Primary Information |
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| BoMiProt ID | Bomi4022 |
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| Protein Name | Armadillo repeat-containing protein 8 |
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| Organism | Bos taurus |
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| Uniprot ID | Q2KI54 |
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| Milk Fraction | Whey |
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| Ref Sequence ID | NP_001039923.1 |
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| Aminoacid Length | 673 |
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| Molecular Weight | 75451 |
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| FASTA Sequence |
Download |
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| Gene Name | ARMC8 |
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| Gene ID | 539591 |
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| Protein Existence Status | reviewed |
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Secondary Information |
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| Protein Function | Armc8 is involved in the negative regulation of adherens junctional CCC complex members possibly through the degradation of αE-catenin.ARMC8 binds to the N-terminal sequence of α-catenin (amino acids 82–148) and promotes its degradation to regulate cell adhesion.ARMC8 upregulates matrix metalloproteinase-7 and Snail and degrades α-catenin to disrupt the α-catenin/E-cadherin complex and promote the migration and invasion of hepatocellular carcinoma, breast cancer.ARMC8 upregulates the expression of β-catenin, cyclin D1, MMP7, and c-Myc induced by TGF-β1 by activating the canonical Wnt signaling pathway and thereby promote the proliferation, migration, invasion and epithelial-mesenchymal transition (EMT) of lung cancer and bladder cancer cells |
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| Biochemical Properties | ARMC8 is highly conserved across vertebrates. It is a key component of the C-terminal of the lissencephaly type-1-like homology motif (CTLH) complex, which has E-3 ligase activity. C-terminal domain of human Armc8α is able to interact with human αE-catenin .This binding domain resides between its two armadillo domains. |
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| Significance in milk | cell–cell contacts and intracellular signaling |
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| PTMs | Acetylation and phosphorylation |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|Q2KI54|ARMC8_BOVIN Armadillo repeat-containing protein 8 OS=Bos taurus OX=9913 GN=ARMC8 PE=2 SV=1
MACLLETPIRMSVLSEVTASSRHYVDRLFDPDPQKVLQGVIDMKNAVIGNNKQKANLIVL
GAVPRLLYLLQQETSSTELKTECAVVLGSLAMGTENNVKSLLDCHIIPALLQGLLSPDLK
FIEACLRCLRTIFTSPVTPEELLYTDATVIPHLMALLSRSRYTQEYICQIFSHCCKGPDH
QTILFNHGAVQNIAHLLTSVSYKVRMQALKCFSVLAFENPQVSMTLVNVLVDGELLPQIF
VKMLQRDKPIEMQLTSAKCLTYMCRAGAIRTDDNCIVLKTLPCLVRMCSKERLLEERVEG
AETLAYLIEPDVELQRIASITDHLIAMLADYFKYPSS*337VSAITDIKRLDHDLKHAHELRQA
AFKLYASLGANDEDIRKKIIDTENMMDRIVTGLSESSVKVRLAAVRCLHSLSRSVQQLRT
SFQDHAVWKPLMKVLQNAPDEILVVASSMLCNLLLEFSPSKEPILESGAVELLCGLTQSE
NPALRVNGIWALMNMAFQAEQKIKADILRSLS*512TEQLFRLLSDSDLNVLMKTLGLLRNLLS
TRPHIDKIMSTHGKQIMQAVTLILEGEHNIEVKEQTLCILANIADGTTAKELIMTNDDIL
QKIKYYMGHSHVKLQLAAMFCISNLVWNEEEGSQERQDKLRDMGIVDILHKLSQSPDSNL
CDKAKTALQQYLA
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| Predicted Disorder Regions | NA |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Bibliography | Huang Y, Jiang Z, Gao X, Luo P, Jiang X. ARMC Subfamily: Structures, Functions, Evolutions, Interactions, and Diseases. Front Mol Biosci. 2021 Nov 29;8:791597. doi: 10.3389/fmolb.2021.791597. PMID: 34912852; PMCID: PMC8666550. |
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