Search by BoMiProt ID - Bomi4892


Primary Information

BoMiProt ID Bomi4892
Protein Name Costars family protein ABRACL/ABRA C-terminal-like protein
Organism Bos taurus
Uniprot IdQ3ZBN0
Milk FractionExosomes
Ref Sequence Id NP_001160033.1
Aminoacid Length 81
Molecular Weight 9047
Fasta Sequence https://www.uniprot.org/uniprot/Q3ZBN0.fasta
Gene Name ABRACL
Gene Id 505914
Protein Existence Status Reviewed

Secondary Information

Presence in other biological fluids/tissue/cells abdominal lymph node 
Protein Function ABRACL modulates actin dynamics through its interaction with cofilin and thereby regulates cancer cell migration and participates in cancer pathogenesis.
Biochemical Properties Although ABRACL resembles the F-actin-binding domain of ABRA, it has further defined two F-actin-binding domains, ABD1 (aa 193–296) and ABD2 (aa 294–375); both domains can bind F-actin independently when tested in vitro, but ABD2 binds with a much lower affinity than ABD1. The protein sequence of ABRACL exhibits homology mostly to ABD2, with ~40% identities and ~60% similarities to aa 326–381 of ABRA.
PTMs N-acetylation at Meth
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
na
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction No TM helices
Additional Comments ABRACL is overexpressed in cancerous tissues and that cancer cells with ABRACL expression, rather than cells depleted of ABRACL, migrate more robustly, proliferate better, and are more capable of generating colonies even under anchorage-independent conditions.
Bibliography 1.Hsiao BY, Chen CH, Chi HY, Yen PR, Yu YZ, Lin CH, Pang TL, Lin WC, Li ML, Yeh YC, Chou TY, Chen MY. Human Costars Family Protein ABRACL Modulates Actin Dynamics and Cell Migration and Associates with Tumorigenic Growth. Int J Mol Sci. 2021 Feb 18;22(4):2037. doi: 10.3390/ijms22042037. PMID: 33670794; PMCID: PMC7922284. 2.Fogl C., Puckey L., Hinssen U., Zaleska M., El-Mezgueldi M., Croasdale R., Bowman A., Matsukawa A., Samani N.J., Savva R., et al. A structural and functional dissection of the cardiac stress response factor MS1. Proteins. 2012;80:398–409. doi: 10.1002/prot.23201.