of the homologous SCARB2, a model of the extracellullar domain of CD36 has been produced.[25] Like SCARB2, CD36 is proposed to contain an antiparallel β-barrel core with many short α-helices adorning it. The structure is predicted to contain a hydrophobic transport tunnel. Disulfide linkages between 4 of the 6 cysteine residues in the extracellular loop are required for efficient intracellular processing and transport of CD36 to the plasma membrane.[26] It is not clear what role these linkages play on the function of the mature CD36 protein on the cell surface.

Posttranslational modification

Besides glycosylation, additional posttranslational modifications have been reported for CD36. CD36 is modified with 4 palmitoyl chains, 2 on each of the two intracellular domains.[24] The function of these lipid modifications is currently unknown but they likely promote the association of CD36 with the membrane and possibly lipid rafts which appear to be important for some CD36 functions.[27][28] CD36 could be also phosphorylated at Y62, T92, T323,[29] ubiquitinated at K56, K469, K472 and acetylated at K52, K56, K166, K231, K394, K398, K403.[30][31][32]

Protein-protein interactions

In the absence of ligand, membrane bound CD36 exists primarily in a monomeric state. However exposure to the thrombospondin ligand causes CD36 to dimerize. This dimerization has been proposed to play an important role in CD36 signal transduction.[33]


In humans, The gene is located on the long arm of chromosome 7 at band 11.2 (7q11.2[34]) and is encoded by 15 exons that extend over more than 32 kilobases. Both the 5' and the 3' untranslated regions contain introns: the 5' with two and the 3' one. Exons 1, 2 and first 89 nucleotides of exon 3 and as well as exon 15 are non-coding. Exon 3 contains encodes the N-terminal cytoplasmic and transmembrane domains. The C-terminal cytoplasmic and transmembrane regions is encoded by exon 14. The extracellular domain is encoded by the central 11 exons. Alternative splicing of the untranslated regions gives rise to at least two mRNA species.

The transcription initiation site of the CD36 gene has been mapped to 289 nucleotides upstream from the translational start codon and a TATA box and several putative cis regulatory regions lie further 5'. A binding site for PEBP2/CBF factors has been identified between -158 and -90 and disruption of this site reduces expression. The gene is the transcriptional control of the nuclear receptor PPAR/RXR heterodimer (Peroxisome proliferator-activated receptorRetinoid X receptor) and gene expression can be up regulated using synthetic and natural ligands for PPAR and RXR, including the thiazolidinedione class of anti-diabetic drugs and the vitamin A metabolite 9-cis-retinoic acid respectively.

Tissue distribution

CD36 is found on platelets, erythrocytes, monocytes, differentiated adipocytes, skeletal muscle, mammary epithelial cells, spleen cells and some skin microdermal endothelial cells.


The protein itself belongs to the class B scavenger receptor family which includes receptors for selective cholesteryl ester uptake, scavenger receptor class B type I (SR-BI) and lysosomal integral membrane protein II (LIMP-II).

CD36 interacts with a number of ligands, including collagen types I and IV, thrombospondin, erythrocytes parasitized with Plasmodium falciparum, platelet-agglutinating protein p37, oxidized low density lipoprotein and long-chain fatty acids.[citation needed]

On macrophages CD36 forms part of a non-opsonic receptor (the scavenger receptor CD36/alphaV beta3 complex) and is involved[clarification needed] in phagocytosis.[citation needed]

CD36 has also been implicated in hemostasis, thrombosis, malaria, inflammation, lipid metabolism and atherogenesis.[citation needed]

On binding a ligand the protein and ligand are internalized. This internalization is independent of macropinocytosis and occurs by an actin dependent mechanism requiring the activation Src-family kinases, JNK and Rho-family GTPases.[35] Unlike macropinocytosis this process is not affected by inhibitors of phosphatidylinositol 3-kinase or Na+/H+ exchange.

