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Conserved domains on  [gi|392050757|ref|NP_001254706|]
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intraflagellar transport protein 20 homolog isoform 4 [Homo sapiens]

Protein Classification

intraflagellar transport protein 20 homolog( domain architecture ID 10633075)

intraflagellar transport protein 20 homolog that as a subunit of the intraflagellar transport complex B (IFT-B) is involved in mediating anterograde trafficking from the base to the distal tip of cilia, powered by the kinesin-2 motor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IFT20 pfam14931
Intraflagellar transport complex B, subunit 20; IFT20 is subunit 20 of the intraflagellar ...
 11-106 3.20e-39

Intraflagellar transport complex B, subunit 20; IFT20 is subunit 20 of the intraflagellar transport complex B. The intraflagellar transport complex assembles and maintains eukaryotic cilia and flagella. IFT20 is localized to the Golgi complex and is anchored there by the Golgi polypeptide, GMAP210, whereas all other subunits except IFT172 localize to cilia and the peri-basal body or centrosomal region at the base of cilia. IFT20 accompanies Golgi-derived vesicles to the point of exocytosis near the basal bodies where the other IFT polypeptides are present, and where the intact IFT particle is assembled in association with the inner surface of the cell membrane. Passage of the IFT complex then follows, through the flagellar pore recognition site at the transition region, into the ciliary compartment. There also appears to be a role of intraflagellar transport (IFT) polypeptides in the formation of the immune synapse in non ciliated cells. The flagellum, in addition to being a sensory and motile organelle, is also a secretory organelle. A number of IFT components are expressed in haematopoietic cells, which have no cilia, indicating an unexpected role of IFT proteins in immune synapse-assembly and intracellular membrane trafficking in T lymphocytes; this suggests that the immune synapse could represent the functional homolog of the primary cilium in these cells.


:

Pssm-ID: 464383 [Multi-domain]  Cd Length: 109  Bit Score: 126.54  E-value: 3.20e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392050757   11 LHFDELNKLRVLDPEVTQQTIELKEECKDFVDKIGQFQKIVGGLIELVDQLAKEAENEKMKAIGARNLLKSIAKQREAQQ 90
Cdd:pfam14931   1 LYFDELNKIRVLDPEVADQTEELKEECKEFVNKISEFQKIVGGFIEIVDTLAKKVEKEKLKAIGARNLLKSEAKQREAEQ 80

                          90
                  ....*....|....*.
gi 392050757   91 QQLQALIAEKKMQLER 106
Cdd:pfam14931  81 QQLQALILEKKVELER 96
 
Name Accession Description Interval E-value
IFT20 pfam14931
Intraflagellar transport complex B, subunit 20; IFT20 is subunit 20 of the intraflagellar ...
 11-106 3.20e-39

Intraflagellar transport complex B, subunit 20; IFT20 is subunit 20 of the intraflagellar transport complex B. The intraflagellar transport complex assembles and maintains eukaryotic cilia and flagella. IFT20 is localized to the Golgi complex and is anchored there by the Golgi polypeptide, GMAP210, whereas all other subunits except IFT172 localize to cilia and the peri-basal body or centrosomal region at the base of cilia. IFT20 accompanies Golgi-derived vesicles to the point of exocytosis near the basal bodies where the other IFT polypeptides are present, and where the intact IFT particle is assembled in association with the inner surface of the cell membrane. Passage of the IFT complex then follows, through the flagellar pore recognition site at the transition region, into the ciliary compartment. There also appears to be a role of intraflagellar transport (IFT) polypeptides in the formation of the immune synapse in non ciliated cells. The flagellum, in addition to being a sensory and motile organelle, is also a secretory organelle. A number of IFT components are expressed in haematopoietic cells, which have no cilia, indicating an unexpected role of IFT proteins in immune synapse-assembly and intracellular membrane trafficking in T lymphocytes; this suggests that the immune synapse could represent the functional homolog of the primary cilium in these cells.


Pssm-ID: 464383 [Multi-domain]  Cd Length: 109  Bit Score: 126.54  E-value: 3.20e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392050757   11 LHFDELNKLRVLDPEVTQQTIELKEECKDFVDKIGQFQKIVGGLIELVDQLAKEAENEKMKAIGARNLLKSIAKQREAQQ 90
Cdd:pfam14931   1 LYFDELNKIRVLDPEVADQTEELKEECKEFVNKISEFQKIVGGFIEIVDTLAKKVEKEKLKAIGARNLLKSEAKQREAEQ 80

                          90
                  ....*....|....*.
gi 392050757   91 QQLQALIAEKKMQLER 106
Cdd:pfam14931  81 QQLQALILEKKVELER 96
 
Name Accession Description Interval E-value
IFT20 pfam14931
Intraflagellar transport complex B, subunit 20; IFT20 is subunit 20 of the intraflagellar ...
 11-106 3.20e-39

Intraflagellar transport complex B, subunit 20; IFT20 is subunit 20 of the intraflagellar transport complex B. The intraflagellar transport complex assembles and maintains eukaryotic cilia and flagella. IFT20 is localized to the Golgi complex and is anchored there by the Golgi polypeptide, GMAP210, whereas all other subunits except IFT172 localize to cilia and the peri-basal body or centrosomal region at the base of cilia. IFT20 accompanies Golgi-derived vesicles to the point of exocytosis near the basal bodies where the other IFT polypeptides are present, and where the intact IFT particle is assembled in association with the inner surface of the cell membrane. Passage of the IFT complex then follows, through the flagellar pore recognition site at the transition region, into the ciliary compartment. There also appears to be a role of intraflagellar transport (IFT) polypeptides in the formation of the immune synapse in non ciliated cells. The flagellum, in addition to being a sensory and motile organelle, is also a secretory organelle. A number of IFT components are expressed in haematopoietic cells, which have no cilia, indicating an unexpected role of IFT proteins in immune synapse-assembly and intracellular membrane trafficking in T lymphocytes; this suggests that the immune synapse could represent the functional homolog of the primary cilium in these cells.


Pssm-ID: 464383 [Multi-domain]  Cd Length: 109  Bit Score: 126.54  E-value: 3.20e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392050757   11 LHFDELNKLRVLDPEVTQQTIELKEECKDFVDKIGQFQKIVGGLIELVDQLAKEAENEKMKAIGARNLLKSIAKQREAQQ 90
Cdd:pfam14931   1 LYFDELNKIRVLDPEVADQTEELKEECKEFVNKISEFQKIVGGFIEIVDTLAKKVEKEKLKAIGARNLLKSEAKQREAEQ 80

                          90
                  ....*....|....*.
gi 392050757   91 QQLQALIAEKKMQLER 106
Cdd:pfam14931  81 QQLQALILEKKVELER 96
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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