ID  Q5R4B6;
PN  Dematin;
GN  DMTN;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000250}. Membrane {ECO:0000250}. Endomembrane system {ECO:0000250}. 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 (By similarity). {ECO:0000250}.
DR  UNIPROT: Q5R4B6;
DR  Pfam: PF16182;
DR  Pfam: PF02209;
DR  PROSITE: PS51089;
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 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). {ECO:0000250}.
DE  Reference Proteome: Yes;
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: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:0048821;
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
//