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PR01198

Identifier
BETTRANSPORT  [View Relations]  [View Alignment]  
Accession
PR01198
No. of Motifs
3
Creation Date
21-JUN-1999
Title
Betaine transporter signature
Database References
PRINTS; PR00176 NANEUSMPORT
PRODOM; PD013666; PD017174; PD013673
INTERPRO; IPR002983
Literature References
1. ATTELL, D. AND MOBBS, P.
Neurotransmitter transporters.
CURR.OPIN.NEUROBIOL. 4 353-359 (1994).
 
2. MALANDRO, M.S. AND KILBERG, M.S.
Molecular biology of mammalian amino acid transporters.
ANNU.REV.BIOCHEMISTRY 65 305-336 (1996).
 
3. AMARA, S.G. AND ARRIZA, J.L.
Neurotransmitter transporters: three distinct gene families.
CURR.OPIN.NEUROBIOL. 3 337-344 (1993).
 
4. UHL, G.R. AND JOHNSON, P.S.
Neurotransmitter transporters: Three important gene families for neuronal
function.
J.EXP.BIOL. 196 229-236 (1994).
 
5. LILL, H. AND NELSON, N.
Homologies and family relationships among Na+/Cl- neurotransmitter
transporters.
METHODS ENZYMOL. 306 425-436 (1998).
 
6. BECK, F.X., SCHMOLKE, M. AND GUDER, W.G.
Osmolytes.
CURR.OPIN.NEPHROL.HYPERTENS. 1 43-52 (1992).
 
7. MATSKEVITCH, I., WAGNER, C.A., STEGEN, C., BROER, S., NOLL, B., RISLER, T.,
KWON, H.M., HANDLER, J.S., WALDEGGER, S., BUSCH, A.E. AND LANG, F.
Functional characterization of the Betaine/gamma-aminobutyric acid
transporter BGT-1 expressed in Xenopus oocytes.
J.BIOL.CHEM. 11 16709-16716 (1999). 

Documentation
Neurotransmitter transport systems are integral to the release, re-uptake
and recycling of neurotransmitters at synapses. High affinity tranport
proteins found in the plasma membrane of presynaptic nerve terminals and
glial cells are responsible for the removal from the extracellular space
of released-transmitters, thereby terminating their actions [1]. Plasma
membrane neurotransmitter transporters fall into two structurally and
mechanistically distinct families. The majority of the transporters
constitute an extensive family of homologous proteins that derive energy
from the co-transport of Na+ and Cl-, in order to transport neurotransmitter
molecules into the cell against their concentration gradient. The family 
has a common structure of 12 presumed transmembrane helices and includes 
carriers for gamma-aminobutyric acid (GABA), noradrenaline/adrenaline, 
dopamine, serotonin, proline, glycine, choline, betaine and taurine. They
are structurally distinct from the second more-restricted family of plasma
membrane transporters, which are responsible for excitatory amino acid
tranport. The latter couple glutamate and aspartate uptake to the co-
transport of Na+ and the counter-transport of K+, with no apparent
dependence on Cl- [2]. In addition, both of these transporter families
are distinct from the vesicular neurotransmitter transporters [3,4].
 
Sequence analysis of the Na+/Cl- neurotransmitter superfamily reveals that
it can be divided into four subfamilies, these being transporters for
monoamines, the amino acids proline and glycine, GABA, and a group of
orphan transporters [5].
 
Cells regulate their volume and adapt to alterations in the tonicity of
their local environment by adjusting their solute content accordingly.
Resultant water movements rapidly establish osmotic balance. Solutes
utilised in this manner are referred to as osmolytes and include: glycero-
phosphorylcholine, betaine, myo-inositol, sorbitol and taurine [6].
Cell membrane transporters for betaine and taurine have been cloned, and by
sequence similarity they have been shown to belong to the Na+ and Cl-
-coupled neurotransmitter transporter superfamily. Functional studies of
the cloned betaine transporter (BGT-1) have revealed that it can also
transport GABA, and that its mode of transport is electrogenic, with uptake
of betaine depolarising the cell [7]. In humans, the gene maps to chromosome
12p13, and is found to be expressed in: the kidney, brain, liver, heart,
skeletal muscle and placenta.
 
