Gal_Lectin | |||||||||
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Identifiers | |||||||||
Symbol | Gal_Lectin | ||||||||
Pfam | PF02140 | ||||||||
InterPro | IPR000922 | ||||||||
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In molecular biology, the galactose binding lectin domain is a protein domain. It is found in many proteins including the lectin purified from sea urchin (Anthocidaris crassispina) eggs, SUEL. This lectin exists as a disulfide-linked homodimer of two subunits; the dimeric form is essential for hemagglutination activity. [1] The sea urchin egg lectin (SUEL) forms a new class of lectins. Although SUEL was first isolated as a D-galactoside binding lectin, it was later shown that it binds to L-rhamnose preferentially. [1] [2] L-rhamnose and D-galactose share the same hydroxyl group orientation at C2 and C4 of the pyranose ring structure.
A cysteine-rich domain (the galactose binding lectin domain) homologous to the SUEL protein has been identified in the following proteins: [3] [4] [5]
Histone acetyltransferase p300 also known as p300 HAT or E1A-associated protein p300 also known as EP300 or p300 is an enzyme that, in humans, is encoded by the EP300 gene. It functions as histone acetyltransferase that regulates transcription of genes via chromatin remodeling by allowing histone proteins to wrap DNA less tightly. This enzyme plays an essential role in regulating cell growth and division, prompting cells to mature and assume specialized functions (differentiate), and preventing the growth of cancerous tumors. The p300 protein appears to be critical for normal development before and after birth.
A latrotoxin is a high-molecular mass neurotoxin found in the venom of spiders of the genus Latrodectus as well as at least one species of another genus in the same family, Steatoda nobilis. Latrotoxins are the main active components of the venom and are responsible for the symptoms of latrodectism.
POU domain, class 2, transcription factor 1 is a protein that in humans is encoded by the POU2F1 gene.
Filamin A, alpha (FLNA) is a protein that in humans is encoded by the FLNA gene.
Interferon-alpha/beta receptor beta chain is a protein that in humans is encoded by the IFNAR2 gene.
Beta-galactoside alpha-2,6-sialyltransferase 1 is an enzyme that in humans is encoded by the ST6GAL1 gene.
Latrophilin 1 is a protein that in humans is encoded by the ADGRL1 gene. It is a member of the adhesion-GPCR family of receptors. Family members are characterized by an extended extracellular region with a variable number of protein domains coupled to a TM7 domain via a domain known as the GPCR-Autoproteolysis INducing (GAIN) domain.
Latrophilin 3 is a protein that in humans is encoded by the ADGRL3 gene.
Alpha-actinin-1 is a protein that in humans is encoded by the ACTN1 gene.
Latrophilin 2 is a protein that in humans is encoded by the ADGRL2 gene.
Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 is a protein that in humans is encoded by the GNB1 gene.
Guanine nucleotide-binding protein G(o) subunit alpha is a protein that in humans is encoded by the GNAO1 gene.
ARF GTPase-activating protein GIT1 is an enzyme that in humans is encoded by the GIT1 gene.
Galectin-3-binding protein is a protein that in humans is encoded by the LGALS3BP gene.
Interleukin 13 receptor, alpha 1, also known as IL13RA1 and CD213A1, is a human gene.
Glutamate receptor-interacting protein 2 is a protein that in humans is encoded by the GRIP2 gene.
Interferon-alpha/beta receptor alpha chain is a protein that in humans is encoded by the IFNAR1 gene.
In molecular biology, the jacalin-like lectin domain is a mannose-binding lectin domain with a beta-prism fold consisting of three 4-stranded beta-sheets, with an internal pseudo 3-fold symmetry. Some lectins in this group stimulate distinct T- and B-cell functions, such as Jacalin, which binds to the T-antigen and acts as an agglutinin. This domain is found in 1 to 6 copies in lectins. The domain is also found in the salt-stress induced protein from rice and an animal prostatic spermine-binding protein.
In molecular biology, the leguminous lectin family is a family of lectin proteins.
In molecular biology the L-like lectin domain is a protein domain found in lectins which are similar to the leguminous plant lectins.