CD36 ligands have also been shown to promote sterile inflammation through assembly of a Toll-like receptor 4 and 6 heterodimer.[36]

Recently, CD36 was linked to store-operated calcium flux, phospholipase A2 activation, and production of prostaglandin E2[37]

CD36 function in long-chain fatty acid uptake and signaling can be irreversibly inhibited by sulfo-N-succinimidyl oleate (SSO), which binds lysine 164 within a hydrophobic pocked shared by several CD36 ligands, e.g. fatty acid and oxLDL.[31]

Clinical significance


Infections with the human malaria parasite Plasmodium falciparum are characterized by sequestration of erythrocytes infected with mature forms of the parasite and CD36 has been shown to be a major sequestration receptor on microvascular endothelial cells. Parasitised erythrocytes adhere to endothelium at the trophozoite/schizonts stage simultaneous with the appearance of the var gene product (erythrocyte membrane protein 1) on the erythrocyte surface. The appearance of Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1) on the erythrocyte surface is a temperature dependent phenomenon which is due to increased protein trafficking to the erythrocyte surface at the raised temperature. PfEMP1 can bind other endothelial receptors - thrombospondin (TSP) and intercellular adhesion molecule 1 (ICAM-1) – in addition to CD36 - and genes other than PfEMP1 also bind to CD36: cytoadherence linked protein (clag) and sequestrin. The PfEMP1 binding site on CD36 is known to be located on exon 5.

CD36 on the surface of the platelets has been shown to be involved in adherence but direct adherence to the endothelium by the infected erythrocytes also occurs. Autoaggregation of infected erythrocytes by platelets has been shown to correlate with severe malaria and cerebral malaria in particular and antiplatelet antibodies may offer some protection.

Several lines of evidence suggest that mutations in CD36 are protective against malaria: mutations in the promoters and within introns and in exon 5 reduce the risk of severe malaria. Gene diversity studies suggest there has been positive selection on this gene presumably due to malarial selection pressure. Dissenting reports are also known suggesting that CD36 is not the sole determinant of severe malaria. In addition a role for CD36 has been found in the clearance of gametocytes (stages I and II).

CD36 has been shown to have a role in the innate immune response to malaria in mouse models.[38] Compared with wild type mice CD36 (-/-) mice the cytokine induction response and parasite clearance were impaired. Earlier peak parasitemias, higher parasite densities and higher mortality were noted. It is thought that CD36 is involved in the Plasmodium falciparum glycophosphatidylinositol (PfGPI) induced MAPK activation and proinflammatory cytokine secretion. When macrophages were exposed to PfGPI the proteins ERK1/2, JNK, p38, and c-Jun became phosphorylated. All these proteins are involved as secondary messengers in the immune response. These responses were blunted in the CD36 (-/-) mice. Also in the CD36 (-/-) macrophages secreted significantly less TNF-alpha on exposure to PfGPI. Work is ongoing to determine how these exactly how these responses provide protection against malaria.

CD36 deficiency and alloimmune thrombocytopenia

CD36 is also known as glycoprotein IV (gpIV) or glycoprotein IIIb (gpIIIb) in platelets and gives rise to the Naka antigen. The Naka null phenotype is found in 0.3% of Caucasians and appears to be asymptomatic. The null phenotype is more common in African (2.5%), Japanese, and other Asian populations (5-11%).

Mutations in the human CD36 gene were first identified in a patient who, despite multiple platelet transfusions, continued to exhibit low platelet levels.[39][40] This condition is known as refractoriness to platelet transfusion. Subsequent studies have shown that CD36 found on the surface of platelets. This antigen is recognized by the monoclonal antibodies (MAbs) OKM5 and OKM8. It is bound by the Plasmodium falciparum protein sequestrin.[41]

Depending on the nature of the mutation in codon 90 CD36 may be absent either on both platelets and monocytes (type 1) or platelets alone (type 2). Type 2 has been divided into two subtypes - a and b. Deficiency restricted to the platelets alone is known as type 2a; if CD36 is also absent from the erythoblasts the phenotype is classified as type 2b.[42] The molecular basis is known for some cases: T1264G in both Kenyans and Gambians; C478T (50%), 539 deletion of AC and 1159 insertion of an A, 1438-1449 deletion and a combined 839-841 deletion GAG and insertion of AAAAC in Japanese.

