SPRINT Home UMBER Home Contents Standard Search Advanced Search Relation Search

==SPRINT==> PRINTS View



  selected as


PR00443

Identifier
GPROTEINAS  [View Relations]  [View Alignment]  
Accession
PR00443
No. of Motifs
6
Creation Date
12-JUN-1995  (UPDATE 17-DEC-1999)
Title
G-protein alpha subunit group S signature
Database References
PRINTS; PR00318 GPROTEINA
INTERPRO; IPR000367
PDB; 1GIA
SCOP; 1GIA
Literature References
1. LINDER, M.E. AND GILMAN, A.G.
G proteins.
SCI.AM. 267 56 (1992).
 
2. KAZIRO, Y., ITOH, H., KOZASA, T., NAKAFUKU, M. AND SATOH, T.
Structure and function of signal-transducing GTP-binding proteins.
ANNU.REV.BIOCHEMISTRY 60 349-400 (1991).
 
3. SIMON, M.I., STRATHMANN, M.P. AND GAUTAM, N.
Diversity of G proteins in signal transduction.
SCIENCE 252 802-808 (1993).

Documentation
Guanine nucleotide binding proteins (G proteins) are a family of membrane-
associated proteins that couple extracellularly-activated integral-membrane
receptors to intracellular effectors, such as ion channels and enzymes that
vary the concentration of second messenger molecules [1-3]. G proteins are
composed of 3 subunits (alpha, beta and gamma) which, in the resting state,
associate as a trimer at the inner face of the plasma membrane. The alpha
subunit has a molecule of guanosine diphosphate (GDP) bound to it:
stimulation of the G protein by an activated receptor leads to its exchange
for GTP (guanosine triphosphate). This results in the separation of the
alpha from the beta and gamma subunits, which always remain tightly
associated as a dimer. Both the alpha and beta-gamma subunits are then able
to interact with effectors, either individually or in a cooperative manner.
The intrinsic GTPase activity of the alpha subunit hydrolyses the bound GTP
to GDP. This returns the alpha subunit to its inactive conformation and
allows it to reassociate with the beta-gamma subunit, thus restoring the
system to its resting state.
 
G protein alpha subunits are 350-400 amino acids in length and have
molecular weights in the range 40-45 kDa. Seventeen distinct types of
alpha subunit have been identified in mammals. These fall into 4 main 
groups on the basis of both sequence similarity and function: alpha-S,
alpha-Q, alpha-I and alpha-12 [3]. Many alpha subunits are substrates for
ADP-ribosylation by cholera or pertussis toxins. They are often N-terminally
acylated, usually with myristate and/or palmitoylate, and these fatty acid
modifications are probably important for membrane association and high-
affinity interactions with other proteins. The atomic structure of the
alpha subunit of the G protein involved in mammalian vision, transducin,
has been elucidated in both GTP- and GDB-bound forms, and shows considerable
similarity in both primary and tertiary structure in the nucleotide-binding
regions to other G proteins, such as p21-ras and EF-Tu.
 
The G protein alpha-S class couple receptors, such as the beta-adrenergic
receptor, to the effector enzyme adenylyl cyclase, which produces the
intracellular second messenger cyclic adenosine monophosphate (cAMP).
Alpha-S is found in a variety of tissues in 4 different splice forms (1-4),
the difference caused by the inclusion or deletion of 15 or 16 residues
after the 71st amino acid - the only observed functional change is a higher
rate of GDP dissociation in the longer variants. Alpha-olf is a specialised
form of alpha-S expressed in olfactory neuroepithelial cells, brain and
pancreas. In addition to its interaction with adenylyl cyclase, alpha-S
also activates ion channels, such as atrial voltage gated sodium channels
and dihydropyridine-sensitive calcium channels in skeletal muscle.
 
