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Protein

Dematin

Gene

Dmtn

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.3 Publications

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • protein self-association Source: UniProtKB
  • receptor binding Source: UniProtKB
  • spectrin binding Source: UniProtKB

GO - Biological processi

  • actin cytoskeleton organization Source: UniProtKB
  • actin filament bundle assembly Source: UniProtKB
  • actin filament capping Source: UniProtKB-KW
  • actin filament reorganization Source: UniProtKB
  • calcium-mediated signaling using extracellular calcium source Source: UniProtKB
  • calcium-mediated signaling using intracellular calcium source Source: UniProtKB
  • cellular response to calcium ion Source: UniProtKB
  • cellular response to cAMP Source: UniProtKB
  • erythrocyte development Source: UniProtKB
  • negative regulation of cell-substrate adhesion Source: UniProtKB
  • negative regulation of focal adhesion assembly Source: UniProtKB
  • negative regulation of peptidyl-serine phosphorylation Source: UniProtKB
  • negative regulation of peptidyl-threonine phosphorylation Source: UniProtKB
  • negative regulation of peptidyl-tyrosine phosphorylation Source: UniProtKB
  • negative regulation of protein targeting to membrane Source: UniProtKB
  • negative regulation of substrate adhesion-dependent cell spreading Source: UniProtKB
  • positive regulation of blood coagulation Source: UniProtKB
  • positive regulation of fibroblast migration Source: UniProtKB
  • positive regulation of integrin-mediated signaling pathway Source: UniProtKB
  • positive regulation of platelet aggregation Source: UniProtKB
  • positive regulation of substrate adhesion-dependent cell spreading Source: UniProtKB
  • positive regulation of wound healing Source: UniProtKB
  • protein complex assembly Source: UniProtKB
  • protein secretion by platelet Source: UniProtKB
  • regulation of actin cytoskeleton organization Source: UniProtKB
  • regulation of cell shape Source: UniProtKB
  • regulation of filopodium assembly Source: UniProtKB
  • regulation of lamellipodium assembly Source: UniProtKB

Keywordsi

Molecular functionActin capping, Actin-binding

Enzyme and pathway databases

ReactomeiR-MMU-5223345. Miscellaneous transport and binding events.

Names & Taxonomyi

Protein namesi
Recommended name:
Dematin
Alternative name(s):
Dematin actin-binding protein
Erythrocyte membrane protein band 4.9
Gene namesi
Name:Dmtn
Synonyms:Epb4.9, Epb49
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:99670. Dmtn.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice are viable and born at the expected Mendelian ratio. Adult mice show compensated anemia and display mild microcytosis and spherocytosis. The erythrocyte plasma membrane association with the spectrin-actin skeleton is fragile and mechanically unstable.1 Publication

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002187561 – 405DematinAdd BLAST405

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei16PhosphoserineBy similarity1
Modified residuei18PhosphoserineBy similarity1
Modified residuei26PhosphoserineBy similarity1
Modified residuei92PhosphoserineCombined sources1
Modified residuei96PhosphoserineCombined sources1
Modified residuei110PhosphoserineCombined sources1
Modified residuei113PhosphoserineCombined sources1
Modified residuei114PhosphothreonineCombined sources1
Modified residuei156PhosphoserineCombined sources1
Modified residuei226PhosphoserineCombined sources1
Modified residuei269PhosphoserineBy similarity1
Modified residuei279PhosphoserineBy similarity1
Modified residuei289PhosphoserineBy similarity1
Modified residuei303PhosphoserineBy similarity1
Modified residuei315PhosphoserineCombined sources1
Modified residuei333PhosphoserineCombined sources1
Modified residuei372PhosphoserineCombined sources1
Modified residuei383PhosphoserineCombined sources1
Modified residuei403Phosphoserine; by PKABy similarity1

Post-translational modificationi

Phosphorylated. Phosphorylation at Ser-403 by PKA causes the C-terminal headpiece domain to associate with the N-terminal core domain, and leads to the inhibition of its actin bundling activity (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

PeptideAtlasiQ9WV69.
PRIDEiQ9WV69.

PTM databases

iPTMnetiQ9WV69.
PhosphoSitePlusiQ9WV69.

Expressioni

Tissue specificityi

Expressed in platelets. Isoform 1 and isoform 2 are expressed in mature erythrocytes (at protein level).2 Publications

Gene expression databases

BgeeiENSMUSG00000022099.
CleanExiMM_EPB4.9.
GenevisibleiQ9WV69. MM.

Interactioni

Subunit structurei

Monomeric (isoform 2); under reducing conditions. Self-associates. Exists under oxidizing condition as a trimer of two isoforms 2 and isoform 1 linked by disulfide bonds (Probable). Found in a complex with DMTN, F-actin and spectrin. Found in a complex with ADD2, DMTN and SLC2A1. Interacts with F-actin, ITPKB and spectrin. Isoform 2 interacts with SLC2A1 (via C-terminus cytoplasmic region) (By similarity). Interacts with RASGRF2.By similarityCurated2 Publications

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • protein self-association Source: UniProtKB
  • receptor binding Source: UniProtKB
  • spectrin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi199464. 1 interactor.
IntActiQ9WV69. 2 interactors.
MINTiMINT-4093018.

Structurei

3D structure databases

ProteinModelPortaliQ9WV69.
SMRiQ9WV69.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini337 – 405HPAdd BLAST69

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni224 – 308Interaction with RASGRF2By similarityAdd BLAST85

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi216 – 222Poly-Glu7

Domaini

Both the N-terminal core domain and the C-terminal headpiece domain are sufficient for binding to F-actin and necessary for actin bundling activity.

