SPRINT Home UMBER Home Contents Standard Search Advanced Search Relation Search

==SPRINT==> PRINTS View



  selected as


PR00636

Identifier
ANGIOTENSN2R  [View Relations]  [View Alignment]  
Accession
PR00636
No. of Motifs
9
Creation Date
08-DEC-1996  (UPDATE 06-JUN-1999)
Title
AT2 angiotensin II receptor signature
Database References
PRINTS; PR90007 7TM; PR90006 GPCRCLAN; PR00237 GPCRRHODOPSN
PRINTS; PR00241 ANGIOTENSINR
INTERPRO; IPR000147
GCRDB; GCR_0890; GCR_1007; GCR_1010; GCR_0807; GCR_0816
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, S.
Angiotensin.
IN THE G PROTEIN-LINKED RECEPTOR FACTSBOOK, ACADEMIC PRESS, pp55-59.

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]. 
 
Angiotensin II is the principal mediator of the renin-angiotensin system;
it circulates in the bloodstream, stimulating vasoconstriction and
retention of salt and water [6]. It also stimulates increased fluid intake
and regulates the neuroendocrine system. Many of its actions are mediated
by release of hormones from endocrine glands, e.g. vasopressin, catechol-
amines, aldosterone, growth-hormone, etc.. Molecular cloning studies have
identifed 2 major receptor subtypes, designated AT1 and AT2. 
 
The AT2 receptor is abundant in the adrenal medulla, uterus and brain [6].
Activation of AT2 receptors has been reported to decrease basal cGMP levels
and to inhibit atrial natriuretic peptide-stimulated formation of cGMP,
possibly by activation of a protein tyrosine phosphatase [6]. 
 
ANGIOTENSN2R is a 9-element fingerprint that provides a signature for AT2
angiotensin II receptors. The fingerprint was derived from an initial
alignment of 4 sequences: the motifs were drawn from conserved sections
largely within loop or N- and C-terminal regions, focusing on those areas
of the alignment that characterise the AT2 receptors but distinguish them
from the rest of the angiotensin family - motifs 1 and 2 span the N-terminus;
motif 3 spans the first cytoplasmic loop; motif 4 spans the second
cytoplasmic loop, leading into TM domain 4; motifs 5 and 6 span the second
external loop; motif 7 lies in the third cytoplasmic loop; and motifs 8 and
9 span the C-terminus. A single iteration on OWL29.0 was required to reach
convergence, no further sequences being identified beyond the starting set.
A single partial match was also found, S81979, an ovine angtiotensin II
receptor fragment.
 
An update on SPTR37_9f identified a true set of 3 sequences.
Summary Information
3 codes involving  9 elements
0 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
9333333333
8000000000
7000000000
6000000000
5000000000
4000000000
3000000000
2000000000
123456789
True Positives
AG22_HUMAN    AG22_MOUSE    AG22_RAT      
Sequence Titles
AG22_HUMAN  TYPE-2 ANGIOTENSIN II RECEPTOR (AT2) - HOMO SAPIENS (HUMAN). 
AG22_MOUSE TYPE-2 ANGIOTENSIN II RECEPTOR (AT2) - MUS MUSCULUS (MOUSE).
AG22_RAT TYPE-2 ANGIOTENSIN II RECEPTOR (AT2) - RATTUS NORVEGICUS (RAT).
Scan History
OWL29_0    1  50   NSINGLE    
SPTR37_9f 2 4 NSINGLE
Initial Motifs
Motif 1  width=20
Element Seqn Id St Int Rpt
ATTSKNITSGLHFGLVNISG AGG2_HUMAN 8 8 -
ATTSKNITSGLHFGLVNISG HSU15592 8 8 -
AATSRNITSSLPFDNLNATG AG22_RAT 8 8 -
AATSRNITSSRPFDNLNATG AG22_MOUSE 8 8 -

Motif 2 width=19
Element Seqn Id St Int Rpt
GNNESTLNCSQKPSDKHLD HSU15592 27 -1 -
GTNESAFNCSHKPADKHLE AG22_RAT 27 -1 -
GTNESAFNCSHKPSDKHLE AG22_MOUSE 27 -1 -
GNNESTLNCSQKPSDKHLD AGG2_HUMAN 27 -1 -

Motif 3 width=15
Element Seqn Id St Int Rpt
VVTLFCCQKGPKKVS AGG2_HUMAN 65 19 -
VVTLFCCQKGPKKVS HSU15592 65 19 -
VVSLFCCQKGPKKVS AG22_MOUSE 65 19 -
VVSLFCCQKGPKKVS AG22_RAT 65 19 -

Motif 4 width=19
Element Seqn Id St Int Rpt
QSVIYPFLSQRRNPWQASY HSU15592 144 64 -
QSVIYPFLSQRRNPWQASY AG22_RAT 144 64 -
QSVIYPFLSQRRNPWQASY AG22_MOUSE 144 64 -
QSVIYPFLSQRRNPWQASY AGG2_HUMAN 144 64 -