GPROTEINAS is a 6-element fingerprint that provides a signature for the
G protein alpha subunit group S. The fingerprint was derived from an initial
alignment of 5 sequences: the motifs were drawn from conserved regions
spanning virtually the full alignment length, focusing on those sections 
that characterise group S alpha subunits but distinguish them from other
G protein alpha subtypes. Two iterations on SPTR37_10f were required to 
reach convergence, at which point a true set comprising 17 sequences was
identified. Five partial matches were also found: O18678 and O44744 are
C.elegans alpha-S proteins that lack significant matches with motifs 2 and
3; the remaining matches are human alpha-S proteins that lack the N-terminal
portions of their sequences.
Summary Information
  17 codes involving  6 elements
0 codes involving 5 elements
2 codes involving 4 elements
1 codes involving 3 elements
2 codes involving 2 elements
Composite Feature Index
6171717171717
5000000
4200222
3000111
2000022
123456
True Positives
GBAF_HUMAN    GBAF_RAT      GBAS_BOVIN    GBAS_CRILO    
GBAS_HOMAM GBAS_HUMAN GBAS_LYMST GBAS_MOUSE
GBAS_PIG GBAS_SCHMA GBAS_XENLA GBS1_DROME
GBS2_DROME Q63803 Q9Z1N8 Q9Z1R7
Q9Z1R8
True Positive Partials
Codes involving 4 elements
O18678 O44744
Codes involving 3 elements
O60726
Codes involving 2 elements
O75632 O75633
Sequence Titles
GBAF_HUMAN  GUANINE NUCLEOTIDE-BINDING PROTEIN G(OLF), ALPHA SUBUNIT (ADENYLATE CYCLASE-STIM 
GBAF_RAT GUANINE NUCLEOTIDE-BINDING PROTEIN G(OLF), ALPHA SUBUNIT (ADENYLATE CYCLASE-STIM
GBAS_BOVIN GUANINE NUCLEOTIDE-BINDING PROTEIN G(S), ALPHA SUBUNIT (ADENYLATE CYCLASE-STIMUL
GBAS_CRILO GUANINE NUCLEOTIDE-BINDING PROTEIN G(S), ALPHA SUBUNIT (ADENYLATE CYCLASE-STIMUL
GBAS_HOMAM GUANINE NUCLEOTIDE-BINDING PROTEIN G(S), ALPHA SUBUNIT (ADENYLATE CYCLASE-STIMUL
GBAS_HUMAN GUANINE NUCLEOTIDE-BINDING PROTEIN G(S), ALPHA SUBUNIT (ADENYLATE CYCLASE-STIMUL
GBAS_LYMST GUANINE NUCLEOTIDE-BINDING PROTEIN G(S), ALPHA SUBUNIT (ADENYLATE CYCLASE-STIMUL
GBAS_MOUSE GUANINE NUCLEOTIDE-BINDING PROTEIN G(S), ALPHA SUBUNIT (ADENYLATE CYCLASE-STIMUL
GBAS_PIG GUANINE NUCLEOTIDE-BINDING PROTEIN G(S), ALPHA SUBUNIT (ADENYLATE CYCLASE-STIMUL
GBAS_SCHMA GUANINE NUCLEOTIDE-BINDING PROTEIN G(S), ALPHA SUBUNIT (ADENYLATE CYCLASE-STIMUL
GBAS_XENLA GUANINE NUCLEOTIDE-BINDING PROTEIN G(S), ALPHA SUBUNIT (ADENYLATE CYCLASE-STIMUL
GBS1_DROME GUANINE NUCLEOTIDE-BINDING PROTEIN G(S)-L, ALPHA SUBUNIT (ADENYLATE CYCLASE-STIM
GBS2_DROME GUANINE NUCLEOTIDE-BINDING PROTEIN G(S)-S, ALPHA SUBUNIT (ADENYLATE CYCLASE-STIM
Q63803 XLAS - RATTUS NORVEGICUS (RAT).
Q9Z1N8 G-PROTEIN XLAS - MUS MUSCULUS (MOUSE).
Q9Z1R7 GUANINE NUCLEOTIDE-BINDING PROTEIN - MUS MUSCULUS (MOUSE).
Q9Z1R8 GUANINE NUCLEOTIDE-BINDING PROTEIN - RATTUS NORVEGICUS (RAT).