Sequence similaritiesi

Belongs to the villin/gelsolin family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00760000119039.
HOGENOMiHOG000285997.
HOVERGENiHBG031499.
InParanoidiQ9WV69.
OMAiYKQREST.
OrthoDBiEOG091G06PE.
PhylomeDBiQ9WV69.
TreeFamiTF318042.

Family and domain databases

Gene3Di1.10.950.10. 1 hit.
InterProiView protein in InterPro
IPR032402. AbLIM_anchor.
IPR003128. Villin_headpiece.
IPR036886. Villin_headpiece_dom_sf.
PfamiView protein in Pfam
PF16182. AbLIM_anchor. 2 hits.
PF02209. VHP. 1 hit.
SMARTiView protein in SMART
SM00153. VHP. 1 hit.
SUPFAMiSSF47050. SSF47050. 1 hit.
PROSITEiView protein in PROSITE
PS51089. HP. 1 hit.

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9WV69-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MERLQKQPLT SPGSVSSSRD SSVPGSPSSI VAKMDNQVLG YKDLAAIPKD
60 70 80 90 100
KAILDIERPD LMIYEPHFTY SLLEHVELPR SRECSLSPKS TSPPPSPEVW
110 120 130 140 150
AESRTLGIIS QASTPRTTGT PRTSLPHFHH PETTRPDSNI YKKPPIYKQR
160 170 180 190 200
ESVGGSPQSK HLIEDLIIES SKFPAAQPPD PNQPAKIETD YWPCPPSLAV
210 220 230 240 250
VETEWRKRKA SRKGAEEEEE EEDDDSEEEI KAIRERQKEE LSKVTSNLGK
260 270 280 290 300
MILKEEMEKS LPIRRKTRSL PDRTPFHTSL HSGTSKSSSL PSYGRTTLSR
310 320 330 340 350
LQSTEFSPSG SEAGSPGLQN GEGQRGRMDR GNSLPCVLEQ KIYPYEMLVV
360 370 380 390 400
TNKGRTKLPP GVDRMRLERH LSAEDFSRVF AMSPEEFGKL ALWKRNELKK

KASLF
Length:405
Mass (Da):45,468
Last modified:November 1, 1999 - v1
Checksum:iAECA552500BDD19A
GO
Isoform 2 (identifier: Q9WV69-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     320-341: Missing.

Show »
Length:383
Mass (Da):43,042
Checksum:iC8F3299489322DF1
GO
Isoform 3 (identifier: Q9WV69-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     7-31: Missing.

Show »
Length:380
Mass (Da):43,071
Checksum:i27E8E56877D0B310
GO
Isoform 4 (identifier: Q9WV69-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     7-31: Missing.
     320-341: Missing.

Show »
Length:358
Mass (Da):40,644
Checksum:i6EF6B051450E509C
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0474917 – 31Missing in isoform 3 and isoform 4. 2 PublicationsAdd BLAST25
Alternative sequenceiVSP_047492320 – 341Missing in isoform 2 and isoform 4. 3 PublicationsAdd BLAST22

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF079846 mRNA. Translation: AAD34233.1.
AF155547 mRNA. Translation: AAD38412.1.
AK158744 mRNA. Translation: BAE34638.1.
AK162866 mRNA. Translation: BAE37092.1.
AK165294 mRNA. Translation: BAE38123.1.
AC154563 Genomic DNA. No translation available.
BC016897 mRNA. Translation: AAH16897.1.
BC037021 mRNA. Translation: AAH37021.1.
CCDSiCCDS27259.1. [Q9WV69-2]
RefSeqiNP_001239591.1. NM_001252662.1. [Q9WV69-1]
NP_001239592.1. NM_001252663.1. [Q9WV69-2]
NP_001239593.1. NM_001252664.1. [Q9WV69-3]
NP_001239594.1. NM_001252665.1. [Q9WV69-4]
NP_001239595.1. NM_001252666.1. [Q9WV69-4]
NP_038542.1. NM_013514.4. [Q9WV69-2]
XP_006518593.1. XM_006518530.3. [Q9WV69-1]
XP_006518594.1. XM_006518531.2. [Q9WV69-1]
XP_006518595.1. XM_006518532.2. [Q9WV69-1]
XP_006518602.1. XM_006518539.2. [Q9WV69-3]
XP_006518603.1. XM_006518540.3. [Q9WV69-3]
XP_006518604.1. XM_006518541.2. [Q9WV69-3]
XP_006518605.1. XM_006518542.3. [Q9WV69-4]
XP_017171327.1. XM_017315838.1. [Q9WV69-1]
XP_017171328.1. XM_017315839.1. [Q9WV69-2]
XP_017171329.1. XM_017315840.1. [Q9WV69-4]
UniGeneiMm.210863.

Genome annotation databases

EnsembliENSMUST00000022694; ENSMUSP00000022694; ENSMUSG00000022099. [Q9WV69-2]
ENSMUST00000022695; ENSMUSP00000022695; ENSMUSG00000022099. [Q9WV69-3]
ENSMUST00000110984; ENSMUSP00000106612; ENSMUSG00000022099. [Q9WV69-2]
GeneIDi13829.
KEGGimmu:13829.
UCSCiuc007uom.2. mouse. [Q9WV69-1]
uc029sln.1. mouse. [Q9WV69-4]
uc029slq.1. mouse. [Q9WV69-3]
uc033grx.1. mouse. [Q9WV69-2]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiDEMA_MOUSE
AccessioniPrimary (citable) accession number: Q9WV69
Secondary accession number(s): F8WIF9
, Q3TYC5, Q8JZV5, Q9WVM2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: November 1, 1999
Last modified: October 25, 2017
This is version 124 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families