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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2000-1-18
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pubmed:databankReference |
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pubmed:abstractText |
A novel receptor, SorCS, was isolated from murine brain. It shows homology to the mosaic receptor SorLA and the neurotensin receptor sortilin based on a common VPS10 domain which is the hallmark of this new receptor family. In the N-terminus of SorCS two putative cleavage sites for the convertase furin mark the beginning of the VPS10 domain, followed by a module of imperfect leucine-rich repeats and a transmembrane domain. The short intracellular C-terminus contains consensus signals for rapid internalization. The identified putative binding motifs for SH2 and SH3 domains are unique in the family of VPS10 domain receptors. SorCS is predominantly expressed in brain, but also in heart, liver, and kidney. SorCS transcripts detected by in situ hybridization in the murine central nervous system point to a neuronal expression.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Vesicular...,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PEP1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, LDL,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Sorl1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Vesicular Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/sortilin
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0006-291X
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pubmed:author |
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pubmed:copyrightInfo |
Copyright 1999 Academic Press.
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pubmed:issnType |
Print
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pubmed:day |
20
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pubmed:volume |
266
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
347-51
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:10600506-Adaptor Proteins, Vesicular Transport,
pubmed-meshheading:10600506-Amino Acid Sequence,
pubmed-meshheading:10600506-Animals,
pubmed-meshheading:10600506-Brain,
pubmed-meshheading:10600506-Cloning, Molecular,
pubmed-meshheading:10600506-Fungal Proteins,
pubmed-meshheading:10600506-In Situ Hybridization,
pubmed-meshheading:10600506-Membrane Glycoproteins,
pubmed-meshheading:10600506-Membrane Transport Proteins,
pubmed-meshheading:10600506-Mice,
pubmed-meshheading:10600506-Molecular Sequence Data,
pubmed-meshheading:10600506-Nerve Tissue Proteins,
pubmed-meshheading:10600506-RNA, Messenger,
pubmed-meshheading:10600506-Receptors, Cell Surface,
pubmed-meshheading:10600506-Receptors, LDL,
pubmed-meshheading:10600506-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:10600506-Sequence Alignment,
pubmed-meshheading:10600506-Sequence Homology, Amino Acid,
pubmed-meshheading:10600506-Vesicular Transport Proteins
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pubmed:year |
1999
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pubmed:articleTitle |
Identification and characterization of SorCS, a third member of a novel receptor family.
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pubmed:affiliation |
Zentrum für Molekulare Neurobiologie, Universität Hamburg, Martinistrasse 52, Hamburg, 20246, Germany. hermey@zmnh.uni-hamburg.de
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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