LLPS-Bot-a772
DMTN
Integrated Annotations
▼ OVERVIEW
Status: | Unreviewed |
Protein Name: | Dematin; Dematin actin-binding protein; Erythrocyte membrane protein band 4.9 |
Gene Name: | DMTN, DMT, EPB49 |
Ensembl Gene: | ENSBTAG00000045887.2 |
Ensembl Protein: | ENSBTAP00000062374.1 |
Organism: | Bos taurus |
Taxa ID: | 9913 |
LLPS Type: | Others |
▼ Classification
Condensates:
Condensate | Evidence | Orthologs |
---|---|---|
Postsynaptic density | Predicted from orthologs | (View) |
▼ FUNCTION
Membrane-cytoskeleton-associated protein with F-actin-binding activity that induces F-actin bundles formation and stabilization. Its F-actin-bundling activity is reversibly regulated upon its phosphorylation by the cAMP-dependent protein kinase A (PKA). Binds to the erythrocyte membrane glucose transporter-1 SLC2A1/GLUT1, and hence stabilizes and attaches the spectrin-actin network to the erythrocytic plasma membrane. Plays a role in maintaining the functional integrity of PKA-activated erythrocyte shape and the membrane mechanical properties. Plays also a role as a modulator of actin dynamics in fibroblasts; acts as negative regulator of the RhoA activation pathway. In platelets, functions as a regulator of internal calcium mobilization across the dense tubular system that affects platelet granule secretion pathways and aggregation. Also required for the formation of a diverse set of cell protrusions, such as filopodia and lamellipodia, necessary for platelet cell spreading, motility and migration. Acts as a tumor suppressor and inhibits malignant cell transformation (By similarity). |
▼ CROSS REFERENCE
Database | Nucleotide ID | Protein ID |
---|---|---|
Ensembl | ENSBTAT00000074551.1 | ENSBTAP00000062374.1 |
Ensembl | ENSBTAT00000067620.1 | ENSBTAP00000061425.1 |
Ensembl | ENSBTAT00000071384.1 | ENSBTAP00000067289.1 |
Ensembl | ENSBTAT00000066196.2 | ENSBTAP00000054225.2 |
Ensembl | ENSBTAT00000065148.2 | ENSBTAP00000054110.2 |
UniProt | Q08DM1, DEMA_BOVIN | |
GeneBank | BC123672 | AAI23673.1 |
Entrez | 512981 |
▼ SEQUENCE
Protein Sequence (FASTA) |
---|
1 MERLQKQPLT SPGSVSSSRD SSVPGSPSSI VAKMDNQVLG YKDLAAIPKD KAILDIERPD 60 61 LMIYEPHFTY SLLEHVELPR SRERSLSPKS TSPPPSPEVW AESRSPGTIS QASAPRTAGT 120 121 PRTSLPHFHH PETTRPDSNI YKKPPIYKQR AESTGGSPQS KHPIEDLIIE SSKFPAAQPP 180 181 DPNQPAKIET DYWPCPPSLA VVETEWRKRK ASRRGAEEEE EEEDDDSGEE MKALRERQRE 240 241 ELSKVTSNLG KMILKEEMEK SLPIRRKTRS LPDRTPFHTS LHAGTSKSSS LPAYGRTTLS 300 301 RLQSTDFSPS GSEAESPGLQ VSALRRGTCG PRKPWMDGET AVLGEGVVGP RSHLVRPQEA 360 361 HEKAGEVSLP HSGSLRLWSP QNGEGQRGRM DRGNSLPCVL EQKIYPYEML VVTNRGRTKL 420 421 PPGVDRMRLE RHLSAEDFSR VFSMSPEEFG KLALWKRNEL KKKASLF 467 |
Nucleotide CDS Sequence (FASTA) |
1 ATGGAACGAC TGCAGAAGCA ACCACTTACC TCCCCTGGGA GCGTCAGCTC CTCCCGAGAC 60 61 TCCAGTGTTC CCGGCTCTCC CTCCAGCATC GTGGCCAAGA TGGACAATCA AGTGCTGGGC 120 121 TATAAGGACT TGGCTGCCAT CCCCAAGGAC AAGGCCATCC TGGACATCGA GAGGCCTGAC 180 181 CTCATGATCT ATGAGCCCCA CTTTACCTAT TCTCTGCTGG AACACGTGGA GCTGCCCAGA 240 241 AGCCGGGAGC GCTCGCTGTC ACCCAAATCC ACATCCCCCC CACCATCCCC AGAGGTGTGG 300 301 GCAGAGAGCC GGTCTCCTGG AACCATCTCT CAGGCTTCAG CCCCGAGAAC TGCTGGGACC 360 361 CCCCGGACCA GCCTGCCCCA TTTCCATCAT CCTGAGACCA CTCGCCCAGA TTCCAATATC 420 421 TACAAGAAGC CCCCCATCTA CAAGCAGAGA GCAGAGTCCA CAGGAGGCAG CCCTCAGAGC 480 481 AAGCACCCCA TTGAGGACCT CATCATCGAG TCCTCCAAGT TCCCCGCAGC CCAGCCTCCC 540 541 GACCCCAACC AGCCAGCCAA GATCGAAACG GACTACTGGC CATGCCCCCC ATCTCTGGCT 600 601 GTTGTGGAAA CAGAATGGAG GAAGCGGAAG GCGTCGAGGA GGGGGGCCGA GGAGGAGGAG 660 661 GAGGAAGAGG ATGACGACTC CGGGGAGGAG ATGAAGGCTC TCAGGGAGCG GCAGAGAGAG 720 721 GAACTCAGTA AGGTTACTTC CAACTTGGGA