O18678 G PROTEIN ALPHA SUBUNIT - CAENORHABDITIS ELEGANS.
O44744 R06A10.2 PROTEIN - CAENORHABDITIS ELEGANS.

O60726 MUTANT GUANINE NUCLEOTIDE-BINDING PROTEIN G(S), ALPHA SUBUNIT - HOMO SAPIENS (HU

O75632 GUANINE NUCLEOTIDE-BINDING PROTEIN GS ALPHA SUBUNIT ISOFORM L2 - HOMO SAPIENS (H
O75633 GUANINE NUCLEOTIDE-BINDING PROTEIN GS ALPHA SUBUNIT ISOFORM L3 - HOMO SAPIENS (H
Scan History
SPTR37_10f 2  25   NSINGLE    
Initial Motifs
Motif 1  width=15
Element Seqn Id St Int Rpt
GEKATKVQDIKNNLK GBAS_BOVIN 86 86 -
GEKATKVQDIKNNLK GBAS_HUMAN 86 86 -
EEKKQKILDIRKNVK GBAF_HUMAN 73 73 -
SEKKQKIDDIKKNIR GBS1_DROME 74 74 -
SEKKQKIDDIKKNIR GBS2_DROME 74 74 -

Motif 2 width=16
Element Seqn Id St Int Rpt
EAIETIVAAMSNLVPP GBAS_BOVIN 101 0 -
EAIETIVAAMSNLVPP GBAS_HUMAN 101 0 -
DAIVTIVSAMSTIIPP GBAF_HUMAN 88 0 -
DAILTITGAMSTLNPP GBS1_DROME 89 0 -
DAILTITGAMSTLNPP GBS2_DROME 89 0 -

Motif 3 width=15
Element Seqn Id St Int Rpt
VELANPENQFRVDYI GBAS_BOVIN 117 0 -
VELANPENQFRVDYI GBAS_HUMAN 117 0 -
VPLANPENQFRSDYI GBAF_HUMAN 104 0 -
VALEKKENEPRVEYI GBS1_DROME 105 0 -
VALEKKENEPRVEYI GBS2_DROME 105 0 -

Motif 4 width=16
Element Seqn Id St Int Rpt
LNLFKSIWNNRWLRTI GBAS_BOVIN 270 138 -
LNLFKSIWNNRWLRTI GBAS_HUMAN 270 138 -
LDLFESIWNNRWLRTI GBAF_HUMAN 257 138 -
LDLFKSIWNNRWLRTI GBS1_DROME 258 138 -
LDLFKSIWNNRWLRTI GBS2_DROME 258 138 -

Motif 5 width=15
Element Seqn Id St Int Rpt
VTRAKYFIRDEFLRI GBAS_BOVIN 334 48 -
VTRAKYFIRDEFLRI GBAS_HUMAN 334 48 -
VTRAKFFIRDLFLRI GBAF_HUMAN 321 48 -
VIRAKYFIRDEFLRI GBS1_DROME 325 51 -
VIRAKYFIRDEFLRI GBS2_DROME 322 48 -

