DEMA_MOUSE
ID DEMA_MOUSE Reviewed; 405 AA.
AC Q9WV69; F8WIF9; Q3TYC5; Q8JZV5; Q9WVM2;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Dematin;
DE AltName: Full=Dematin actin-binding protein;
DE AltName: Full=Erythrocyte membrane protein band 4.9;
GN Name=Dmtn; Synonyms=Epb4.9, Epb49;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Erythrocyte, and Spleen;
RX PubMed=10501976; DOI=10.1007/s003359901153;
RA Azim A.C., Kim A.C., Lutchman M., Andrabi S., Peters L.L., Chishti A.H.;
RT "cDNA sequence, genomic structure, and expression of the mouse dematin gene
RT (Epb4.9).";
RL Mamm. Genome 10:1026-1029(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Hypothalamus, Spleen, and Visual cortex;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
RC STRAIN=FVB/N; TISSUE=Eye, and Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH RASGRF2.
RX PubMed=11856323; DOI=10.1046/j.0014-2956.2001.02694.x;
RA Lutchman M., Kim A.C., Cheng L., Whitehead I.P., Oh S.S., Hanspal M.,
RA Boukharov A.A., Hanada T., Chishti A.H.;
RT "Dematin interacts with the Ras-guanine nucleotide exchange factor Ras-GRF2
RT and modulates mitogen-activated protein kinase pathways.";
RL Eur. J. Biochem. 269:638-649(2002).
RN [6]
RP FUNCTION, SUBUNIT, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=12011427; DOI=10.1073/pnas.052155999;
RA Khanna R., Chang S.H., Andrabi S., Azam M., Kim A., Rivera A., Brugnara C.,
RA Low P.S., Liu S.C., Chishti A.H.;
RT "Headpiece domain of dematin is required for the stability of the
RT erythrocyte membrane.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:6637-6642(2002).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156; SER-226 AND SER-372, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-114 AND SER-226, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18505823; DOI=10.1128/mcb.00237-08;
RA Mohseni M., Chishti A.H.;
RT "The headpiece domain of dematin regulates cell shape, motility, and wound
RT healing by modulating RhoA activation.";
RL Mol. Cell. Biol. 28:4712-4718(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92; SER-96; SER-110; SER-113;
RP THR-114; SER-226; SER-315; SER-333 AND SER-383, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [12]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=23060452; DOI=10.1074/jbc.m112.364679;
RA Wieschhaus A.J., Le Breton G.C., Chishti A.H.;
RT "Headpiece domain of dematin regulates calcium mobilization and signaling
RT in platelets.";
RL J. Biol. Chem. 287:41218-41231(2012).
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.
CC {ECO:0000269|PubMed:12011427, ECO:0000269|PubMed:18505823,
CC ECO:0000269|PubMed:23060452}.
CC -!- SUBUNIT: Monomeric (isoform 2); under reducing conditions. Self-
CC associates. Exists under oxidizing condition as a trimer of two
CC isoforms 2 and isoform 1 linked by disulfide bonds (Probable). Found in
CC 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 Isoform 2 interacts with SLC2A1 (via C-terminus cytoplasmic region) (By
CC similarity). Interacts with RASGRF2. {ECO:0000250,
CC ECO:0000269|PubMed:11856323, ECO:0000269|PubMed:12011427, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:18505823}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:18505823}. Cytoplasm, cytoskeleton {ECO:0000250}.
CC Cell membrane {ECO:0000250}. Membrane {ECO:0000269|PubMed:18505823}.
CC Endomembrane system {ECO:0000250}. Cell projection
CC {ECO:0000269|PubMed:18505823}. Note=Localized at the spectrin-actin
CC junction of erythrocyte plasma membrane. Localized to intracellular
CC membranes and the cytoskeletal network. Localized at intracellular
CC membrane-bounded organelle compartment in platelets that likely
CC represent the dense tubular network membrane (By similarity).
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9WV69-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9WV69-2; Sequence=VSP_047492;
CC Name=3;
CC IsoId=Q9WV69-3; Sequence=VSP_047491;
CC Name=4;
CC IsoId=Q9WV69-4; Sequence=VSP_047491, VSP_047492;
CC -!- TISSUE SPECIFICITY: Expressed in platelets. Isoform 1 and isoform 2 are
CC expressed in mature erythrocytes (at protein level).
CC {ECO:0000269|PubMed:12011427, ECO:0000269|PubMed:23060452}.
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.
CC -!- PTM: Phosphorylated. Phosphorylation at Ser-403 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 -!- DISRUPTION PHENOTYPE: Mice are viable and born at the expected
CC Mendelian ratio. Adult mice show compensated anemia and display mild
CC microcytosis and spherocytosis. The erythrocyte plasma membrane
CC association with the spectrin-actin skeleton is fragile and
CC mechanically unstable. {ECO:0000269|PubMed:12011427}.
