3UIT


Conserved Protein Domain Family
L27_N

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pfam09060: L27_N (This model is not part of the current CDD release)
L27_N
The L27_N domain plays a role in the biogenesis of tight junctions and in the establishment of cell polarity in epithelial cells. Each L27_N domain consists of three alpha-helices, the first two of which form an antiparallel coiled-coil. Two L27 domains come together to form a four-helical bundle with the antiparallel coiled-coils formed by the first two helices. The third helix of each domain forms another coiled-coil packing at one end of the four-helix bundle, creating a large hydrophobic interface: the hydrophobic interactions are the major force that drives heterodimer formation.
Statistics
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PSSM-Id: 518663
Aligned: 12 rows
Threshold Bit Score: 59.7112
Created: 15-Feb-2025
Updated: 28-Apr-2025
Structure
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Program:
Drawing:
Aligned Rows:
PubMed ReferencesClick to see Conserved Features Help

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
3UIT_A        81 EIEDLFSSLKHIQHTLVDSQSQEDISLLLQLVQNKDFQNAFKIHNAIT 128 synthetic construct
1_pfamImport   1 ELAELLQALKWAHHCLADAQSQQDVELIMQLLSKEDFKNAYTIFIAVS 48 
6_pfamImport   1 ELDELLQVLKWVQHSLSDSQSQQDVEVTMQLLAKEEFRNAYTIYSVLS 48 
5_pfamImport   1 ELEELLQTLKWVQHCLTDAQSQQDVELITQLLTKEDFRTAYSIYSAVS 48 
7_pfamImport   1 ELNDLLQSLQRVRYSLGDAESQADVQVVMELLQQREFQQAFSMHSTVA 48 
Q1LVF4       150 ELEDLLMSLKQVQHNLNDSQSQEDVELVLQLVQKPDFQKAFSIHNSVA 197 zebrafish
XP_006632749 122 DLEDLLASLKHIQYSLSDSQSQEDISVVLQLIQKTDFQNAFQIHNAVA 169
XP_005991524 125 DVDELLSSLKQVQHGLVDSQSQEDMSVILQLVQNSEFQNAFKIYNAVA 172
NP_001186634 123 EVEELLTSLKHIQHVLVDPQSQEDLALILQLVQNTDFQNAFKIHNAVT 170
XP_004083475 106 DLEDLEQALKWAQHCLNDAQSQQDVDLIMQLLAKEEFRNAYAIFTTLS 153
XP_003962332 122 eleelllslKQVRGCLADQQSQNDIELVLTLLHKSDFQSALKIHNAVA 169 torafugu
XP_003971802 110 DVEEWQQALKWTLHCLTDVQSQQDVALIMQLLSAEDFRAAYSVYKAVS 157 torafugu
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