| Identifier | PRSTNOIDEP2R [View Relations] [View Alignment]
|
| Accession | PR00581 |
| No. of Motifs | 8 |
| Creation Date | 25-SEP-1996 (UPDATE 07-JUN-1999) |
| Title | Prostanoid EP2 receptor signature |
| Database References | PRINTS; PR90007 7TM; PR90006 GPCRCLAN; PR00237 GPCRRHODOPSN
PRINTS; PR01788 PROSTANOIDR; PR00428 PROSTAGLNDNR
INTERPRO; IPR001923 |
| Literature References | 1. ATTWOOD, T.K. AND FINDLAY, J.B.C.
Fingerprinting G protein-coupled receptors.
PROTEIN ENG. 7(2) 195-203 (1994).
2. ATTWOOD, T.K. AND FINDLAY, J.B.C.
G protein-coupled receptor fingerprints.
7TM, VOLUME 2, EDS. G.VRIEND AND B.BYWATER (1993).
3. BIRNBAUMER, L.
G proteins in signal transduction.
ANNU.REV.PHARMACOL.TOXICOL. 30 675-705 (1990).
4. CASEY, P.J. AND GILMAN, A.G.
G protein involvement in receptor-effector coupling.
J.BIOL.CHEM. 263(6) 2577-2580 (1988).
5. ATTWOOD, T.K. AND FINDLAY, J.B.C.
Design of a discriminating fingerprint for G protein-coupled receptors.
PROTEIN ENG. 6(2) 167-176 (1993).
6. WATSON, S. AND ARKINSTALL,
Prostanoids.
IN THE G PROTEIN-LINKED RECEPTOR FACTSBOOK, ACADEMIC PRESS, pp239-251.
|
| Documentation | G protein-coupled receptors (GPCRs) constitute a vast protein family that
encompasses a wide range of functions (including various autocrine, para-
crine and endocrine processes). They show considerable diversity at the
sequence level, on the basis of which they can be separated into distinct
groups. We use the term clan to describe the GPCRs, as they embrace a group
of families for which there are indications of evolutionary relationship,
but between which there is no statistically significant similarity in
sequence [1]. The currently known clan members include the rhodopsin-like
GPCRs, the secretin-like GPCRs, the cAMP receptors, the fungal mating
pheromone receptors, and the metabotropic glutamate receptor family.
The rhodopsin-like GPCRs themselves represent a widespread protein family
that includes hormone, neurotransmitter and light receptors, all of
which transduce extracellular signals through interaction with guanine
nucleotide-binding (G) proteins. Although their activating ligands vary
widely in structure and character, the amino acid sequences of the
receptors are very similar and are believed to adopt a common structural
framework comprising 7 transmembrane (TM) helices [3-5].
Prostanoids (prostaglandins (PG) and thromboxanes (TX)) mediate a wide
variety of actions and play important physiological roles in the cardio-
vascular and immune systems, and in pain sensation in peripheral systems
[6]. PGI2 and TXA2 have opposing actions, involving regulation of the
interaction of platelets with the vascular endothelium, while PGE2, PGI2
and PGD2 are powerful vasodilators and potentiate the action of various
autocoids to induce plasma extravasation and pain sensation. To date,
evidence for at least 5 classes of prostanoid receptor has been obtained.
However, identification of subtypes and their distribution is hampered by
expression of more than one receptor within a tissue, coupled with poor
selectivity of available agonists and antagonists.
EP2 receptors mediate vasodilation, bronchodilation and relaxation of
intestinal smooth muscle, and stimulate fluid secretion in the intestine
[6]. The receptors activate adenylate cyclase through Gs [6].
PRSTNOIDEP2R is an 8-element fingerprint that provides a signature for the
prostanoid EP2 receptors. The fingerprint was derived from an initial
alignment of 3 sequences: the motifs were drawn from conserved sections
within either loop or N- and C-terminal regions, focusing on those areas
of the alignment that characterise the prostanoid EP2 receptors but
distinguish them from the rest of the rhodopsin-like superfamily - motifs
1 and 2 span the N-terminus; motif 3 spans the first cytoplasmic loop; motif
4 lies in the first external loop; motifs 5 and 6 lie in the third
cytoplasmic loop; motif 7 spans the third external loop; and motif 8 lies
at the C-terminus. A single iteration on OWL28.0 was required to reach
convergence, no further sequences being identified beyond the starting set.
An update on SPTR37_9f identified a true set of 3 sequences.
|
| Summary Information | 3 codes involving 8 elements
0 codes involving 7 elements
0 codes involving 6 elements
0 codes involving 5 elements
0 codes involving 4 elements
0 codes involving 3 elements
0 codes involving 2 elements
|
| Composite Feature Index | | 8 | 3 | 3 | 3 | 3 | 3 | 3 | 3 | 3 | | 7 | 0 | 0 | 0 | 0 | 0 | 0 | 0 | 0 | | 6 | 0 | 0 | 0 | 0 | 0 | 0 | 0 | 0 | | 5 | 0 | 0 | 0 | 0 | 0 | 0 | 0 | 0 | | 4 | 0 | 0 | 0 | 0 | 0 | 0 | 0 | 0 | | 3 | 0 | 0 | 0 | 0 | 0 | 0 | 0 | 0 | | 2 | 0 | 0 | 0 | 0 | 0 | 0 | 0 | 0 | | 1 | 2 | 3 | 4 | 5 | 6 | 7 | 8 |
|
| True Positives | PE22_HUMAN PE22_MOUSE PE22_RAT |
| Sequence Titles | PE22_HUMAN Prostaglandin E2 receptor, EP2 subtype (Prostanoid EP2 receptor) (PGE receptor, EP2 subtype) - Homo sapiens (Human).