CC -!- SIMILARITY: Belongs to the villin/gelsolin family. {ECO:0000305}.
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DR EMBL; AF079846; AAD34233.1; -; mRNA.
DR EMBL; AF155547; AAD38412.1; -; mRNA.
DR EMBL; AK158744; BAE34638.1; -; mRNA.
DR EMBL; AK162866; BAE37092.1; -; mRNA.
DR EMBL; AK165294; BAE38123.1; -; mRNA.
DR EMBL; AC154563; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC016897; AAH16897.1; -; mRNA.
DR EMBL; BC037021; AAH37021.1; -; mRNA.
DR CCDS; CCDS27259.1; -. [Q9WV69-2]
DR CCDS; CCDS88706.1; -. [Q9WV69-4]
DR CCDS; CCDS88707.1; -. [Q9WV69-3]
DR CCDS; CCDS88708.1; -. [Q9WV69-1]
DR RefSeq; NP_001239591.1; NM_001252662.1. [Q9WV69-1]
DR RefSeq; NP_001239592.1; NM_001252663.1. [Q9WV69-2]
DR RefSeq; NP_001239593.1; NM_001252664.1. [Q9WV69-3]
DR RefSeq; NP_001239594.1; NM_001252665.1. [Q9WV69-4]
DR RefSeq; NP_001239595.1; NM_001252666.1. [Q9WV69-4]
DR RefSeq; NP_038542.1; NM_013514.4. [Q9WV69-2]
DR RefSeq; XP_006518593.1; XM_006518530.3.
DR RefSeq; XP_006518594.1; XM_006518531.2.
DR RefSeq; XP_006518595.1; XM_006518532.2.
DR RefSeq; XP_006518602.1; XM_006518539.2.
DR RefSeq; XP_006518603.1; XM_006518540.3.
DR RefSeq; XP_006518604.1; XM_006518541.2.
DR RefSeq; XP_006518605.1; XM_006518542.3.
DR RefSeq; XP_017171327.1; XM_017315838.1.
DR RefSeq; XP_017171328.1; XM_017315839.1.
DR RefSeq; XP_017171329.1; XM_017315840.1.
DR AlphaFoldDB; Q9WV69; -.
DR BMRB; Q9WV69; -.
DR SMR; Q9WV69; -.
DR BioGRID; 199464; 8.
DR IntAct; Q9WV69; 1.
DR STRING; 10090.ENSMUSP00000106612; -.
DR iPTMnet; Q9WV69; -.
DR PhosphoSitePlus; Q9WV69; -.
DR jPOST; Q9WV69; -.
DR MaxQB; Q9WV69; -.
DR PeptideAtlas; Q9WV69; -.
DR PRIDE; Q9WV69; -.
DR ProteomicsDB; 277312; -. [Q9WV69-1]
DR ProteomicsDB; 277313; -. [Q9WV69-2]
DR ProteomicsDB; 277314; -. [Q9WV69-3]
DR ProteomicsDB; 277315; -. [Q9WV69-4]
DR Antibodypedia; 9250; 247 antibodies from 31 providers.
DR DNASU; 13829; -.
DR Ensembl; ENSMUST00000022694; ENSMUSP00000022694; ENSMUSG00000022099. [Q9WV69-1]
DR Ensembl; ENSMUST00000022695; ENSMUSP00000022695; ENSMUSG00000022099. [Q9WV69-3]
DR Ensembl; ENSMUST00000110984; ENSMUSP00000106612; ENSMUSG00000022099. [Q9WV69-2]
DR Ensembl; ENSMUST00000228001; ENSMUSP00000153945; ENSMUSG00000022099. [Q9WV69-4]
DR Ensembl; ENSMUST00000228009; ENSMUSP00000153828; ENSMUSG00000022099. [Q9WV69-2]
DR Ensembl; ENSMUST00000228295; ENSMUSP00000154373; ENSMUSG00000022099. [Q9WV69-3]
DR Ensembl; ENSMUST00000228824; ENSMUSP00000154045; ENSMUSG00000022099. [Q9WV69-4]
DR GeneID; 13829; -.
DR KEGG; mmu:13829; -.
DR UCSC; uc007uom.2; mouse. [Q9WV69-1]
DR UCSC; uc029sln.1; mouse. [Q9WV69-4]
DR UCSC; uc029slq.1; mouse. [Q9WV69-3]
DR UCSC; uc033grx.1; mouse. [Q9WV69-2]
DR CTD; 2039; -.
DR MGI; MGI:99670; Dmtn.
DR VEuPathDB; HostDB:ENSMUSG00000022099; -.