Motif 6 width=14
Element Seqn Id St Int Rpt
STASGDGRHYCYPH GBAS_BOVIN 349 0 -
STASGDGRHYCYPH GBAS_HUMAN 349 0 -
STATGDGKHYCYPH GBAF_HUMAN 336 0 -
STASGDGKHYCYPH GBS1_DROME 340 0 -
STASGDGKHYCYPH GBS2_DROME 337 0 -
Final Motifs
Motif 1  width=15
Element Seqn Id St Int Rpt
GEKATKVQDIKNNLK GBAS_BOVIN 86 86 -
GEKATKVQDIKNNLK Q9Z1R8 54 54 -
GEKATKVQDIKNNLK Q9Z1R7 54 54 -
GEKATKVQDIKNNLK Q63803 538 538 -
GEKATKVQDIKNNLK GBAS_MOUSE 86 86 -
GEKATKVQDIKNNLK GBAS_HUMAN 86 86 -
GEKATKVQDIKNNLK GBAS_CRILO 86 86 -
SEKATKVQDIKNNLK Q9Z1N8 448 448 -
DEKATKVQDIKNNLK GBAS_PIG 71 71 -
EEKKTKVQDIKNNIK GBAS_XENLA 71 71 -
EEKKQKILDIRKNVK GBAF_HUMAN 73 73 -
EEKKQKILDIRKNVK GBAF_RAT 73 73 -
SEKKQKIDDIKKNIR GBS1_DROME 74 74 -
SEKKQKIDDIKKNIR GBS2_DROME 74 74 -
EERKQKIEDIKRNVR GBAS_LYMST 68 68 -
EEKREKIHAIRCNIR GBAS_HOMAM 71 71 -
REKKEKIDAIRKNLR GBAS_SCHMA 70 70 -

Motif 2 width=16
Element Seqn Id St Int Rpt
EAIETIVAAMSNLVPP GBAS_BOVIN 101 0 -
EAIETIVAAMSNLVPP Q9Z1R8 69 0 -
EAIETIVAAMSNLVPP Q9Z1R7 69 0 -
EAIETIVAAMSNLVPP Q63803 553 0 -
EAIETIVAAMSNLVPP GBAS_MOUSE 101 0 -
EAIETIVAAMSNLVPP GBAS_HUMAN 101 0 -
EAIETIVAAMSNLVPP GBAS_CRILO 101 0 -
EAIETIVAAMSNLVPP Q9Z1N8 463 0 -
EAIETIVAAMSNLVPP GBAS_PIG 86 0 -
EAIETIVTAMGNLSPP GBAS_XENLA 86 0 -
DAIVTIVSAMSTIIPP GBAF_HUMAN 88 0 -
DAIVTIVSAMSTIIPP GBAF_RAT 88 0 -
DAILTITGAMSTLNPP GBS1_DROME 89 0 -
DAILTITGAMSTLNPP GBS2_DROME 89 0 -
DAILTITGAMSTLNPP GBAS_LYMST 83 0 -
DAILTITGNMSTLTPP GBAS_HOMAM 86 0 -
DAICSIAGAMGSLKPP GBAS_SCHMA 85 0 -

Motif 3 width=15
Element Seqn Id St Int Rpt
VELANPENQFRVDYI GBAS_BOVIN 117 0 -
VELANPENQFRVDYI Q9Z1R8 85 0 -
VELANPENQFRVDYI Q9Z1R7 85 0 -
VELANPENQFRVDYI Q63803 569 0 -
VELANPENQFRVDYI GBAS_MOUSE 117 0 -
VELANPENQFRVDYI GBAS_HUMAN 117 0 -
VELANPENQFRVDYI GBAS_CRILO 117 0 -
VELANPENQFRVDYI Q9Z1N8 479 0 -
VELANPENQFRVDYI GBAS_PIG 102 0 -
VELVNPENQFRIDYI GBAS_XENLA 102 0 -
VPLANPENQFRSDYI GBAF_HUMAN 104 0 -
VPLANPENQFRSDYI GBAF_RAT 104 0 -
VALEKKENEPRVEYI GBS1_DROME 105 0 -
VALEKKENEPRVEYI GBS2_DROME 105 0 -
VQLEHPQNKAKVDYI GBAS_LYMST 99 0 -
IALENPAHQFRVDYI GBAS_HOMAM 102 0 -
VKLELSENRKLRDYI GBAS_SCHMA 101 0 -

