Descriptions

Coiled-coil protein DIX1 (Ccd1, Dixin) is an important positive regulator activating the canonical Wnt signaling pathway. The DIX domain of Ccd1 functions as a switching hub in the Wnt pathway via dynamic polymerization. Homopolymerization of the DIX domain is regulated by insertion of loop β1-β2 of the DIX domain into the head-to-tail interface, preventing the formation of head-to-tail helical filaments and consequently inhibiting its transcriptional activity. The autoinhibition of Ccd1 is relieved by co-expression of Dvl, binding to DISC1, and Cdk25- or MARK1/4-mediated phosphorylation.

Autoinhibitory domains (AIDs)

Target domain

407-416 (β3-β4 loop)

Relief mechanism

Partner binding, PTM

Assay

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

2 structures for Q804T6

Entry ID Method Resolution Chain Position Source
5Y3C X-ray 196 A A 356-438 PDB
AF-Q804T6-F1 Predicted AlphaFoldDB

No variants for Q804T6

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q804T6

No associated diseases with Q804T6

3 regional properties for Q804T6

Type Name Position InterPro Accession
domain Homeobox domain 242 - 309 IPR001356
domain PBX, PBC domain 48 - 243 IPR005542
conserved_site Homeobox, conserved site 280 - 303 IPR017970

Functions

Description
EC Number
Subcellular Localization
  • Cell junction, focal adhesion
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
focal adhesion A cell-substrate junction that anchors the cell to the extracellular matrix and that forms a point of termination of actin filaments. In insects focal adhesion has also been referred to as hemi-adherens junction (HAJ).

2 GO annotations of molecular function

Name Definition
frizzled binding Binding to a frizzled (fz) receptor.
identical protein binding Binding to an identical protein or proteins.

3 GO annotations of biological process

Name Definition
camera-type eye development The process whose specific outcome is the progression of the camera-type eye over time, from its formation to the mature structure. The camera-type eye is an organ of sight that receives light through an aperture and focuses it through a lens, projecting it on a photoreceptor field.
canonical Wnt signaling pathway The series of molecular signals initiated by binding of a Wnt protein to a frizzled family receptor on the surface of the target cell, followed by propagation of the signal via beta-catenin, and ending with a change in transcription of target genes. In this pathway, the activated receptor signals via downstream effectors that result in the inhibition of beta-catenin phosphorylation, thereby preventing degradation of beta-catenin. Stabilized beta-catenin can then accumulate and travel to the nucleus to trigger changes in transcription of target genes.
forebrain development The process whose specific outcome is the progression of the forebrain over time, from its formation to the mature structure. The forebrain is the anterior of the three primary divisions of the developing chordate brain or the corresponding part of the adult brain (in vertebrates, includes especially the cerebral hemispheres, the thalamus, and the hypothalamus and especially in higher vertebrates is the main control center for sensory and associative information processing, visceral functions, and voluntary motor functions).

3 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q155Q3 DIXDC1 Dixin Homo sapiens (Human) SS
Q80Y83 Dixdc1 Dixin Mus musculus (Mouse) EV
Q2VUH7 Dixdc1 Dixin Rattus norvegicus (Rat) SS
10 20 30 40 50 60
MGAKQMKCLS SSSPSHTPKE EYIIAKSEDS GELVGNHTEQ PQSLEDVVKS SATDPYPGPE
70 80 90 100 110 120
HVVKEESSTW EEQLCAQQEQ LEKEMQETRK MVSRLQALLL HGSLPEDEQT STLSFGDTAS
130 140 150 160 170 180
SEQQLILTRS RLDQSMEESL DLKRELLRYK QEARNLQAVK DALQQRMSVQ EDSVLQLKQE
190 200 210 220 230 240
LLRSSMTREE LEGQNVELER KLSERNRLLS EYKKELGQKD RLLQQQQTKL DDALRRISES
250 260 270 280 290 300
YHRLSGCENN GYSHMMDTSS AVFQHRMGDE LQLVRDALRS LRDSFSGHDP QHHTLDTLEQ
310 320 330 340 350 360
GVASLVDRLH TSDTKKRPER KGSTRSPGRK ANHTDRESWP STSKIAHSHS SPVLSAAAST
370 380 390 400 410 420
KVLYYTDRSL TPFLVNIPKR LGDVTLQDFK AAVDRHGSFR YHFKSLDPEF GTVKEEVFQD
430 440
DAVIPGWEGK IVAWVEEDHG EGR