choline transporter-like protein 2 isoform 3 [Mus musculus]
Protein Classification
choline transporter-like family protein( domain architecture ID 10517537)
choline transporter-like (CTL) family protein is involved in Na(+)-independent, high affinity choline transport to supply choline for the synthesis of cell membrane phospholipids to certain cell types
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| Choline_transpo | pfam04515 | Plasma-membrane choline transporter; This family represents a high-affinity plasma-membrane ... |
318-674 | 1.86e-123 | ||||||
Plasma-membrane choline transporter; This family represents a high-affinity plasma-membrane choline transporter in C.elegans which is thought to be rate-limiting for ACh synthesis in cholinergic nerve terminals. : Pssm-ID: 461337 Cd Length: 325 Bit Score: 370.76 E-value: 1.86e-123
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| ABC_6TM_exporters super family | cl38913 | Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
235-275 | 9.24e-03 | ||||||
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis. The actual alignment was detected with superfamily member cd18587: Pssm-ID: 365789 Cd Length: 293 Bit Score: 38.57 E-value: 9.24e-03
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| Name | Accession | Description | Interval | E-value | ||||||
| Choline_transpo | pfam04515 | Plasma-membrane choline transporter; This family represents a high-affinity plasma-membrane ... |
318-674 | 1.86e-123 | ||||||
Plasma-membrane choline transporter; This family represents a high-affinity plasma-membrane choline transporter in C.elegans which is thought to be rate-limiting for ACh synthesis in cholinergic nerve terminals. Pssm-ID: 461337 Cd Length: 325 Bit Score: 370.76 E-value: 1.86e-123
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| ABC_6TM_LapB_like | cd18587 | Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
235-275 | 9.24e-03 | ||||||
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), such as LapB. LapB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion, LapA is a RTX (repeats in toxin) protein found in Pseudomonas fluorescens and is required for biofilm formation in this organism. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. In this T1SS system, LapB is a cytoplasmic membrane-localized ATPase, LapC is a membrane fusion protein, and LapE is an outer membrane protein. Pssm-ID: 350031 Cd Length: 293 Bit Score: 38.57 E-value: 9.24e-03
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| Name | Accession | Description | Interval | E-value | ||||||
| Choline_transpo | pfam04515 | Plasma-membrane choline transporter; This family represents a high-affinity plasma-membrane ... |
318-674 | 1.86e-123 | ||||||
Plasma-membrane choline transporter; This family represents a high-affinity plasma-membrane choline transporter in C.elegans which is thought to be rate-limiting for ACh synthesis in cholinergic nerve terminals. Pssm-ID: 461337 Cd Length: 325 Bit Score: 370.76 E-value: 1.86e-123
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| ABC_6TM_LapB_like | cd18587 | Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
235-275 | 9.24e-03 | ||||||
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), such as LapB. LapB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion, LapA is a RTX (repeats in toxin) protein found in Pseudomonas fluorescens and is required for biofilm formation in this organism. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. In this T1SS system, LapB is a cytoplasmic membrane-localized ATPase, LapC is a membrane fusion protein, and LapE is an outer membrane protein. Pssm-ID: 350031 Cd Length: 293 Bit Score: 38.57 E-value: 9.24e-03
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