AAGATGATCT TGAAAGAAGA GATGGAAAAG 780 781 TCATTGCCTA TTCGGAGGAA AACCCGCTCT CTGCCCGACC GGACACCCTT CCATACCTCC 840 841 TTGCACGCAG GAACGTCTAA ATCTTCTTCC CTCCCCGCCT ATGGCAGGAC CACCCTGAGC 900 901 CGGCTCCAGT CTACAGACTT CAGCCCATCT GGGAGTGAGG CTGAAAGCCC AGGTCTCCAG 960 961 AATGGAGAGG GCCAGAGGGG GAGGATGGAC CGGGGGAACT CCCTGCCCTG TGTGCTGGAG 1020 1021 CAGAAGATCT ATCCTTATGA AATGCTGGTG GTGACCAATA GGGGGCGAAC CAAGTTGCCT 1080 1081 CCAGGTGTGG ATCGGATGAG GCTGGAGAGG CACCTGTCAG CAGAAGACTT CTCTAGGGTC 1140 1141 TTCTCCATGT CTCCTGAAGA GTTTGGCAAG CTGGCTCTGT GGAAGCGGAA CGAACTCAAG 1200 1201 AAAAAGGCCT CTCTCTTCTG A 1221 |
▼ KEYWORD
▼ GENE ONTOLOGY
ID | Classification | Description |
Cellular Component | Actin cytoskeleton | |
Cellular Component | Actin filament | |
Cellular Component | Cell projection membrane | |
Cellular Component | Cortical cytoskeleton | |
Cellular Component | Cytoplasmic vesicle | |
Cellular Component | Cytosol | |
Cellular Component | Endomembrane system | |
Cellular Component | Perinuclear region of cytoplasm | |
Cellular Component | Plasma membrane | |
Cellular Component | Platelet dense tubular network membrane | |
Cellular Component | Postsynaptic density | |
Cellular Component | Spectrin-associated cytoskeleton | |
Molecular Function | Actin binding | |
Molecular Function | Actin filament binding | |
Molecular Function | Protein self-association | |
Molecular Function | Signaling receptor binding | |
Molecular Function | Spectrin binding | |
Biological Process | Actin cytoskeleton organization | |
Biological Process | Actin filament bundle assembly | |
Biological Process | Actin filament capping | |
Biological Process | Actin filament reorganization | |
Biological Process | Calcium-mediated signaling using extracellular calcium source | |
Biological Process | Calcium-mediated signaling using intracellular calcium source | |
Biological Process | Cellular response to calcium ion | |
Biological Process | Cellular response to cAMP | |
Biological Process | Erythrocyte development | |
Biological Process | Lamellipodium assembly | |
Biological Process | Negative regulation of cell-substrate adhesion | |
Biological Process | Negative regulation of focal adhesion assembly | |
Biological Process | Negative regulation of peptidyl-serine phosphorylation | |
Biological Process | Negative regulation of peptidyl-threonine phosphorylation | |
Biological Process | Negative regulation of peptidyl-tyrosine phosphorylation | |
Biological Process | Negative regulation of protein targeting to membrane | |
Biological Process | Negative regulation of substrate adhesion-dependent cell spreading | |
Biological Process | Positive regulation of blood coagulation | |
Biological Process | Positive regulation of fibroblast migration | |
Biological Process | Positive regulation of integrin-mediated signaling pathway | |
Biological Process | Positive regulation of platelet aggregation | |
Biological Process | Positive regulation of substrate adhesion-dependent cell spreading | |
Biological Process | Positive regulation of wound healing | |
Biological Process | Protein secretion by platelet | |
Biological Process | Protein-containing complex assembly | |
Biological Process | Regulation of actin cytoskeleton organization | |
Biological Process | Regulation of cell shape | |
Biological Process | Regulation of filopodium assembly | |
Biological Process | Regulation of lamellipodium assembly |
▼ ORTHOLOGY
DrLLPS ID | Organism | Identity | E-value | Score |
---|---|---|---|---|
LLPS-Hos-a781 | Homo sapiens | 0.0 | 659 | undefined |
LLPS-Mum-a768 | Mus musculus | 0.0 | 650 | undefined |