DEMA_BOVIN
ID DEMA_BOVIN Reviewed; 406 AA.
AC Q08DM1;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Dematin;
DE AltName: Full=Dematin actin-binding protein;
DE AltName: Full=Erythrocyte membrane protein band 4.9;
GN Name=DMTN; Synonyms=DMT, EPB49;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Brain cortex;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Membrane-cytoskeleton-associated protein with F-actin-binding
CC activity that induces F-actin bundles formation and stabilization. Its
CC F-actin-bundling activity is reversibly regulated upon its
CC phosphorylation by the cAMP-dependent protein kinase A (PKA). Binds to
CC the erythrocyte membrane glucose transporter-1 SLC2A1/GLUT1, and hence
CC stabilizes and attaches the spectrin-actin network to the erythrocytic
CC plasma membrane. Plays a role in maintaining the functional integrity
CC of PKA-activated erythrocyte shape and the membrane mechanical
CC properties. Also plays a role as a modulator of actin dynamics in
CC fibroblasts; acts as negative regulator of the RhoA activation pathway.
CC In platelets, functions as a regulator of internal calcium mobilization
CC across the dense tubular system that affects platelet granule secretion
CC pathways and aggregation. Also required for the formation of a diverse
CC set of cell protrusions, such as filopodia and lamellipodia, necessary
CC for platelet cell spreading, motility and migration. Acts as a tumor
CC suppressor and inhibits malignant cell transformation (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Monomeric; under reducing conditions. Self-associates. Exists
CC under oxidizing condition as a trimer linked by disulfide bonds. Found
CC in a complex with DMTN, F-actin and spectrin. Found in a complex with
CC ADD2, DMTN and SLC2A1. Interacts with F-actin, ITPKB and spectrin.
CC Interacts with SLC2A1 (via C-terminus cytoplasmic region). Interacts
CC with RASGRF2 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytosol
CC {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm,
CC cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000250}. Membrane
CC {ECO:0000250}. Endomembrane system {ECO:0000250}. Cell projection
CC {ECO:0000250}. Note=Localized at the spectrin-actin junction of
CC erythrocyte plasma membrane. Localized to intracellular membranes and
CC the cytoskeletal network. Localized at intracellular membrane-bounded
CC organelle compartment in platelets that likely represent the dense
CC tubular network membrane (By similarity). {ECO:0000250}.
CC -!- DOMAIN: Both the N-terminal core domain and the C-terminal headpiece
CC domain are sufficient for binding to F-actin and necessary for actin
CC bundling activity. {ECO:0000250}.
CC -!- PTM: Phosphorylated. Phosphorylation at Ser-404 by PKA causes the C-
CC terminal headpiece domain to associate with the N-terminal core domain,
CC and leads to the inhibition of its actin bundling activity (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the villin/gelsolin family. {ECO:0000305}.
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DR EMBL; BC123672; AAI23673.1; -; mRNA.
DR AlphaFoldDB; Q08DM1; -.
DR SMR; Q08DM1; -.
DR PaxDb; Q08DM1; -.
DR Ensembl; ENSBTAT00000067620; ENSBTAP00000061425; ENSBTAG00000045887.
DR VEuPathDB; HostDB:ENSBTAG00000045887; -.
DR VGNC; VGNC:56943; DMTN.
DR eggNOG; KOG1044; Eukaryota.
DR GeneTree; ENSGT00950000182850; -.
DR InParanoid; Q08DM1; -.
DR TreeFam; TF318042; -.
DR Proteomes; UP000009136; Chromosome 8.
DR Bgee; ENSBTAG00000045887; Expressed in temporal cortex and 99 other tissues.
DR ExpressionAtlas; Q08DM1; baseline.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005884; C:actin filament; ISS:UniProtKB.
DR GO; GO:0031253; C:cell projection membrane; ISS:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0031095; C:platelet dense tubular network membrane; ISS:UniProtKB.
DR GO; GO:0014731; C:spectrin-associated cytoskeleton; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; ISS:UniProtKB.
DR GO; GO:0030507; F:spectrin binding; ISS:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0051017; P:actin filament bundle assembly; ISS:UniProtKB.
DR GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR GO; GO:0090527; P:actin filament reorganization; ISS:UniProtKB.
DR GO; GO:0035585; P:calcium-mediated signaling using extracellular calcium source; ISS:UniProtKB.