DR eggNOG; KOG1044; Eukaryota.
DR GeneTree; ENSGT00950000182850; -.
DR HOGENOM; CLU_001357_12_1_1; -.
DR InParanoid; Q9WV69; -.
DR OMA; DWLENRS; -.
DR OrthoDB; 1083894at2759; -.
DR PhylomeDB; Q9WV69; -.
DR TreeFam; TF318042; -.
DR Reactome; R-MMU-5223345; Miscellaneous transport and binding events.
DR BioGRID-ORCS; 13829; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Dmtn; mouse.
DR PRO; PR:Q9WV69; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9WV69; protein.
DR Bgee; ENSMUSG00000022099; Expressed in primary visual cortex and 202 other tissues.
DR ExpressionAtlas; Q9WV69; baseline and differential.
DR Genevisible; Q9WV69; MM.
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; IDA:UniProtKB.
DR GO; GO:0030863; C:cortical cytoskeleton; IDA:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA: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:0014069; C:postsynaptic density; IDA:MGI.
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; IDA: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; IMP: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; IMP:UniProtKB.
DR GO; GO:0035585; P:calcium-mediated signaling using extracellular calcium source; IMP:UniProtKB.
DR GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; IMP:UniProtKB.
DR GO; GO:0071277; P:cellular response to calcium ion; IMP:UniProtKB.
DR GO; GO:0071320; P:cellular response to cAMP; ISS:UniProtKB.
DR GO; GO:0048821; P:erythrocyte development; IMP:UniProtKB.
DR GO; GO:0030032; P:lamellipodium assembly; IBA:GO_Central.
DR GO; GO:0010812; P:negative regulation of cell-substrate adhesion; IMP:UniProtKB.
DR GO; GO:0051895; P:negative regulation of focal adhesion assembly; IMP:UniProtKB.
DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IMP:UniProtKB.
DR GO; GO:0010801; P:negative regulation of peptidyl-threonine phosphorylation; IMP:UniProtKB.
DR GO; GO:0050732; P:negative regulation of peptidyl-tyrosine phosphorylation; IMP:UniProtKB.
DR GO; GO:0090315; P:negative regulation of protein targeting to membrane; IMP:UniProtKB.
DR GO; GO:1900025; P:negative regulation of substrate adhesion-dependent cell spreading; IMP:UniProtKB.
DR GO; GO:0030194; P:positive regulation of blood coagulation; IMP:UniProtKB.
DR GO; GO:0010763; P:positive regulation of fibroblast migration; IDA:UniProtKB.
DR GO; GO:2001046; P:positive regulation of integrin-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:1901731; P:positive regulation of platelet aggregation; IMP:UniProtKB.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IMP:UniProtKB.
DR GO; GO:0090303; P:positive regulation of wound healing; IMP:UniProtKB.
DR GO; GO:0070560; P:protein secretion by platelet; IMP:UniProtKB.
DR GO; GO:0065003; P:protein-containing complex assembly; IDA:UniProtKB.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IDA: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 1: Evidence at protein level;
KW Actin capping; Actin-binding; Alternative splicing; Cell membrane;
KW Cell projection; Cytoplasm; Cytoskeleton; Disulfide bond; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; Tumor suppressor.
FT CHAIN 1..405
FT /note="Dematin"
FT /id="PRO_0000218756"
FT DOMAIN 337..405
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 81..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..308
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 108..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..318
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:0007744|PubMed:21183079"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 114
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08495"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08495"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08495"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08495"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 403
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:Q08495"
FT VAR_SEQ 7..31
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_047491"
FT VAR_SEQ 320..341
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10501976,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_047492"
SQ SEQUENCE 405 AA; 45468 MW; AECA552500BDD19A CRC64;
MERLQKQPLT SPGSVSSSRD SSVPGSPSSI VAKMDNQVLG YKDLAAIPKD KAILDIERPD
LMIYEPHFTY SLLEHVELPR SRECSLSPKS TSPPPSPEVW AESRTLGIIS QASTPRTTGT
PRTSLPHFHH PETTRPDSNI YKKPPIYKQR ESVGGSPQSK HLIEDLIIES SKFPAAQPPD
PNQPAKIETD YWPCPPSLAV VETEWRKRKA SRKGAEEEEE EEDDDSEEEI KAIRERQKEE
LSKVTSNLGK MILKEEMEKS LPIRRKTRSL PDRTPFHTSL HSGTSKSSSL PSYGRTTLSR
LQSTEFSPSG SEAGSPGLQN GEGQRGRMDR GNSLPCVLEQ KIYPYEMLVV TNKGRTKLPP
GVDRMRLERH LSAEDFSRVF AMSPEEFGKL ALWKRNELKK KASLF
