Summary: Microtubule-associated protein Bicaudal-D
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Microtubule-associated protein Bicaudal-D Provide feedback
BicD proteins consist of three coiled-coiled domains and are involved in dynein-mediated minus end-directed transport from the Golgi apparatus to the endoplasmic reticulum (ER). For full functioning they bind with GSK-3beta PF05350 to maintain the anchoring of microtubules to the centromere. It appears that amino-acid residues 437-617 of BicD and the kinase activity of GSK-3 are necessary for the formation of a complex between BicD and GSK-3beta in intact cells [1].
Literature references
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Fumoto K, Hoogenraad CC, Kikuchi A; , EMBO J. 2006;25:5670-5682.: GSK-3beta-regulated interaction of BICD with dynein is involved in microtubule anchorage at centrosome. PUBMED:17139249 EPMC:17139249
Internal database links
SCOOP: | ADIP ATG16 Crescentin ERM EzrA Macoilin Spc7 |
This tab holds annotation information from the InterPro database.
InterPro entry IPR018477
Bicaudal-D (BicD) is a family of motor adaptor proteins consist of three coiled-coiled domains. BicD plays an essential for the correct localization of maternal mRNAs in Drosophila's oocyte [PUBMED:17827179] and functions as a regulator of the Golgi to ER retrograde transport in mammalian cells [PUBMED:19018277]. BicD was suggested to be a linker bridging cargo and dynein and have roles in the regulation of cargo motility [PUBMED:19754453]. It also functions as a novel regulator of neurotrophin (NT) signaling [PUBMED:28215293].
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
Molecular function | dynein complex binding (GO:0070840) |
cytoskeletal adaptor activity (GO:0008093) |
Domain organisation
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Alignments
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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
Seed (7) |
Full (1210) |
Representative proteomes | UniProt (1955) |
NCBI (3513) |
Meta (0) |
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RP15 (179) |
RP35 (415) |
RP55 (847) |
RP75 (1273) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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Seed (7) |
Full (1210) |
Representative proteomes | UniProt (1955) |
NCBI (3513) |
Meta (0) |
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RP15 (179) |
RP35 (415) |
RP55 (847) |
RP75 (1273) |
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Raw Stockholm | |||||||||
Gzipped |
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
Note: You can also download the data file for the tree.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
Seed source: | KOGs (KOG0999) |
Previous IDs: | none |
Type: | Coiled-coil |
Sequence Ontology: | SO:0001080 |
Author: |
KOGs, Finn RD |
Number in seed: | 7 |
Number in full: | 1210 |
Average length of the domain: | 538.20 aa |
Average identity of full alignment: | 47 % |
Average coverage of the sequence by the domain: | 81.78 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 47079205 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 719 | ||||||||||||
Family (HMM) version: | 10 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the BicD domain has been found. There are 8 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.
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