ID  Q08495;
PN  Dematin;
GN  DMTN;
OS  9606;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm. Cytoplasm, cytosol. Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, cytoskeleton. Cell membrane. Membrane {ECO:0000250}. Endomembrane system. Cell projection {ECO:0000250}. Note=Localized at the spectrin-actin junction of erythrocyte plasma membrane. Localized to intracellular membranes and the cytoskeletal network. Localized at intracellular membrane-bounded organelle compartment in platelets that likely represent the dense tubular network membrane. Detected at the cell membrane and at the parasitophorous vacuole in malaria-infected erythrocytes at late stages of plasmodium berghei or falciparum development.
DR  UNIPROT: Q08495;
DR  UNIPROT: A8K0T5;
DR  UNIPROT: B3KP70;
DR  UNIPROT: B3KRH3;
DR  UNIPROT: B4DI75;
DR  UNIPROT: E9PEJ0;
DR  UNIPROT: Q13215;
DR  UNIPROT: Q9BRE3;
DR  PDB: 1QZP;
DR  PDB: 1ZV6;
DR  Pfam: PF16182;
DR  Pfam: PF02209;
DR  PROSITE: PS51089;
DR  OMIM: 125305;
DR  DisGeNET: 2039;
DE  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. Also plays a role as a modulator of actin dynamics in fibroblasts; acts as a 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. {ECO:0000269|PubMed:10565303, ECO:0000269|PubMed:11856323, ECO:0000269|PubMed:18347014, ECO:0000269|PubMed:19241372, ECO:0000269|PubMed:22927433, ECO:0000269|PubMed:23355471}.
DE  Reference Proteome: Yes;
DE  Interaction: O43237; IntAct: EBI-731827; Score: 0.00
DE  Interaction: Q9UNN8; IntAct: EBI-734445; Score: 0.00
DE  Interaction: Q86YD1; IntAct: EBI-735504; Score: 0.00
DE  Interaction: P62316; IntAct: EBI-736673; Score: 0.00
DE  Interaction: P31946; IntAct: EBI-8796749; Score: 0.35
DE  Interaction: P14618; IntAct: EBI-9355736; Score: 0.44
DE  Interaction: Q08379; IntAct: EBI-10225555; Score: 0.56
DE  Interaction: Q8TAP6; IntAct: EBI-24382670; Score: 0.56
DE  Interaction: Q8IYF3; IntAct: EBI-24387259; Score: 0.56
DE  Interaction: Q12933; IntAct: EBI-24472525; Score: 0.56
DE  Interaction: Q8IWV7; IntAct: EBI-21864310; Score: 0.35
DE  Interaction: Q86TI2; IntAct: EBI-21864310; Score: 0.35
DE  Interaction: P63104; IntAct: EBI-21864310; Score: 0.35
DE  Interaction: P62258; IntAct: EBI-21864310; Score: 0.35
DE  Interaction: P61981; IntAct: EBI-21864310; Score: 0.35
DE  Interaction: Q04917; IntAct: EBI-21907689; Score: 0.35
DE  Interaction: P50552; IntAct: EBI-30845230; Score: 0.44
GO  GO:0015629;
GO  GO:0005884;
GO  GO:0031253;
GO  GO:0030863;
GO  GO:0031410;
GO  GO:0005829;
GO  GO:0012505;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0031095;
GO  GO:0014069;
GO  GO:0014731;
GO  GO:0003779;
GO  GO:0051015;
GO  GO:0043621;
GO  GO:0005102;
GO  GO:0030507;
GO  GO:0030036;
GO  GO:0051017;
GO  GO:0051693;
GO  GO:0090527;
GO  GO:0035585;
GO  GO:0035584;
GO  GO:0071277;
GO  GO:0071320;
GO  GO:0007010;
GO  GO:0048821;
GO  GO:0030032;
GO  GO:0010812;
GO  GO:0051895;
GO  GO:0033137;
GO  GO:0010801;
GO  GO:0050732;
GO  GO:0090315;
GO  GO:1900025;
GO  GO:0030194;
GO  GO:0010763;
GO  GO:2001046;
GO  GO:1901731;
GO  GO:1900026;
GO  GO:0090303;
GO  GO:0070560;
GO  GO:0065003;
GO  GO:0032956;
GO  GO:0008360;
GO  GO:0051489;
GO  GO:0010591;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MERLQKQPLTSPGSVSPSRDSSVPGSPSSIVAKMDNQVLGYKDLAAIPKDKAILDIERPDLMIYEPHFTYSLLEHVELPR
SQ  SRERSLSPKSTSPPPSPEVWADSRSPGIISQASAPRTTGTPRTSLPHFHHPETSRPDSNIYKKPPIYKQRESVGGSPQTK
SQ  HLIEDLIIESSKFPAAQPPDPNQPAKIETDYWPCPPSLAVVETEWRKRKASRRGAEEEEEEEDDDSGEEMKALRERQREE
SQ  LSKVTSNLGKMILKEEMEKSLPIRRKTRSLPDRTPFHTSLHQGTSKSSSLPAYGRTTLSRLQSTEFSPSGSETGSPGLQN
SQ  GEGQRGRMDRGNSLPCVLEQKIYPYEMLVVTNKGRTKLPPGVDRMRLERHLSAEDFSRVFAMSPEEFGKLALWKRNELKK
SQ  KASLF
//