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PR00440

Identifier
GPROTEINA12  [View Relations]  [View Alignment]  
Accession
PR00440
No. of Motifs
7
Creation Date
12-JUN-1995  (UPDATE 17-DEC-1999)
Title
G-protein alpha subunit group 12 signature
Database References
PRINTS; PR00318 GPROTEINA
INTERPRO; IPR000469
PDB; 1TND
SCOP; 1TND
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 alpha-12 group of G proteins includes G12 and G13 proteins. An
alpha-12-like protein has also been found in Drosophila. The functions of
these proteins are unknown.
 
GPROTEINA12 is a 7-element fingerprint that provides a signature for the
G protein alpha subunit group 12. 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 the group 12 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 6 
sequences was identified. A single partial match was also found: Q19572 
is a C.elegans G protein with considerable similarity to the alpha-12 
group but lacking significant matches with motifs 1, 2 and 5.
Summary Information
   6 codes involving  7 elements
0 codes involving 6 elements
0 codes involving 5 elements
1 codes involving 4 elements
0 codes involving 3 elements
0 codes involving 2 elements
Composite Feature Index
76666666
60000000
50000000
40011011
30000000
20000000
1234567
True Positives
GB12_HUMAN    GB12_MOUSE    GB13_HUMAN    GB13_MOUSE    
GBAL_DROME Q63210
True Positive Partials
Codes involving 4 elements
Q19572
Sequence Titles
GB12_HUMAN  GUANINE NUCLEOTIDE-BINDING PROTEIN, ALPHA-12 SUBUNIT (G ALPHA 12) - HOMO SAPIENS 
GB12_MOUSE GUANINE NUCLEOTIDE-BINDING PROTEIN, ALPHA-12 SUBUNIT (G ALPHA 12) - MUS MUSCULUS
GB13_HUMAN GUANINE NUCLEOTIDE-BINDING PROTEIN, ALPHA-13 SUBUNIT (G ALPHA 13) - HOMO SAPIENS
GB13_MOUSE GUANINE NUCLEOTIDE-BINDING PROTEIN, ALPHA-13 SUBUNIT (G ALPHA 13) - MUS MUSCULUS
GBAL_DROME GUANINE NUCLEOTIDE-BINDING PROTEIN, ALPHA SUBUNIT HOMOLOG (PROTEIN CONCERTINA) -
Q63210 GUANINE NUCLEOTIDE-BINDING PROTEIN, ALPHA-12 SUBUNIT (G ALPHA 12) - RATTUS NORVEGICUS (RAT).

Q19572 SIMILAR TO GUANINE NUCLEOTIDE-BINDING PROTEINS - CAENORHABDITIS ELEGANS.
Scan History
SPTR37_10f 2  45   NSINGLE    
Initial Motifs
Motif 1  width=10
Element Seqn Id St Int Rpt
REFDQKALLE GB12_MOUSE 81 81 -
REFDQKALLE GB12_HUMAN 83 83 -
QDFDQRAREE GB13_HUMAN 74 74 -
QDFDQRAREE GB13_MOUSE 74 74 -
VNFDYELLLE GBAL_DROME 158 158 -

Motif 2 width=13
Element Seqn Id St Int Rpt
FRDTIFDNILKGS GB12_MOUSE 91 0 -
FRDTIFDNILKGS GB12_HUMAN 93 0 -
FRPTIYSNVIKGM GB13_HUMAN 84 0 -
FRPTIYSNVIKGM GB13_MOUSE 84 0 -
YQSVIYQNVIRGM GBAL_DROME 168 0 -

Motif 3 width=10
Element Seqn Id St Int Rpt
RVLVDARDKL GB12_MOUSE 104 0 -
RVLVDARDKL GB12_HUMAN 106 0 -
RVLVDAREKL GB13_HUMAN 97 0 -
RVLVDAREKL GB13_MOUSE 97 0 -
QVLLDAREKL GBAL_DROME 181 0 -

Motif 4 width=13
Element Seqn Id St Int Rpt
IKKHFPDFKGDPH GB12_MOUSE 308 194 -
IKKHFPDFRGDPH GB12_HUMAN 310 194 -
IKDYFLEFEGDPH GB13_HUMAN 305 198 -
IKDYFLEFEGDPH GB13_MOUSE 305 198 -
IRWYYPHFNGNPH GBAL_DROME 385 194 -

