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PR01188

Identifier
ANIONEXHNGR2  [View Relations]  [View Alignment]  
Accession
PR01188
No. of Motifs
4
Creation Date
15-JUN-1999
Title
Anion exchanger isoform 2 signature
Database References
PRINTS; PR00165 ANIONEXCHNGR
PRODOM; PD014490
INTERPRO; IPR002978
Literature References
1. KOPITO, R.R.
Molecular biology of the anion exchanger gene family.
INT.REV.CYTOL. 123 177-199 (1990).
 
2. ALPER, S.L.
The band 3-related anion exchanger (AE) gene family.
ANNU.REV.PHYSIOL. 53 549-564 (1991).
 
3. TANNER, M.J.
The structure and function of band 3 (AE1): recent developments (review).
MOL.MEMBR.BIOL. 14 155-165 (1997).
 
4. LINDSEY, A.E., SCHNEIDER, K., SIMMONS, D.M., BARON, R., LEE, B.S. AND
KOPITO, R.R.
Functional expression and subcellular localization of an anion exchanger
cloned from choroid plexus.
PROC.NATL.ACAD.SCI.U.S.A. 87 5278-5282 (1990).
 
5. WANG, Z., SCHULTHEIS, P.J. AND SHULL, G.E.
Three N-terminal variants of the AE2 Cl-/HCO3- exchanger are encoded by
mRNAs transcribed from alternative promoters.
J.BIOL.CHEM. 271 7835-7843 (1996).

Documentation
Anion exchange proteins are thought to participate in pH and cell volume
regulation. They are glycosylated, plasma-membrane transport proteins that
exchange hydrogen carbonate (HCO3-) for chloride (Cl-) in a reversible,
electroneutral manner [1,2]. To date three anion exchanger isoforms have
been identified (AE1-3), AE1 being the previously-characterised erythrocyte
band 3 protein. They share a predicted topology of 12-14 transmembrane (TM)
domains, but have differing distribution patterns and cellular localisation.
The best characterised isoform, AE1, is known to be the most abundant
membrane protein in mature erythrocytes. It has a molecular mass of ~95 kDa
and consists of two major domains. The N-terminal 390 residues form a water-
soluble, highly elongated domain that serves as an attachment site for the
binding of the membrane skeleton and other cytoplasmic proteins. The 
remainder of the protein is a 55kDa hydrophobic domain that is responsible
for catalysing anion exchange. The function of the analogous domains of AE2
and AE3 remains to be determined [3].
 
AE2 (~1240 amino acids) is a non-erythroid anion exchanger. It was cloned
from choroid plexus but has been detected in many organs including the
gastrointestinal tract and kidney. It is expressed in both epithelial and
non-epithelial cells, and may be present in the Golgi apparatus in addition
to the cell membrane [4]. Three AE2 N-terminal variants have been described,
arising due to the presence of alternative promoter sites within the gene. 
They are referred to as AE2a-c and have differing distribution patterns:
AE2a is expressed in all tissues; AE2b exhibits a more restricted
distribution, with highest levels in the stomach; and AE2c is expressed
only in the stomach [5].
 