Motif 4 width=16
Element Seqn Id St Int Rpt
LNLFKSIWNNRWLRTI GBAS_BOVIN 270 138 -
LNLFKSIWNNRWLRTI Q9Z1R8 238 138 -
LNLFKSIWNNRWLRTI Q9Z1R7 238 138 -
LNLFKSIWNNRWLRTI Q63803 722 138 -
LNLFKSIWNNRWLRTI GBAS_MOUSE 270 138 -
LNLFKSIWNNRWLRTI GBAS_HUMAN 270 138 -
LNLFKSIWNNRWLRTI GBAS_CRILO 270 138 -
LNLFKSIWNNRWLRTI Q9Z1N8 632 138 -
LNLFKSIWNNRWLRTI GBAS_PIG 255 138 -
LNLFKSIWNNRWLRTI GBAS_XENLA 255 138 -
LDLFESIWNNRWLRTI GBAF_HUMAN 257 138 -
LDLFESIWNNRWLRTI GBAF_RAT 257 138 -
LDLFKSIWNNRWLRTI GBS1_DROME 258 138 -
LDLFKSIWNNRWLRTI GBS2_DROME 258 138 -
LDLFKSIWNNRWLRTI GBAS_LYMST 252 138 -
LDLFKSIWNNRWLRTI GBAS_HOMAM 255 138 -
LELLASIWNNRWLRNI GBAS_SCHMA 254 138 -

Motif 5 width=15
Element Seqn Id St Int Rpt
VTRAKYFIRDEFLRI GBAS_BOVIN 334 48 -
VTRAKYFIRDEFLRI Q9Z1R8 302 48 -
VTRAKYFIRDEFLRI Q9Z1R7 302 48 -
VTRAKYFIRDEFLRI Q63803 786 48 -
VTRAKYFIRDEFLRI GBAS_MOUSE 334 48 -
VTRAKYFIRDEFLRI GBAS_HUMAN 334 48 -
VTRAKYFIRDEFLRI GBAS_CRILO 334 48 -
VTRAKYFIRDEFLRI Q9Z1N8 696 48 -
VTRAKYFIRDEFLRI GBAS_PIG 337 66 -
VTRAKYFIRDEFLRI GBAS_XENLA 319 48 -
VTRAKFFIRDLFLRI GBAF_HUMAN 321 48 -
VTRAKFFIRDLFLRI GBAF_RAT 321 48 -
VIRAKYFIRDEFLRI GBS1_DROME 325 51 -
VIRAKYFIRDEFLRI GBS2_DROME 322 48 -
VVRAKYFIRDEFLRI GBAS_LYMST 316 48 -
VVRAKYFIRDEFLRI GBAS_HOMAM 319 48 -
VVRARFFFRDEFLKV GBAS_SCHMA 319 49 -

Motif 6 width=14
Element Seqn Id St Int Rpt
STASGDGRHYCYPH GBAS_BOVIN 349 0 -
STASGDGRHYCYPH Q9Z1R8 317 0 -
STASGDGRHYCYPH Q9Z1R7 317 0 -
STASGDGRHYCYPH Q63803 801 0 -
STASGDGRHYCYPH GBAS_MOUSE 349 0 -
STASGDGRHYCYPH GBAS_HUMAN 349 0 -
STASGDGRHYCYPH GBAS_CRILO 349 0 -
STASGDGRHYCYPH Q9Z1N8 711 0 -
STASGDGRHYCYPH GBAS_PIG 352 0 -
STASGDGRHYCYPH GBAS_XENLA 334 0 -
STATGDGKHYCYPH GBAF_HUMAN 336 0 -
STATGDGKHYCYPH GBAF_RAT 336 0 -
STASGDGKHYCYPH GBS1_DROME 340 0 -
STASGDGKHYCYPH GBS2_DROME 337 0 -
STASGDGRHYCYPH GBAS_LYMST 331 0 -
STASGDGKHYCYPH GBAS_HOMAM 334 0 -
TSNNNGGRHYCYPH GBAS_SCHMA 334 0 -