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A transmembrane domain (TMD, TM domain) is a membrane-spanning protein domain.TMDs may consist of one or several alpha-helices or a transmembrane beta barrel.Because the interior of the lipid bilayer is hydrophobic, the amino acid residues in TMDs are often hydrophobic, although proteins such as membrane pumps and ion channels can contain polar residues.
ABC transporter transmembrane domain is the main transmembrane structural unit of ATP-binding cassette transporter proteins, consisting of six alpha helixes that traverse the plasma membrane. Many members of the ABC transporter family ( Pfam PF00005 ) have two such regions.
This causes the cross-prediction between them, which is a weakness of many transmembrane topology predictors. By predicting signal peptides and transmembrane helices simultaneously (Phobius [14]), the errors caused by cross-prediction are reduced and the performance is substantially increased. Another feature used to increase the accuracy of ...
244049 Ensembl ENSG00000140563 ENSMUSG00000032776 UniProt Q6DN12 Q5RJH2 RefSeq (mRNA) NM_001159643 NM_001159644 NM_018349 NM_001024703 RefSeq (protein) NP_001153115 NP_001153116 NP_060819 NP_001019874 Location (UCSC) Chr 15: 94.23 – 94.48 Mb Chr 7: 71.73 – 71.96 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Multiple C2 domains, transmembrane 2 is a protein that in humans is ...
Cross-sectional view of the structures that can be formed by phospholipids in an aqueous solution. A biological membrane, biomembrane or cell membrane is a selectively permeable membrane that separates the interior of a cell from the external environment or creates intracellular compartments by serving as a boundary between one part of the cell and another.
The protein can broadly be split into the Notch extracellular domain (NECD) and Notch intracellular domain (NICD) joined together by a single-pass transmembrane domain (TM). The NECD contains 36 EGF repeats in Drosophila , [ 13 ] 28-36 in humans, and 13 and 10 in C. elegans Lin-12 and GLP-1 respectively. [ 27 ]
OmpA-like transmembrane domain is an evolutionarily conserved domain of bacterial outer membrane proteins. This domain consists of an eight-stranded beta barrel. [1] OmpA is the predominant cell surface antigen in enterobacteria found in about 100,000 copies per cell. [2] The expression of OmpA is tightly regulated by a variety of mechanisms.