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PR01189

Identifier
ANIONEXHNGR3  [View Relations]  [View Alignment]  
Accession
PR01189
No. of Motifs
4
Creation Date
15-JUN-1999
Title
Anion exchanger isoform 3 signature
Database References
PRINTS; PR00165 ANIONEXCHNGR
PRODOM; PD018440
INTERPRO; IPR002979
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. LINN, S.C., KUDRYCKI, K.E. AND SHULL, G.E.
The predicted translation product of a cardiac AE3 mRNA contains an N
terminus distinct from that of the brain AE3 Cl-/HCO3- exchanger. Cloning
of a cardiac AE3 cDNA, organization of the AE3 gene, and identification of
an alternative transcription initiation site.
J.BIOL.CHEM. 15 7927-7935 (1992).
 
5. YANNOUKAKOS, D., STUART-TILLEY, A., FERNANDEZ, H.A., FEY, P., DUYK, G.
AND ALPER, S.L.
Molecular cloning, expression, and chromosomal localization of two isoforms
of the AE3 anion exchanger from human heart.
CIRC.RES. 75 603-614 (1994).

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].
 
AE3 is an anion exchanger that is primarily expressed in the brain and
heart. Several tissue-specific variants have been identified, which arise
due to both alternative promoter and exon usage. Two AE3-encoding cDNAs have
been isolated from human heart. These clones share long portions of common 
sequence but have different 5' ends, therefore encoding distinct N-terminal
amino acid sequences. The longer AE3 polypeptide (1232 amino acids) displays
~96% amino acid sequence identity to the rat and mouse AE3 `brain isoforms'.
The shorter polypeptide (1034 amino acids) corresponds to the rat AE3 
`cardiac isoform'. Studies of Cl- transport suggest that both isoforms are
capable of anion exchange [4,5].
 
ANIONEXHNGR3 is a 4-element fingerprint that provides a signature for the
anion exchanger isoform 3. The fingerprint was derived from an initial
alignment of 2 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 3 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 4 sequences was identified.
Summary Information
4 codes involving  4 elements
0 codes involving 3 elements
0 codes involving 2 elements
Composite Feature Index
44444
30000
20000
1234
True Positives
B3A3_HUMAN    B3A3_MOUSE    B3A3_RAT      O18917        
Sequence Titles
B3A3_HUMAN  ANION EXCHANGE PROTEIN 3 (CARDIAC/BRAIN BAND 3-LIKE PROTEIN) (CAE3/BAE3) - HOMO  
B3A3_MOUSE ANION EXCHANGE PROTEIN 3 (NEURONAL BAND 3-LIKE PROTEIN) - MUS MUSCULUS (MOUSE).
B3A3_RAT ANION EXCHANGE PROTEIN 3 (NEURONAL BAND 3-LIKE PROTEIN) - RATTUS NORVEGICUS (RAT
O18917 ANION EXCHANGER 3 BRAIN ISOFORM - ORYCTOLAGUS CUNICULUS (RABBIT).
Scan History
SPTR37_9f  2  50   NSINGLE    
Initial Motifs
Motif 1  width=16
Element Seqn Id St Int Rpt
GDLISKTPAWDPEKPS B3A3_RAT 48 48 -
GDLISKTPAWDPEKPS B3A3_MOUSE 48 48 -

Motif 2 width=21
Element Seqn Id St Int Rpt
GESEAEPVEPPPPGPPQKAKF B3A3_RAT 146 82 -
GESEAEPVEPLPPGPPQKAKF B3A3_MOUSE 146 82 -

Motif 3 width=20
Element Seqn Id St Int Rpt
PTPSHGPDGAVPTMADDLGE B3A3_RAT 454 287 -
PTPSHGPDGAVPTMADDQGE B3A3_MOUSE 454 287 -

Motif 4 width=18
Element Seqn Id St Int Rpt
PAPLWPHDPDAKEKPLHM B3A3_RAT 474 0 -
PAPLWPHDPDAKEKPLHM B3A3_MOUSE 474 0 -
Final Motifs
Motif 1  width=16
Element Seqn Id St Int Rpt
GDLISKTPAWDPEKPS B3A3_RAT 48 48 -
GDLISKPPAWDPEKPS B3A3_HUMAN 48 48 -
GDLISKTPAWDPEKPS B3A3_MOUSE 48 48 -
GDLISKPPAWDPEKPS O18917 48 48 -

Motif 2 width=21
Element Seqn Id St Int Rpt
GESEAEPVEPPPPGPPQKAKF B3A3_RAT 146 82 -
GESEAEPVEPPPSGTPQKAKF B3A3_HUMAN 146 82 -
GESEAEPVEPLPPGPPQKAKF B3A3_MOUSE 146 82 -
GESETEAVEPPPSGSPQKAKF O18917 147 83 -

Motif 3 width=20
Element Seqn Id St Int Rpt
PTPSHGPDGAVPTMADDLGE B3A3_RAT 454 287 -
PTPSHGPDGAVPTMADDLGE B3A3_HUMAN 455 288 -
PTPSHGPDGAVPTMADDQGE B3A3_MOUSE 454 287 -
ATPSHGPDGAVPTMADDLGE O18917 456 288 -

Motif 4 width=18
Element Seqn Id St Int Rpt
PAPLWPHDPDAKEKPLHM B3A3_RAT 474 0 -
PAPLWPHDPDAKEKPLHM B3A3_HUMAN 475 0 -
PAPLWPHDPDAKEKPLHM B3A3_MOUSE 474 0 -
PAPLWPHDPDAKERPLHM O18917 476 0 -