ANIONEXHNGR2 is a 4-element fingerprint that provides a signature for the
anion exchanger isoform 2. The fingerprint was derived from an initial
alignment of 4 sequences: the motifs were drawn from conserved regions 
within the N-terminal half of the alignment, focusing on those sections that
characterise the anion exchanger isoform 2 but distinguish it from others -
motifs 1-4 reside within the large putative cytoplasmic N-terminus. Two
iterations on SPTR37_9f were required to reach convergence, at which point
a true set comprising 5 sequences was identified.
Summary Information
5 codes involving  4 elements
0 codes involving 3 elements
0 codes involving 2 elements
Composite Feature Index
45555
30000
20000
1234
True Positives
B3A2_HUMAN    B3A2_MOUSE    B3A2_RABIT    B3A2_RAT      
Q99654
Sequence Titles
B3A2_HUMAN  ANION EXCHANGE PROTEIN 2 (NON-ERYTHROID BAND 3-LIKE PROTEIN) (BND3L) - HOMO SAPI 
B3A2_MOUSE ANION EXCHANGE PROTEIN 2 (NON-ERYTHROID BAND 3-LIKE PROTEIN) (B3RP) - MUS MUSCUL
B3A2_RABIT ANION EXCHANGE PROTEIN 2 (NON-ERYTHROID BAND 3-LIKE PROTEIN) (B3RP) - ORYCTOLAGU
B3A2_RAT ANION EXCHANGE PROTEIN 2 (NON-ERYTHROID BAND 3-LIKE PROTEIN) (B3RP) - RATTUS NOR
Q99654 AE2 ANION EXCHANGER - HOMO SAPIENS (HUMAN).
Scan History
SPTR37_9f  2  150  NSINGLE    
Initial Motifs
Motif 1  width=17
Element Seqn Id St Int Rpt
TPEPESLGPGTPGFPEQ B3A2_HUMAN 17 17 -
TPEPESLSPGTPGFPEQ B3A2_MOUSE 17 17 -
TPEPESLSPGTPGFPEQ B3A2_RAT 17 17 -
TPEPESLGPGTPGFPEQ B3A2_RABIT 17 17 -

Motif 2 width=14
Element Seqn Id St Int Rpt
EEILQEAGSRGGEE B3A2_HUMAN 48 14 -
EEILQEAGSRGGEE B3A2_MOUSE 47 13 -
EEILQEAGSRGGEE B3A2_RAT 48 14 -
EEILQEAGSRGGEE B3A2_RABIT 48 14 -

Motif 3 width=17
Element Seqn Id St Int Rpt
REGREPGPTPRARPRAP B3A2_HUMAN 301 239 -
REGREPGPTPRARPRAP B3A2_MOUSE 297 236 -
REGREPGPTPRARPRAP B3A2_RAT 298 236 -
REGREPGPTPRSRPRAP B3A2_RABIT 297 235 -

Motif 4 width=20
Element Seqn Id St Int Rpt
ESDPHVTEPLMGGVPETRLE B3A2_HUMAN 460 142 -
ESDPHVTEPLIGGVPETRLE B3A2_MOUSE 456 142 -
ESDPHVTEPLIGGVPETRLE B3A2_RAT 457 142 -
ESDPHVTEPLIGGIPETRLD B3A2_RABIT 456 142 -
Final Motifs
Motif 1  width=17
Element Seqn Id St Int Rpt
TPEPESLGPGTPGFPEQ B3A2_HUMAN 17 17 -
TPEPESLGPGTPGFPEQ Q99654 17 17 -
TPEPESLSPGTPGFPEQ B3A2_MOUSE 17 17 -
TPEPESLSPGTPGFPEQ B3A2_RAT 17 17 -
TPEPESLGPGTPGFPEQ B3A2_RABIT 17 17 -

Motif 2 width=14
Element Seqn Id St Int Rpt
EEILQEAGSRGGEE B3A2_HUMAN 48 14 -
EEILQEAGSRGGEE Q99654 48 14 -
EEILQEAGSRGGEE B3A2_MOUSE 47 13 -
EEILQEAGSRGGEE B3A2_RAT 48 14 -
EEILQEAGSRGGEE B3A2_RABIT 48 14 -

Motif 3 width=17
Element Seqn Id St Int Rpt
REGREPGPTPRARPRAP B3A2_HUMAN 301 239 -
REGREPGPTPRARPRAP Q99654 301 239 -
REGREPGPTPRARPRAP B3A2_MOUSE 297 236 -
REGREPGPTPRARPRAP B3A2_RAT 298 236 -
REGREPGPTPRSRPRAP B3A2_RABIT 297 235 -

Motif 4 width=20
Element Seqn Id St Int Rpt
ESDPHVTEPLMGGVPETRLE B3A2_HUMAN 460 142 -
ESDPHVTEPLMGGVPETRLE Q99654 460 142 -
ESDPHVTEPLIGGVPETRLE B3A2_MOUSE 456 142 -
ESDPHVTEPLIGGVPETRLE B3A2_RAT 457 142 -
ESDPHVTEPLIGGIPETRLD B3A2_RABIT 456 142 -