Source:http://linkedlifedata.com/resource/pubmed/id/19535143
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
13
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pubmed:dateCreated |
2009-7-21
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pubmed:abstractText |
Glycoproteins of the scavenger receptor cysteine-rich (SRCR) superfamily contain one or more protein modules homologous to the membrane-distal domain of macrophage scavenger receptor I. These domains can be found in the extracellular regions of membrane proteins and in secreted glycoproteins, from the most primitive species to vertebrates. A systematic, bioinformatics-based search for putative human proteins related to the forty-seven known human group B SRCR domains identified a new family member that we have called Soluble Scavenger with 5 Domains (SSc5D). SSc5D is a new soluble protein whose expression is restricted to monocytes/macrophages and T-lymphocytes, and is particularly enriched in the placenta. The gene encoding SSc5D spans 30kb of genomic DNA, and contains fourteen exons producing a 4.8kb-long mRNA. The mature polypeptide is predicted to consist of 1573 amino acids comprising, towards the N-terminus, five very similar SRCR domains that are highly conserved among non-marsupial mammals, and a large (>250nm), very heavily glycosylated, mucin-like sequence towards the C-terminus. Each of the SRCR domains is encoded by a single exon, and contains eight cysteine residues, as observed for all other group B SRCR domains. A shorter isoform encoded by a weakly expressed, alternatively spliced transcript, which lacks the mucin-like C-terminal region, was also identified. It seems likely that SSc5D has a role at the interface between adaptive and innate immunity, or in placental function.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1872-9142
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pubmed:author |
pubmed-author:CarmoAlexandre MAM,
pubmed-author:CastroMónica A AMA,
pubmed-author:DavisSimon JSJ,
pubmed-author:EvansEdward JEJ,
pubmed-author:GonçalvesCarine MCM,
pubmed-author:HenriquesTelmoT,
pubmed-author:MoreiraAlexandraA,
pubmed-author:OliveiraCarlaC,
pubmed-author:OliveiraMarta IMI,
pubmed-author:PinheiroHugo CHC,
pubmed-author:SreenuVattipally BVB
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pubmed:issnType |
Electronic
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pubmed:volume |
46
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2585-96
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pubmed:dateRevised |
2010-4-30
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pubmed:meshHeading |
pubmed-meshheading:19535143-Amino Acid Sequence,
pubmed-meshheading:19535143-Blotting, Northern,
pubmed-meshheading:19535143-Cell Line,
pubmed-meshheading:19535143-Cell Line, Tumor,
pubmed-meshheading:19535143-Cloning, Molecular,
pubmed-meshheading:19535143-Female,
pubmed-meshheading:19535143-Gene Expression Profiling,
pubmed-meshheading:19535143-Humans,
pubmed-meshheading:19535143-Macrophages,
pubmed-meshheading:19535143-Molecular Sequence Data,
pubmed-meshheading:19535143-Monocytes,
pubmed-meshheading:19535143-Phylogeny,
pubmed-meshheading:19535143-Placenta,
pubmed-meshheading:19535143-Protein Isoforms,
pubmed-meshheading:19535143-RNA, Messenger,
pubmed-meshheading:19535143-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:19535143-Scavenger Receptors, Class B,
pubmed-meshheading:19535143-Sequence Homology, Amino Acid,
pubmed-meshheading:19535143-T-Lymphocytes
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pubmed:year |
2009
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pubmed:articleTitle |
Molecular cloning and analysis of SSc5D, a new member of the scavenger receptor cysteine-rich superfamily.
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pubmed:affiliation |
Institute for Molecular and Cellular Biology, Porto, Portugal.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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