ABCA4 p.Thr506Ala

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Publications
PMID: 11320094 [PubMed] Bungert S et al: "Membrane topology of the ATP binding cassette transporter ABCR and its relationship to ABC1 and related ABCA transporters: identification of N-linked glycosylation sites."
No. Sentence Comment
58 ABCR(⌬8) had mutations in eight N-linked glycosylation sites within two ECDs at the following positions: Asn-98 (S100A), Asn-415 (T417A), Asn-444 (T446A), Asn-504 (T506A), Asn-1469 (T1471A), Asn-1529 (S1531A), Asn-1588 (S1590A), and Asn-1662 (T1664A) as shown in Fig. 2.
X
ABCA4 p.Thr506Ala 11320094:58:171
status: NEW
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79 (S100A), Asn-415 (T417A), Asn-444 (T446), and Asn-504 (T506A) were constructed as described above and are listed in Table I. The DNA sequences of all constructs were determined to verify the presence of the desired mutation and the absence of random mutations.
X
ABCA4 p.Thr506Ala 11320094:79:55
status: NEW
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153 TABLE I N-linked glycosylation mutants Protein N-Linked glycosylation sites Mutations ABCR(WT) Asn-98, Asn-415, Asn-444, Asn-504 None Asn-1469, Asn-1529, Asn-1588, Asn-1662 ABCR(⌬8) None S100A, T417A, T446A, T506A T1471A, S1531A, S1590A, T1664A ABCR(⌬4N) Asn-1469, Asn-1529, Asn-1588, Asn-1662 S100A, T417A, T446A, T506A ABCR(⌬4C) Asn-98, Asn-415, Asn-444, Asn-504 T1471A, S1531A, S1590A, T1664A ABCR(⌬7-N1469) Asn-1469 S100A, T417A, T446A, T506A T1471A, S1531A, S1590A S100A, T417A, T446A, T506A ABCR(⌬7-N1529) Asn-1529 T1471A, S1531A, T1664A S100A, T417A, T446A, T506A ABCR(⌬7-N1588) Asn-1588 T1471A, S1590A, T1664A ABCR(⌬7-N1662) Asn-1662 S100A, T417A, T446A, T506A S1531A, S1590A, T1664A N-tr-ABCR (WT) Asn-98, Asn-415, Asn-444, Asn-504 None N-tr-ABCR(⌬4) None S100A, T417A, T446A, T506A N-tr-ABCR(⌬3-N98) Asn-98 T417A, T446A, T506A N-tr-ABCR(⌬3-N415) Asn-415 S100A, T446A, T506A N-tr-ABCR(⌬3-N444) Asn-444 S100A, T417A, T506A N-tr-ABCR(⌬3-N504) Asn-504 S100A, T417A, T446A DISCUSSION Membrane Topology and Structural Features of ABCR- Computer-derived hydropathy profiles and comparative protein analysis serve as a useful starting point in developing working models for the topology of novel membrane proteins.
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ABCA4 p.Thr506Ala 11320094:153:214
status: NEW
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ABCA4 p.Thr506Ala 11320094:153:215
status: NEW
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ABCA4 p.Thr506Ala 11320094:153:327
status: NEW
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ABCA4 p.Thr506Ala 11320094:153:329
status: NEW
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ABCA4 p.Thr506Ala 11320094:153:465
status: NEW
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ABCA4 p.Thr506Ala 11320094:153:469
status: NEW
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ABCA4 p.Thr506Ala 11320094:153:515
status: NEW
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ABCA4 p.Thr506Ala 11320094:153:519
status: NEW
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ABCA4 p.Thr506Ala 11320094:153:595
status: NEW
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ABCA4 p.Thr506Ala 11320094:153:600
status: NEW
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ABCA4 p.Thr506Ala 11320094:153:705
status: NEW
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ABCA4 p.Thr506Ala 11320094:153:712
status: NEW
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ABCA4 p.Thr506Ala 11320094:153:834
status: NEW
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ABCA4 p.Thr506Ala 11320094:153:842
status: NEW
X
ABCA4 p.Thr506Ala 11320094:153:885
status: NEW
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57 ABCR(èc;8) had mutations in eight N-linked glycosylation sites within two ECDs at the following positions: Asn-98 (S100A), Asn-415 (T417A), Asn-444 (T446A), Asn-504 (T506A), Asn-1469 (T1471A), Asn-1529 (S1531A), Asn-1588 (S1590A), and Asn-1662 (T1664A) as shown in Fig. 2.
X
ABCA4 p.Thr506Ala 11320094:57:170
status: NEW
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78 (S100A), Asn-415 (T417A), Asn-444 (T446), and Asn-504 (T506A) were constructed as described above and are listed in Table I. The DNA sequences of all constructs were determined to verify the presence of the desired mutation and the absence of random mutations.
X
ABCA4 p.Thr506Ala 11320094:78:55
status: NEW
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