ABCA4 p.Thr417Ala
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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.
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ABCA4 p.Thr417Ala 11320094:58:137
status: NEW79 (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.
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ABCA4 p.Thr417Ala 11320094:79:18
status: NEW153 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.Thr417Ala 11320094:153:200
status: NEWX
ABCA4 p.Thr417Ala 11320094:153:201
status: NEWX
ABCA4 p.Thr417Ala 11320094:153:313
status: NEWX
ABCA4 p.Thr417Ala 11320094:153:315
status: NEWX
ABCA4 p.Thr417Ala 11320094:153:451
status: NEWX
ABCA4 p.Thr417Ala 11320094:153:455
status: NEWX
ABCA4 p.Thr417Ala 11320094:153:501
status: NEWX
ABCA4 p.Thr417Ala 11320094:153:505
status: NEWX
ABCA4 p.Thr417Ala 11320094:153:581
status: NEWX
ABCA4 p.Thr417Ala 11320094:153:586
status: NEWX
ABCA4 p.Thr417Ala 11320094:153:691
status: NEWX
ABCA4 p.Thr417Ala 11320094:153:698
status: NEWX
ABCA4 p.Thr417Ala 11320094:153:820
status: NEWX
ABCA4 p.Thr417Ala 11320094:153:828
status: NEWX
ABCA4 p.Thr417Ala 11320094:153:871
status: NEW57 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.Thr417Ala 11320094:57:136
status: NEW78 (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.Thr417Ala 11320094:78:18
status: NEW