PE22_MOUSE Prostaglandin E2 receptor, EP2 subtype (Prostanoid EP2 receptor) (PGE receptor, EP2 subtype) - Mus musculus (Mouse).
PE22_RAT Prostaglandin E2 receptor, EP2 subtype (Prostanoid EP2 receptor) (PGE receptor, EP2 subtype) - Rattus norvegicus (Rat).
|
| Scan History | OWL28_2 1 50 NSINGLE
SPTR37_9f 2 4 NSINGLE
|
| Initial Motifs | Motif 1 width=13
Element Seqn Id St Int Rpt
EDCKSRQWLLSGE MUSPEREP2S 12 12 -
EDCETRQWLPPGE O15055 11 11 -
ENCESRQYLLSDE RNU48858 12 12 -
Motif 2 width=13
Element Seqn Id St Int Rpt
ESPAISSVMFSAG MUSPEREP2S 24 -1 -
ESPAISSVMFSAG O15055 23 -1 -
ESPAISSVMFTAG RNU48858 24 -1 -
Motif 3 width=21
Element Seqn Id St Int Rpt
RRWRGDTGCSAGSRTSISLFH MUSPEREP2S 49 12 -
RRWRGDVGCSAGRRSSLSLFH O15055 48 12 -
RRWRGDTGCSAGSRTSISLFH RNU48858 49 12 -
Motif 4 width=15
Element Seqn Id St Int Rpt
RNQTLVALAPESHAC MUSPEREP2S 96 26 -
RNQTLVALAPESRAC O15055 95 26 -
RNQTLVALAPESRAC RNU48858 96 26 -
Motif 5 width=16
Element Seqn Id St Int Rpt
RSRRSRCGLSGSSLRG MUSPEREP2S 229 118 -
RSRRSRCGPSLGSGRG O15055 228 118 -
RSKRSRCGLSGSSLRG RNU48858 229 118 -
Motif 6 width=18
Element Seqn Id St Int Rpt
PGSRRRGERTSMAEETDH MUSPEREP2S 245 0 -
PGARRRGERVSMAEETDH O15055 245 1 -
PGSRRRGERTSMAEETDH RNU48858 245 0 -
Motif 7 width=19
Element Seqn Id St Int Rpt
FTIFAYMDETSSLKEKWDL MUSPEREP2S 280 17 -
FTIFAYMNETSSRKEKWDL O15055 280 17 -
FTIFAYMDETSSRKEKWDL RNU48858 280 17 -
Motif 8 width=18
Element Seqn Id St Int Rpt
RLMRSVLCCRTSLRTQEA MUSPEREP2S 324 25 -
RLMRSVLCCRISLRTQDA O15055 324 25 -
RLMRSVLCCRTSLRAPEA RNU48858 324 25 -
|
| Final Motifs | Motif 1 width=13
Element Seqn Id St Int Rpt
EDCKSRQWLLSGE PE22_MOUSE 12 12 -
ENCESRQYLLSDE PE22_RAT 12 12 -
EDCETRQWLPPGE PE22_HUMAN 11 11 -
Motif 2 width=13
Element Seqn Id St Int Rpt
ESPAISSVMFSAG PE22_MOUSE 24 -1 -
ESPAISSVMFTAG PE22_RAT 24 -1 -
ESPAISSVMFSAG PE22_HUMAN 23 -1 -
Motif 3 width=21
Element Seqn Id St Int Rpt
RRWRGDTGCSAGSRTSISLFH PE22_MOUSE 49 12 -
RRWRGDTGCSAGSRTSISLFH PE22_RAT 49 12 -
RRWRGDVGCSAGRRSSLSLFH PE22_HUMAN 48 12 -
Motif 4 width=15
Element Seqn Id St Int Rpt
RNQTLVALAPESHAC PE22_MOUSE 96 26 -
RNQTLVALAPESRAC PE22_RAT 96 26 -
RNQTLVALAPESRAC PE22_HUMAN 95 26 -
Motif 5 width=16
Element Seqn Id St Int Rpt
RSRRSRCGLSGSSLRG PE22_MOUSE 229 118 -
RSKRSRCGLSGSSLRG PE22_RAT 229 118 -
RSRRSRCGPSLGSGRG PE22_HUMAN 228 118 -
Motif 6 width=18
Element Seqn Id St Int Rpt
PGSRRRGERTSMAEETDH PE22_MOUSE 245 0 -
PGSRRRGERTSMAEETDH PE22_RAT 245 0 -
PGARRRGERVSMAEETDH PE22_HUMAN 245 1 -
Motif 7 width=19
Element Seqn Id St Int Rpt
FTIFAYMDETSSLKEKWDL PE22_MOUSE 280 17 -
FTIFAYMDETSSRKEKWDL PE22_RAT 280 17 -
FTIFAYMNETSSRKEKWDL PE22_HUMAN 280 17 -
Motif 8 width=18
Element Seqn Id St Int Rpt
RLMRSVLCCRTSLRTQEA PE22_MOUSE 324 25 -
RLMRSVLCCRTSLRAPEA PE22_RAT 324 25 -
RLMRSVLCCRISLRTQDA PE22_HUMAN 324 25 -
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