In a study of 827 apparently healthy Japanese volunteers, type I and II deficiencies were found in 8 (1.0%) and 48 (5.8%) respectively.[43] In 1127 healthy French blood donors (almost all of whom were white Europeans) no CD36 deficiency was found.[44] In a second group only 1 of 301 white test subjects was found to be CD36 deficient. 16 of the 206 sub-Saharan black Africans and 1 of 148 black Caribbeans were found to be CD36 -ve. Three of 13 CD36 -ve persons examined had anti CD36 antibodies. In a group of 250 black American blood donors 6 (2.4%) were found to be Naka antigen negative.[45]

CD36 deficiency may be a cause of post transfusion purpura.[46]

Blood pressure

Below normal levels of CD36 expression in the kidneys has been implicated as a genetic risk factor for hypertension (high blood pressure).[47]

Fatty acid uptake

An association with myocardial fatty acid uptake in humans has been noted.[48] The data suggest a link between hypertrophic cardiomyopathy and CD36 but this needs to be confirmed.


RNAi screening in a Drosophila model has revealed that a member of the CD36 family is required for phagocytosis of Mycobacterium tuberculosis into macrophage phagosomes.[49]


CD36's association with the ability to taste fats has made it a target for various studies regarding obesity and alteration of lipid tasting. CD36 mRNA expression was found to be reduced in taste bud cells (TBC) of obese sand rats (P. obesus) compared to lean controls, implicating an association between CD36 and obesity.[50] Although actual levels of CD36 protein were not different between the obese and control rat cells, Abdoul-Azize et al. hypothesize that the physical distribution of CD36 could differ in obese rat cells.[50] Changes in calcium mediation have been associated with CD36 and obesity as well. Taste bud cells (more specifically, cells from the circumvallate papillae) containing CD36 that were isolated from obese mice exhibited a significantly smaller increase in calcium after fatty acid stimulation when compared to control mice:[51] CD36 associated calcium regulation is impaired when mice are made to be obese (but not in normal weight mice), and this could be a mechanism contributing to behavior changes in the obese mice, such as decreased lipid taste sensitivity and decreased attraction to fats.[51]

There has been some investigation into human CD36 as well. A study examined oral detection of fat in obese subjects with genetic bases for high, medium, and low expression of the CD36 receptor. Those subjects with high CD36 expression were eight times more sensitive to certain fats (oleic acid and triolein) than the subjects with low CD36 expression.[17] Those subjects with an intermediate amount of CD36 expression were sensitive to fat at a level between the high and low groups.[17] This study demonstrates that there is a significant relationship between oral fat sensitivity and the amount of CD36 receptor expression, but further investigation into CD36 could be useful for learning more about lipid tasting in the context of obesity, as CD36 may be a target for therapies in the future.

Establishment of cellular senescence

Upregulation of CD36 could contribute to membrane remodeling during senescence.[52] In response to various senescence‐inducing stimuli, CD36 stimulate NF-κB‐dependent inflammatory cytokine and chemokine production, a phenomenon known as the senescence‐associated secretory phenotype (SASP).[53] This secretory molecule production leads to the onset of a comprehensive senescent cell fate.


CD36 plays a role in the regulation of angiogenesis, which may be a therapeutic strategy for controlling the spread of cancer.[54] Some data from in vitro and animal studies suggested that fatty acid uptake through CD36 may promote cancer cell migration and proliferation in hepatocellular carcinoma, glioblastoma, and potentially other cancers; there was limited data from observational studies in people that low CD36 may correlate with a slightly better outcome in glioblastoma.[55]


CD36 has been shown to interact with FYN.[56][57]

Related proteins

CD36 family
4f7b 1.png
Structure of Limp-II. PDB entry 4f7b
Symbol CD36
Pfam PF01130
InterPro IPR002159

Other human scavenger receptors related to CD36 are SCARB1 and SCARB2 proteins.

