Summary: Amino terminal of the G-protein receptor rhodopsin
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Amino terminal of the G-protein receptor rhodopsin Provide feedback
Rhodopsin is the archetypal G-protein-coupled receptor. Such receptors participate in virtually all physiological processes, as signalling molecules. They utilise heterotrimeric guanosine triphosphate (GTP)-binding proteins to transduce extracellular signals to intracellular events. Rhodopsin is important because of the pivotal role it plays in visual signal transduction. Rhodopsin is a dimeric transmembrane protein and its intradiskal surface consists of this amino terminal domain and three loops connecting six of the seven transmembrane helices. The N-terminus is a compact domain of alpha-helical regions with breaks and bends at proline residues outside the membrane . The transmembrane part of rhodopsin is represented by 7tm_1 (PF00001). The N-terminal domain is extracellular is and is necessary for successful dimerisation and molecular stability .
Yeagle PL, Salloum A, Chopra A, Bhawsar N, Ali L, Kuzmanovski G, Alderfer JL, Albert AD; , J Pept Res. 2000;55:455-465.: Structures of the intradiskal loops and amino terminus of the G-protein receptor, rhodopsin. PUBMED:10888202 EPMC:10888202
Fotiadis D, Jastrzebska B, Philippsen A, Muller DJ, Palczewski K, Engel A; , Curr Opin Struct Biol. 2006;16:252-259.: Structure of the rhodopsin dimer: a working model for G-protein-coupled receptors. PUBMED:16567090 EPMC:16567090
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This tab holds annotation information from the InterPro database.
InterPro entry IPR019477
Rhodopsin is the archetypal G-protein-coupled receptor. Such receptors participate in virtually all physiological processes as signalling molecules. They utilise heterotrimeric guanosine triphosphate (GTP)-binding proteins to transduce extracellular signals to intracellular events. Rhodopsin is important because of the pivotal role it plays in visual signal transduction. It is a dimeric transmembrane protein whose intradiskal surface consists of an N-terminal domain and three loops connecting six of the seven transmembrane helices. The N-terminal domain is a compact alpha-helical region with breaks and bends at proline residues outside the membrane [PUBMED:10888202]. This entry represents the N-terminal domain, while the transmembrane region is represented by (INTERPRO). The N-terminal domain is extracellular is and is necessary for successful dimerisation and molecular stability [PUBMED:16567090].
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|Seed source:||Gene3D, pdb_1edx|
|Author:||Finn RD, Coggill PC|
|Number in seed:||17|
|Number in full:||2285|
|Average length of the domain:||30.00 aa|
|Average identity of full alignment:||80 %|
|Average coverage of the sequence by the domain:||15.25 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||4|
|Download:||download the raw HMM for this family|
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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 Rhodopsin_N domain has been found. There are 37 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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