DR GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; ISS:UniProtKB.
DR GO; GO:0071277; P:cellular response to calcium ion; ISS:UniProtKB.
DR GO; GO:0071320; P:cellular response to cAMP; ISS:UniProtKB.
DR GO; GO:0048821; P:erythrocyte development; ISS:UniProtKB.
DR GO; GO:0030032; P:lamellipodium assembly; IBA:GO_Central.
DR GO; GO:0010812; P:negative regulation of cell-substrate adhesion; ISS:UniProtKB.
DR GO; GO:0051895; P:negative regulation of focal adhesion assembly; ISS:UniProtKB.
DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; ISS:UniProtKB.
DR GO; GO:0010801; P:negative regulation of peptidyl-threonine phosphorylation; ISS:UniProtKB.
DR GO; GO:0050732; P:negative regulation of peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
DR GO; GO:0090315; P:negative regulation of protein targeting to membrane; ISS:UniProtKB.
DR GO; GO:1900025; P:negative regulation of substrate adhesion-dependent cell spreading; ISS:UniProtKB.
DR GO; GO:0030194; P:positive regulation of blood coagulation; ISS:UniProtKB.
DR GO; GO:0010763; P:positive regulation of fibroblast migration; ISS:UniProtKB.
DR GO; GO:2001046; P:positive regulation of integrin-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:1901731; P:positive regulation of platelet aggregation; ISS:UniProtKB.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISS:UniProtKB.
DR GO; GO:0090303; P:positive regulation of wound healing; ISS:UniProtKB.
DR GO; GO:0070560; P:protein secretion by platelet; ISS:UniProtKB.
DR GO; GO:0065003; P:protein-containing complex assembly; ISS:UniProtKB.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR GO; GO:0051489; P:regulation of filopodium assembly; ISS:UniProtKB.
DR GO; GO:0010591; P:regulation of lamellipodium assembly; ISS:UniProtKB.
DR Gene3D; 1.10.950.10; -; 1.
DR InterPro; IPR032402; AbLIM_anchor.
DR InterPro; IPR003128; Villin_headpiece.
DR InterPro; IPR036886; Villin_headpiece_dom_sf.
DR Pfam; PF16182; AbLIM_anchor; 2.
DR Pfam; PF02209; VHP; 1.
DR SMART; SM00153; VHP; 1.
DR SUPFAM; SSF47050; SSF47050; 1.
DR PROSITE; PS51089; HP; 1.
PE 2: Evidence at transcript level;
KW Actin capping; Actin-binding; Cell membrane; Cell projection; Cytoplasm;
KW Cytoskeleton; Disulfide bond; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; Tumor suppressor.
FT CHAIN 1..406
FT /note="Dematin"
FT /id="PRO_0000284659"
FT DOMAIN 338..406
FT /note="HP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00595"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..309
FT /note="Interaction with RASGRF2"
FT /evidence="ECO:0000250"
FT COMPBIAS 7..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..217
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08495"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08495"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08495"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08495"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08495"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08495"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WV69"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WV69"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08495"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08495"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08495"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08495"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08495"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08495"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WV69"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08495"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08495"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08495"
FT MOD_RES 404
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:Q08495"
SQ SEQUENCE 406 AA; 45548 MW; 08D6A99F3EFEEFC9 CRC64;
MERLQKQPLT SPGSVSSSRD SSVPGSPSSI VAKMDNQVLG YKDLAAIPKD KAILDIERPD
LMIYEPHFTY SLLEHVELPR SRERSLSPKS TSPPPSPEVW AESRSPGTIS QASAPRTAGT
PRTSLPHFHH PETTRPDSNI YKKPPIYKQR AESTGGSPQS KHPIEDLIIE SSKFPAAQPP
DPNQPAKIET DYWPCPPSLA VVETEWRKRK ASRRGAEEEE EEEDDDSGEE MKALRERQRE
ELSKVTSNLG KMILKEEMEK SLPIRRKTRS LPDRTPFHTS LHAGTSKSSS LPAYGRTTLS
RLQSTDFSPS GSEAESPGLQ NGEGQRGRMD RGNSLPCVLE QKIYPYEMLV VTNRGRTKLP
PGVDRMRLER HLSAEDFSRV FSMSPEEFGK LALWKRNELK KKASLF
