Descriptions

Protein bicaudal D homolog 1 (BICD1) is a protein that regulates coat complex coatomer protein I (COPI)-independent Golgi-endoplasmic reticulum transport by recruiting the dynein-dynactin motor complex. Autoinhibition of BICD1 involves the C-terminal coiled-coil region (CC3) binding to the N-terminal coiled-coil region (CC1), preventing interaction with cytoplasmic dynein. This interaction inhibits the association with cytoplasmic dynein and its cargo-binding function. A structural rearrangement of the core packing in a homodimeric coiled-coil stimulates the release of CC1 from the CC3 region following cargo-binding. Additionally, the three residues (Glu772, Ile784, and Lys787), which are required for Rab6 binding, play a critical role in maintaining the autoinhibitory state through direct interaction with the N-terminal CC1 region.

Autoinhibitory domains (AIDs)

Target domain

1-300 (CC1 region)

Relief mechanism

Partner binding

Assay

Structural analysis, Mutagenesis experiment, Split protein assay

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

2 structures for Q8BR07

Entry ID Method Resolution Chain Position Source
4YTD X-ray 150 A A/B 711-808 PDB
AF-Q8BR07-F1 Predicted AlphaFoldDB

17 variants for Q8BR07

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3388862159 68 Q>* No EVA
rs3388875216 182 L>M No EVA
rs3388872014 190 K>N No EVA
rs3388865753 193 Q>K No EVA
rs3388878047 340 K>* No EVA
rs3388872497 353 Q>K No EVA
rs3388871973 355 E>Q No EVA
rs3388865343 421 R>S No EVA
rs3545186570 472 T>S No EVA
rs3388873361 486 E>D No EVA
rs3388870893 489 K>R No EVA
rs3388875188 498 H>Y No EVA
rs3388872522 523 C>R No EVA
rs3388872007 523 C>Y No EVA
rs3388875190 533 V>F No EVA
rs3388870939 600 I>F No EVA
rs3388875203 705 A>V No EVA

No associated diseases with Q8BR07

No regional properties for Q8BR07

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q8BR07

Functions

Description
EC Number
Subcellular Localization
  • Golgi apparatus
PANTHER Family PTHR31233 BICAUDAL D FAMILY MEMBER
PANTHER Subfamily PTHR31233:SF3 PROTEIN BICAUDAL D HOMOLOG 1
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

8 GO annotations of cellular component

Name Definition
centrosome A structure comprised of a core structure (in most organisms, a pair of centrioles) and peripheral material from which a microtubule-based structure, such as a spindle apparatus, is organized. Centrosomes occur close to the nucleus during interphase in many eukaryotic cells, though in animal cells it changes continually during the cell-division cycle.
cytoplasmic vesicle A vesicle found in the cytoplasm of a cell.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
Golgi apparatus A membrane-bound cytoplasmic organelle of the endomembrane system that further processes the core oligosaccharides (e.g. N-glycans) added to proteins in the endoplasmic reticulum and packages them into membrane-bound vesicles. The Golgi apparatus operates at the intersection of the secretory, lysosomal, and endocytic pathways.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
perinuclear region of cytoplasm Cytoplasm situated near, or occurring around, the nucleus.
secretory vesicle A cytoplasmic, membrane bound vesicle that is capable of fusing to the plasma membrane to release its contents into the extracellular space.
trans-Golgi network The network of interconnected tubular and cisternal structures located within the Golgi apparatus on the side distal to the endoplasmic reticulum, from which secretory vesicles emerge. The trans-Golgi network is important in the later stages of protein secretion where it is thought to play a key role in the sorting and targeting of secreted proteins to the correct destination.

7 GO annotations of molecular function

Name Definition
cytoskeletal anchor activity The binding activity of a protein that brings together a cytoskeletal protein (either a microtubule or actin filament, spindle pole body, or protein directly bound to them) and one or more other molecules, permitting them to function in a coordinated way.
dynactin binding Binding to a dynactin complex; a large protein complex that activates dynein-based motor activity.
dynein complex binding Binding to a dynein complex, a protein complex that contains two or three dynein heavy chains and several light chains, and has microtubule motor activity.
dynein intermediate chain binding Binding to an intermediate chain of the dynein complex.
protein kinase binding Binding to a protein kinase, any enzyme that catalyzes the transfer of a phosphate group, usually from ATP, to a protein substrate.
proteinase activated receptor binding Binding to a proteinase activated receptor.
small GTPase binding Binding to a small monomeric GTPase.

