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PR01187

Identifier
ANIONEXHNGR1  [View Relations]  [View Alignment]  
Accession
PR01187
No. of Motifs
4
Creation Date
15-JUN-1999
Title
Anion exchanger isoform 1 signature
Database References
PRINTS; PR00165 ANIONEXCHNGR
INTERPRO; IPR002977
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. BRUCE, L.J., UNWIN, R.J., WRONG, O. AND TANNER, M.J.
The association between familial distal renal tubular acidosis and
mutations in the red cell anion exchanger (band 3, AE1) gene.
BIOCHEM.CELL BIOL. 76 723-728 (1998).

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].
 
Naturally-occuring mutations have been characterised in the AE1 gene, which
give rise to forms of several inherited human diseases. Around 20% of
hereditary spherocytosis cases arise from heterozygosity for AE1 mutations,
and result in the absence or decrease of the mutant protein in the red cell
membrane. Similarly, familial distal renal tubular acidosis, a condition
associated with kidney stones, has been shown to be associated with
mutations of AE1 of the renal collecting duct alpha-intercalated cell, and
it has been postulated that such mutations may affect the targeting of the
AE1 protein, which is usually directed to the basolateral membrane of
these cells [4].
 
ANIONEXHNGR1 is a 4-element fingerprint that provides a signature for the
anion exchanger isoform 1. 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 anion exchanger isoform 1 but distinguish it from 
others - motif 1 resides within the putative cytoplasmic N-terminus; motif
2 lies on the exoplasmic loop connecting putative TM domains 7 and 8; motif
3 encodes a small portion of the intracellular loop between TM domains 8
and 9; and motif 4 is located on the putative extracellular loop connecting
TM domains 11 and 12. Two iterations on SPTR37_9f were required to reach
convergence, at which point a true set comprising 7 sequences was identified.
Summary Information
7 codes involving  4 elements
0 codes involving 3 elements
0 codes involving 2 elements
Composite Feature Index
47777
30000
20000
1234
True Positives
B3AT_CHICK    B3AT_HUMAN    B3AT_MOUSE    B3AT_ONCMY    
B3AT_RAT Q90579 Q91452
Sequence Titles
B3AT_CHICK  BAND 3 ANION TRANSPORT PROTEIN - GALLUS GALLUS (CHICKEN). 
B3AT_HUMAN BAND 3 ANION TRANSPORT PROTEIN (ANION EXCHANGE PROTEIN 1) (AE 1) - HOMO SAPIENS
B3AT_MOUSE BAND 3 ANION EXCHANGE PROTEIN (MEB3) - MUS MUSCULUS (MOUSE).
B3AT_ONCMY BAND 3 ANION EXCHANGE PROTEIN - ONCORHYNCHUS MYKISS (RAINBOW TROUT) (SALMO GAIRD
B3AT_RAT BAND 3 ANION EXCHANGE PROTEIN, KIDNEY - RATTUS NORVEGICUS (RAT).
Q90579 ERYTHROID ANION TRANSPORTER - GALLUS GALLUS (CHICKEN).
Q91452 ANION EXCHANGER - ONCORHYNCHUS MYKISS (RAINBOW TROUT) (SALMO GAIRDNERI).
Scan History
SPTR37_9f  2  150  NSINGLE    
Initial Motifs
Motif 1  width=10
Element Seqn Id St Int Rpt
TEIQDEGMLQ B3AT_ONCMY 311 311 -
TDAPSEQALL B3AT_HUMAN 324 324 -
TEAPSEKALL B3AT_RAT 337 337 -
TDAPSEKALL B3AT_MOUSE 337 337 -
QEVPSEQHLH B3AT_CHICK 331 331 -

Motif 2 width=9
Element Seqn Id St Int Rpt
GFKVSNSSA B3AT_HUMAN 637 303 -
GLMVSNPNA B3AT_ONCMY 650 329 -
GLEVTNGTA B3AT_CHICK 648 307 -
GLKVSNSSA B3AT_MOUSE 655 308 -
GLKVSNSSA B3AT_RAT 653 306 -

Motif 3 width=6
Element Seqn Id St Int Rpt
PERKMV B3AT_ONCMY 705 46 -
PERKMV B3AT_HUMAN 692 46 -
PERKMI B3AT_RAT 708 46 -
PERKMI B3AT_MOUSE 710 46 -
PERKLV B3AT_CHICK 703 46 -

Motif 4 width=7
Element Seqn Id St Int Rpt
YHPDVPY B3AT_HUMAN 818 120 -
YYPADAY B3AT_ONCMY 827 116 -
YHPKEPY B3AT_CHICK 829 120 -
YHPDVPF B3AT_MOUSE 836 120 -
YHPDVPF B3AT_RAT 834 120 -
Final Motifs
Motif 1  width=10
Element Seqn Id St Int Rpt
TEIQDKGMLQ Q91452 305 305 -
TDAPSEQALL B3AT_HUMAN 324 324 -
TEAPSEKALL B3AT_RAT 337 337 -
TDAPSEKALL B3AT_MOUSE 337 337 -
QEVPSEQHLH B3AT_CHICK 331 331 -
QEVPSEQHLH Q90579 253 253 -
TEIQDEGMLQ B3AT_ONCMY 311 311 -

Motif 2 width=9
Element Seqn Id St Int Rpt
GFKVSNSSA B3AT_HUMAN 637 303 -
GLMVSNPNA Q91452 644 329 -
GLMVSNPNA B3AT_ONCMY 650 329 -
GLEVTNGTA Q90579 570 307 -
GLEVTNGTA B3AT_CHICK 648 307 -
GLKVSNSSA B3AT_MOUSE 655 308 -
GLKVSNSSA B3AT_RAT 653 306 -

Motif 3 width=6
Element Seqn Id St Int Rpt
PERKMV B3AT_ONCMY 705 46 -
PERKMV B3AT_HUMAN 692 46 -
PERKMI B3AT_RAT 708 46 -
PERKMI B3AT_MOUSE 710 46 -
PERKLV B3AT_CHICK 703 46 -
PERKLV Q90579 625 46 -
PERKMV Q91452 699 46 -

Motif 4 width=7
Element Seqn Id St Int Rpt
YHPDVPY B3AT_HUMAN 818 120 -
YYPRDAY Q91452 821 116 -
YYPADAY B3AT_ONCMY 827 116 -
YHPKEPY Q90579 751 120 -
YHPKEPY B3AT_CHICK 829 120 -
YHPDVPF B3AT_MOUSE 836 120 -
YHPDVPF B3AT_RAT 834 120 -