Motif 5 width=17
Element Seqn Id St Int Rpt
TFYFRDVRTIEYLGVNA AGG2_HUMAN 178 15 -
TFYFRDVRTIEYLGVNA HSU15592 178 15 -
TFYFRDVRTIEYLGVNA AG22_MOUSE 178 15 -
TFYFRDVRTIEYLGVNA AG22_RAT 178 15 -

Motif 6 width=15
Element Seqn Id St Int Rpt
IMAFPPEKYAQWSAG HSU15592 196 1 -
IMAFPPEKYAQWSAG AG22_MOUSE 196 1 -
IMAFPPEKYAQWSAG AG22_RAT 196 1 -
IMAFPPEKYAQWSAG AGG2_HUMAN 196 1 -

Motif 7 width=20
Element Seqn Id St Int Rpt
FGIRKHLLKTNSYGKNRITR AGG2_HUMAN 232 21 -
FGIRKHLLKTNSYGKNRITR HSU15592 232 21 -
FGIRKHLLKTNSYGKNRITR AG22_RAT 232 21 -
FGIRKHLLKTNSYGKNRITR AG22_MOUSE 232 21 -

Motif 8 width=19
Element Seqn Id St Int Rpt
FQQKLRSVFRVPITWLQGK HSU15592 325 73 -
FQQKLRSVFRVPITWLQGK AG22_MOUSE 325 73 -
FQQKLRSVFRVPITWLQGK AG22_RAT 325 73 -
FQQKLRSVFRVPITWLQGK AGG2_HUMAN 325 73 -

Motif 9 width=19
Element Seqn Id St Int Rpt
KRESMSCRKSSSLREMETF AGG2_HUMAN 343 -1 -
KRESMSCRKSSSLREMETF HSU15592 343 -1 -
KRETMSCRKGSSLREMDTF AG22_MOUSE 343 -1 -
KRETMSCRKSSSLREMDTF AG22_RAT 343 -1 -
Final Motifs
Motif 1  width=20
Element Seqn Id St Int Rpt
AATSRNITSSLPFDNLNATG AG22_RAT 8 8 -
AATSRNITSSRPFDNLNATG AG22_MOUSE 8 8 -
ATTSKNITSGLHFGLVNISG AG22_HUMAN 8 8 -

Motif 2 width=19
Element Seqn Id St Int Rpt
GTNESAFNCSHKPADKHLE AG22_RAT 27 -1 -
GTNESAFNCSHKPSDKHLE AG22_MOUSE 27 -1 -
GNNESTLNCSQKPSDKHLD AG22_HUMAN 27 -1 -

Motif 3 width=15
Element Seqn Id St Int Rpt
VVSLFCCQKGPKKVS AG22_RAT 65 19 -
VVSLFCCQKGPKKVS AG22_MOUSE 65 19 -
VVTLFCCQKGPKKVS AG22_HUMAN 65 19 -

Motif 4 width=19
Element Seqn Id St Int Rpt
QSVIYPFLSQRRNPWQASY AG22_RAT 144 64 -
QSVIYPFLSQRRNPWQASY AG22_MOUSE 144 64 -
QSVIYPFLSQRRNPWQASY AG22_HUMAN 144 64 -

Motif 5 width=17
Element Seqn Id St Int Rpt
TFYFRDVRTIEYLGVNA AG22_RAT 178 15 -
TFYFRDVRTIEYLGVNA AG22_MOUSE 178 15 -
TFYFRDVRTIEYLGVNA AG22_HUMAN 178 15 -

Motif 6 width=15
Element Seqn Id St Int Rpt
IMAFPPEKYAQWSAG AG22_RAT 196 1 -
IMAFPPEKYAQWSAG AG22_MOUSE 196 1 -
IMAFPPEKYAQWSAG AG22_HUMAN 196 1 -

Motif 7 width=20
Element Seqn Id St Int Rpt
FGIRKHLLKTNSYGKNRITR AG22_RAT 232 21 -
FGIRKHLLKTNSYGKNRITR AG22_MOUSE 232 21 -
FGIRKHLLKTNSYGKNRITR AG22_HUMAN 232 21 -

Motif 8 width=19
Element Seqn Id St Int Rpt
FQQKLRSVFRVPITWLQGK AG22_RAT 325 73 -
FQQKLRSVFRVPITWLQGK AG22_MOUSE 325 73 -
FQQKLRSVFRVPITWLQGK AG22_HUMAN 325 73 -

Motif 9 width=19
Element Seqn Id St Int Rpt
KRETMSCRKSSSLREMDTF AG22_RAT 343 -1 -
KRETMSCRKGSSLREMDTF AG22_MOUSE 343 -1 -
KRESMSCRKSSSLREMETF AG22_HUMAN 343 -1 -