11 GO annotations of biological process

Name Definition
microtubule anchoring at microtubule organizing center Any process in which a microtubule is maintained in a specific location in a cell by attachment to a microtubule organizing center.
minus-end-directed organelle transport along microtubule The directed movement of an organelle towards the minus end of a microtubule, mediated by motor proteins. This process begins with the attachment of an organelle to a microtubule, and ends when the organelle reaches its final destination.
negative regulation of phospholipase C activity Any process that stops, prevents or reduces the frequency, rate or extent of phospholipase C activity.
negative regulation of phospholipase C-activating G protein-coupled receptor signaling pathway Any process that stops, prevents or reduces the frequency, rate or extent of phospholipase C-activating G protein-coupled receptor signaling pathway.
positive regulation of protein localization to centrosome Any process that activates or increases the frequency, rate or extent of protein localization to centrosome.
positive regulation of receptor-mediated endocytosis Any process that activates or increases the frequency, rate or extent of receptor mediated endocytosis, the uptake of external materials by cells, utilizing receptors to ensure specificity of transport.
protein localization to organelle A process in which a protein is transported to, or maintained in, a location within an organelle.
regulation of microtubule cytoskeleton organization Any process that modulates the frequency, rate or extent of the formation, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising microtubules and their associated proteins.
regulation of proteinase activated receptor activity Any process that modulates the frequency, rate or extent of proteinase activated receptor activity.
stress granule assembly The aggregation, arrangement and bonding together of proteins and RNA molecules to form a stress granule.
viral process A multi-organism process in which a virus is a participant. The other participant is the host. Includes infection of a host cell, replication of the viral genome, and assembly of progeny virus particles. In some cases the viral genetic material may integrate into the host genome and only subsequently, under particular circumstances, 'complete' its life cycle.

4 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P16568 BicD Protein bicaudal D Drosophila melanogaster (Fruit fly) EV
Q8TD16 BICD2 Protein bicaudal D homolog 2 Homo sapiens (Human) SS
Q96G01 BICD1 Protein bicaudal D homolog 1 Homo sapiens (Human) SS
Q921C5 Bicd2 Protein bicaudal D homolog 2 Mus musculus (Mouse) SS
10 20 30 40 50 60
MAAEEALKTV DQYKTEIERL TKELTETTHE KIQAAEYGLV VLEEKLTLKQ QYDELEAEYD
70 80 90 100 110 120
GLKQELEQLR EAFGQSFSIH RKVAEDGETR EETLLQESAS KEAYYLNKIL EMQNELKQSR
130 140 150 160 170 180
AVVTNVQAEN ERLSAVVQEL KENNEMVELQ RIRMKDEIRE YKFREARLLQ DYTELEEENI
190 200 210 220 230 240
TLQKLVSTLK QNQVEYEGLK HEIKRFEEET VLLNSQLEDA IRLKEIAEHQ LEEALETLKN
250 260 270 280 290 300
EREQKNNLRK ELSQYINLSD SHISISVDGL KFAEDGSEPN NDDKMNGHIH GPLGKLNGDY
310 320 330 340 350 360
RTPTTRKGES LHPVSDLFSE LNISEIQKLK QQLIQVEREK AILLANLQES QTQLEHTKGA
370 380 390 400 410 420
LTEQHERVHR LTEHVNAMRG LQNSKEIKAE LDCEKGRNSA EEAHDYEVDI NGLEILECKY
430 440 450 460 470 480
RVAVTEVIDL KAEIKALKEK YNKSVENYTE EKTKYESKIQ MYDEQVTNLE KTSKESGEKM
490 500 510 520 530 540
AHMEKELQKM TGIANENHNT LNTAQDELVT FSEELAQLYH HVCLCNNETP NRVMLDYYRQ
550 560 570 580 590 600
SRVTRSGSLK GPDDPRGLLS PRLSRRGVSS PVESRTSSEP VSKENTETSK EPSPTKTPTI
610 620 630 640 650 660
SPVITAPPSS PVLDTSDIRK EPMNIYNLNA IIRDQIKHLQ KAVDRSLQLS RQRAAARELA
670 680 690 700 710 720
PMIDKDKEAL MEEILKLKSL LSTKREQIAT LRAVLKANKQ TAEVALANLK NKYENEKAMV
730 740 750 760 770 780
TETMTKLRNE LKALKEDAAT FSSLRAMFAT RCDEYVTQLD EMQRQLAAAE DEKKTLNTLL
790 800 810 820 830
RMAIQQKLAL TQRLEDLEFD HEQSRRSKGK LGKSKIGSPK IVSSLLPPYR HSAHN