Motif 5 width=11
Element Seqn Id St Int Rpt
QCFDRKRRNRS GB12_MOUSE 331 10 -
QCFDRKRRNRS GB12_HUMAN 333 10 -
ECFRNKRRDQQ GB13_HUMAN 328 10 -
ECFRGKRRDQQ GB13_MOUSE 328 10 -
QMFMSVRRSSS GBAL_DROME 408 10 -

Motif 6 width=11
Element Seqn Id St Int Rpt
KPLFHHFTTAI GB12_MOUSE 342 0 -
KPLFHHFTTAI GB12_HUMAN 344 0 -
KPLYHHFTTAI GB13_HUMAN 340 1 -
RPLYHHFTTAI GB13_MOUSE 340 1 -
SRIYHHFTTAI GBAL_DROME 420 1 -

Motif 7 width=11
Element Seqn Id St Int Rpt
LQENLKDIMLQ GB12_MOUSE 369 16 -
LQENLKDIMLQ GB12_HUMAN 371 16 -
LHDNLKQLMLQ GB13_HUMAN 367 16 -
LHDNLKQLMLQ GB13_MOUSE 367 16 -
LQRNLNALMLQ GBAL_DROME 447 16 -
Final Motifs
Motif 1  width=10
Element Seqn Id St Int Rpt
REFDQKALLE GB12_MOUSE 81 81 -
REFDQKALLE GB12_HUMAN 83 83 -
REFDQKALLE Q63210 81 81 -
QDFDQRAREE GB13_HUMAN 74 74 -
QDFDQRAREE GB13_MOUSE 74 74 -
VNFDYELLLE GBAL_DROME 158 158 -

Motif 2 width=13
Element Seqn Id St Int Rpt
FRDTIFDNILKGS GB12_MOUSE 91 0 -
FRDTIFDNILKGS GB12_HUMAN 93 0 -
FRDTIFDNILKGS Q63210 91 0 -
FRPTIYSNVIKGM GB13_HUMAN 84 0 -
FRPTIYSNVIKGM GB13_MOUSE 84 0 -
YQSVIYQNVIRGM GBAL_DROME 168 0 -

Motif 3 width=10
Element Seqn Id St Int Rpt
RVLVDARDKL GB12_MOUSE 104 0 -
RVLVDARDKL GB12_HUMAN 106 0 -
RVLVDARDKL Q63210 104 0 -
RVLVDAREKL GB13_HUMAN 97 0 -
RVLVDAREKL GB13_MOUSE 97 0 -
QVLLDAREKL GBAL_DROME 181 0 -

Motif 4 width=13
Element Seqn Id St Int Rpt
IKKHFPDFKGDPH GB12_MOUSE 308 194 -
IKKHFPDFRGDPH GB12_HUMAN 310 194 -
IKKHFPDFKGDPH Q63210 308 194 -
IKDYFLEFEGDPH GB13_HUMAN 305 198 -
IKDYFLEFEGDPH GB13_MOUSE 305 198 -
IRWYYPHFNGNPH GBAL_DROME 385 194 -

Motif 5 width=11
Element Seqn Id St Int Rpt
QCFDRKRRNRS GB12_MOUSE 331 10 -
QCFDRKRRNRS GB12_HUMAN 333 10 -
QCFDRKRRNRG Q63210 331 10 -
ECFRNKRRDQQ GB13_HUMAN 328 10 -
ECFRGKRRDQQ GB13_MOUSE 328 10 -
QMFMSVRRSSS GBAL_DROME 408 10 -

Motif 6 width=11
Element Seqn Id St Int Rpt
KPLFHHFTTAI GB12_MOUSE 342 0 -
KPLFHHFTTAI GB12_HUMAN 344 0 -
KPLFHHFTTAI Q63210 342 0 -
KPLYHHFTTAI GB13_HUMAN 340 1 -
RPLYHHFTTAI GB13_MOUSE 340 1 -
SRIYHHFTTAI GBAL_DROME 420 1 -

Motif 7 width=11
Element Seqn Id St Int Rpt
LQENLKDIMLQ GB12_MOUSE 369 16 -
LQENLKDIMLQ GB12_HUMAN 371 16 -
LQENLKDIMLQ Q63210 369 16 -
LHDNLKQLMLQ GB13_HUMAN 367 16 -
LHDNLKQLMLQ GB13_MOUSE 367 16 -
LQRNLNALMLQ GBAL_DROME 447 16 -