BETTRANSPORT is a 3-element fingerprint that provides a signature for the
betaine transporter. The fingerprint was derived from an initial alignment
of 5 sequences: the motifs were drawn from the N- and C-terminal regions of
the alignment, focusing on those sections that characterise the betaine
transporter but distinguish it from others - motif 1 lies at the start of
the putative cytoplasmic N-terminus; and motifs 2-3 reside within the
putative cytoplasmic C-terminal tail. A single iteration on SPTR37_9f was
required to reach convergence, no further sequences being identified beyond
the starting set.
Summary Information
5 codes involving  3 elements
0 codes involving 2 elements
Composite Feature Index
3555
2000
123
True Positives
NTBE_CANFA    NTBE_HUMAN    NTBE_MOUSE    NTBE_RABIT    
NTBE_RAT
Sequence Titles
NTBE_CANFA  SODIUM- AND CHLORIDE-DEPENDENT BETAINE TRANSPORTER (NA+/CL- BETAINE/GABA TRANSPORTER) - CANIS FAMILIARIS (DOG). 
NTBE_HUMAN SODIUM- AND CHLORIDE-DEPENDENT BETAINE TRANSPORTER (NA+/CL- BETAINE/GABA TRANSPORTER) (BGT-1) - HOMO SAPIENS (HUMAN).
NTBE_MOUSE SODIUM- AND CHLORIDE-DEPENDENT BETAINE TRANSPORTER (NA+/CL- BETAINE/GABA TRANSPORTER) (SODIUM- AND CHLORIDE-DEPENDENT GABA TRANSPORTER 4) (GAT2) - MUS MUSCULUS (MOUSE).
NTBE_RABIT SODIUM- AND CHLORIDE-DEPENDENT BETAINE TRANSPORTER (NA+/CL- BETAINE/GABA TRANSPORTER) - ORYCTOLAGUS CUNICULUS (RABBIT).
NTBE_RAT SODIUM- AND CHLORIDE-DEPENDENT BETAINE TRANSPORTER (NA+/CL- BETAINE/GABA TRANSPORTER) - RATTUS NORVEGICUS (RAT).
Scan History
SPTR37_9f  1  300  NSINGLE    
Initial Motifs
Motif 1  width=14
Element Seqn Id St Int Rpt
KVAVHEDGYPVVSW NTBE_MOUSE 4 4 -
KVAVPEDGPPVVSW NTBE_CANFA 4 4 -
KVTVHEDGCPVVSW NTBE_RAT 4 4 -
KVAVQEYGPPAVSW NTBE_HUMAN 4 4 -
KLAVHEDAPPLVSW NTBE_RABIT 4 4 -

Motif 2 width=18
Element Seqn Id St Int Rpt
FKKRLRRLITPDPSLPQP NTBE_MOUSE 565 547 -
FKKRLRQLTTPDPSLPQP NTBE_CANFA 565 547 -
FKKRLQRLITPDPSLPQP NTBE_RAT 565 547 -
FRKRLRQLITPDSSLPQP NTBE_HUMAN 565 547 -
FTKRLRQLITPDPSLPQP NTBE_RABIT 565 547 -

Motif 3 width=13
Element Seqn Id St Int Rpt
SPAKQELIAWEKE NTBE_MOUSE 599 16 -
SPTKEGLIVGEKE NTBE_CANFA 599 16 -
SPVKQELIAWEKE NTBE_RAT 599 16 -
SPTREGLIAGEKE NTBE_HUMAN 599 16 -
SPAKEGLVTVEKE NTBE_RABIT 599 16 -
Final Motifs
Motif 1  width=14
Element Seqn Id St Int Rpt
KVAVHEDGYPVVSW NTBE_MOUSE 4 4 -
KVAVPEDGPPVVSW NTBE_CANFA 4 4 -
KVTVHEDGCPVVSW NTBE_RAT 4 4 -
KVAVQEYGPPAVSW NTBE_HUMAN 4 4 -
KLAVHEDAPPLVSW NTBE_RABIT 4 4 -

Motif 2 width=18
Element Seqn Id St Int Rpt
FKKRLRRLITPDPSLPQP NTBE_MOUSE 565 547 -
FKKRLRQLTTPDPSLPQP NTBE_CANFA 565 547 -
FKKRLQRLITPDPSLPQP NTBE_RAT 565 547 -
FRKRLRQLITPDSSLPQP NTBE_HUMAN 565 547 -
FTKRLRQLITPDPSLPQP NTBE_RABIT 565 547 -

Motif 3 width=13
Element Seqn Id St Int Rpt
SPAKQELIAWEKE NTBE_MOUSE 599 16 -
SPTKEGLIVGEKE NTBE_CANFA 599 16 -
SPVKQELIAWEKE NTBE_RAT 599 16 -
SPTREGLIAGEKE NTBE_HUMAN 599 16 -
SPAKEGLVTVEKE NTBE_RABIT 599 16 -