Summary: Scavenger receptor cysteine-rich domain
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Scavenger receptor cysteine-rich protein domain Edit Wikipedia article
structure of m2bp scavenger receptor cysteine-rich domain
In molecular biology, the protein domain SRCR is short for Scavenger receptor cysteine-rich domain. They are found solely in eukaryotes. These domains are present on the cell membrane and have a role in binding to specific ligands and are often found to be involved with the immune system.
The speract receptor found in egg, is a transmembrane glycoprotein. Other members of this family include the macrophage scavenger receptor type I (a membrane glycoprotein implicated in the pathologic deposition of cholesterol in arterial walls during artherogenesis), an enteropeptidase and T-cell surface glycoprotein CD5 (may act as a receptor in regulating T-cell proliferation).
- Hohenester E, Sasaki T, Timpl R (1999). "Crystal structure of a scavenger receptor cysteine-rich domain sheds light on an ancient superfamily.". Nat Struct Biol 6 (3): 228–32. doi:10.1038/6669. PMID 10074941.
- Liu L, Yang J, Qiu L, Wang L, Zhang H, Wang M et al. (2011). "A novel scavenger receptor-cysteine-rich (SRCR) domain containing scavenger receptor identified from mollusk mediated PAMP recognition and binding.". Dev Comp Immunol 35 (2): 227–39. doi:10.1016/j.dci.2010.09.010. PMID 20888856.
- Resnick D, Pearson A, Krieger M (January 1994). "The SRCR superfamily: a family reminiscent of the Ig superfamily". Trends Biochem. Sci. 19 (1): 5–8. doi:10.1016/0968-0004(94)90165-1. PMID 8140623.
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These domains are disulphide rich extracellular domains. These domains are found in several extracellular receptors and may be involved in protein-protein interactions.
Internal database links
|SCOOP:||Hepsin-SRCR REGB_T4 DUF3027 YecR SRCR_2|
|Similarity to PfamA using HHSearch:||SRCR_2|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR001190
The scavenger receptor cysteine-rich (SRCR) domain is an ancient and highly conserved domain of about 110 residues which is found in diverse secreted and cell-surface proteins, like the type I scavenger receptor, the speract receptor, CD5/Ly-1, CD6, or complement factor I [PUBMED:1978939]. Tandem repeats of SRCR domains are common in the membrane bound proteins. Most SRCR domains have six to eight cysteines that participate in intradomain disulfide bonds. SRCR domains have been subdivided into two groups, A and B, primarily on the differences in the spacing pattern between the cysteine residues [PUBMED:8140623, PUBMED:10074941].
Although the biochemical functions of SRCR domains have not been established with certainty, they are likely to mediate protein-protein interactions and ligand binding [PUBMED:8140623, PUBMED:10074941].
Determination of the crystal structure of the SRCR domain of M2BP reveals that the M2NP SRCR adopts a compact fold of approximate dimensions 22 x 26 x 30 Angstrom, organised around a curved six-stranded beta-sheet cradling an alpha- helix [PUBMED:10074941].
|Cellular component||membrane (GO:0016020)|
|Molecular function||scavenger receptor activity (GO:0005044)|
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We make a range of alignments for each Pfam-A family:
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Curation and family details
|Seed source:||Reference |
|Number in seed:||81|
|Number in full:||11334|
|Average length of the domain:||96.30 aa|
|Average identity of full alignment:||34 %|
|Average coverage of the sequence by the domain:||45.14 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||14|
|Download:||download the raw HMM for this family|
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There are 2 interactions for this family. More...
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 SRCR domain has been found. There are 10 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 seqence.
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