See also


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  49. ^ Philips JA, Rubin EJ, Perrimon N (August 2005). "Drosophila RNAi screen reveals CD36 family member required for mycobacterial infection". Science. 309 (5738): 1251–3. doi:10.1126/science.1116006. PMID 16020694. 
  50. ^ a b Abdoul-Azize S, Atek-Mebarki F, Bitam A, Sadou H, Koceïr EA, Khan NA (2013). "Oro-gustatory perception of dietary lipids and calcium signaling in taste bud cells are altered in nutritionally obesity-prone Psammomys obesus". PLoS One. 8 (8): e68532. doi:10.1371/journal.pone.0068532. PMC 3731325Freely accessible. PMID 23936306. 
  51. ^ a b Chevrot M, Bernard A, Ancel D, Buttet M, Martin C, Abdoul-Azize S, Merlin JF, Poirier H, Niot I, Khan NA, Passilly-Degrace P, Besnard P (September 2013). "Obesity alters the gustatory perception of lipids in the mouse: plausible involvement of lingual CD36". Journal of Lipid Research. 54 (9): 2485–94. doi:10.1194/jlr.M039446. PMC 3735945Freely accessible. PMID 23840049. 
  52. ^ Saitou, M., Lizardo, D., Taskent, R., Millner, A., Atilla-Gokcumen, G. E., & Gokcumen, O. (2018). An evolutionary transcriptomics approach links CD36 to membrane remodeling in replicative senescence. bioRxiv 294512. doi:10.1101/294512
  53. ^ Chong M., et al., (2018). CD36 initiates the secretory phenotype during the establishment of cellular senescence. EMBO Reports, e45274 doi:10.15252/embr.201745274
  54. ^ Ge Y, Elghetany MT (2005). "CD36: a multiligand molecule". Laboratory Hematology. 11 (1): 31–7. doi:10.1532/LH96.04056. PMID 15790550. 
  55. ^ Selwan EM, Finicle BT, Kim SM, Edinger AL (April 2016). "Attacking the supply wagons to starve cancer cells to death". FEBS Letters. 590 (7): 885–907. doi:10.1002/1873-3468.12121. PMC 4833639Freely accessible. PMID 26938658. 
  56. ^ Huang MM, Bolen JB, Barnwell JW, Shattil SJ, Brugge JS (September 1991). "Membrane glycoprotein IV (CD36) is physically associated with the Fyn, Lyn, and Yes protein-tyrosine kinases in human platelets". Proceedings of the National Academy of Sciences of the United States of America. 88 (17): 7844–8. doi:10.1073/pnas.88.17.7844. PMC 52400Freely accessible. PMID 1715582. 
  57. ^ Bull HA, Brickell PM, Dowd PM (August 1994). "Src-related protein tyrosine kinases are physically associated with the surface antigen CD36 in human dermal microvascular endothelial cells". FEBS Letters. 351 (1): 41–4. doi:10.1016/0014-5793(94)00814-0. PMID 7521304. 

Further reading

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.

CD36 family Provide feedback

The CD36 family is thought to be a novel class of scavenger receptors. There is also evidence suggesting a possible role in signal transduction. CD36 is involved in cell adhesion.

Literature references

  1. Crombie R, Silverstein R; , J Biol Chem 1998;273:4855-4863.: Lysosomal integral membrane protein II binds thrombospondin-1. Structure-function homology with the cell adhesion molecule CD36 defines a conserved recognition motif. PUBMED:9478926 EPMC:9478926

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR002159

This entry includes CD36 and CD36-like proteins, including SCARB1/2 from vertebrates and SNMP1/2 from flies.

CD36 is a transmembrane, highly glycosylated, 88kDa glycoprotein expressed by monocytes, macrophages, platelets, microvascular endothelial cells and adipose tissues. Platelet glycoprotein IV (GP IV)(GPIIIb) (CD36 antigen) is also called GPIV, OKM5-antigen or PASIV. CD36 recognises oxidized low density lipoprotein, long chain fatty acids, anionic phospholipids, collagen types I, IV and V, thrombospondin (TSP) and Plasmodium falciparum infected erythrocytes. The recognition of apoptotic neutrophils is in co-operation with TSP and avb3. Other ligands may still be unknown.

CD36 is a scavenger receptor for oxidized LDL and shed photoreceptor outer segments and in recognition and phagocytosis of apoptotic cells and is the cell adhesion molecule in platelet adhesion and aggregation, platelet-monocyte and platelet-tumor cell interaction [PUBMED:9478926].

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

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

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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, the UniProtKB sequence database, the NCBI sequence database, and our metagenomics 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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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

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

HMM logo

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.

Note: You can also download the data file for the tree.

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: Pfam-B_1229 (release 3.0)
Previous IDs: none
Type: Family
Sequence Ontology: SO:0100021
Author: Finn RD , Bateman A
Number in seed: 239
Number in full: 2827
Average length of the domain: 349.30 aa
Average identity of full alignment: 21 %
Average coverage of the sequence by the domain: 81.58 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 45638612 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 26.5 26.5
Trusted cut-off 26.9 26.5
Noise cut-off 26.4 26.4
Model length: 467
Family (HMM) version: 21
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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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

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The tree shows the occurrence of this domain across different species. More...


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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 CD36 domain has been found. There are 20 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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