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Reviewed, UniProtKB/Swiss-Prot Q08495 (DEMA_HUMAN)

Last modified June 16, 2009. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Dematin
Alternative name(s):
    Erythrocyte membrane protein band 4.9
Gene names
Name: EPB49
Synonyms: DMT
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length405 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Actin-bundling protein. May function in mitogen-activated protein kinase pathway. Ref.6

Subunit structure

Exists in solution as a trimer of two short isoforms and one long isoform linked by disulfide bonds Probable. Interacts with RASGRF2.

Subcellular location

Cytoplasm. Ref.6

Tissue specificity

Heart, brain, lung, skeletal muscle, and kidney.

Domain

Contains at least two actin-binding sites, one in the headpiece domain and one in the amino-terminal portion.

Consists of a large core fragment, the amino-terminal portion, and a small headpiece, the C-terminal portion. The headpiece can bind but cannot bundle actin filaments.

Post-translational modification

Actin-bundling activity is abolished upon phosphorylation by cAMP-dependent protein kinase.

The N-terminus is blocked.

Sequence similarities

Belongs to the villin/gelsolin family.

Contains 1 HP (headpiece) domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   DomainRepeat
   LigandActin-binding
   Molecular functionActin capping
   PTMDisulfide bond
Phosphoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processactin filament bundle formation Ref.2

Traceable author statement. Source: UniProtKB

barbed-end actin filament capping

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentactin cytoskeleton Ref.1

Traceable author statement. Source: UniProtKB

   Molecular functionactin binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: Q08495-1)

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.
Isoform Short (identifier: Q08495-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 405405Dematin
PRO_0000218755

Regions

Domain337 – 40569HP
Region224 – 30885Interaction with RASGRF2
Compositional bias216 – 2227Poly-Glu

Amino acid modifications

Modified residue101Phosphothreonine Ref.7
Modified residue141Phosphoserine Ref.7
Modified residue161Phosphoserine Ref.7
Modified residue221Phosphoserine Ref.7
Modified residue261Phosphoserine Ref.7
Modified residue281Phosphoserine Ref.7
Modified residue871Phosphoserine By similarity
Modified residue911Phosphothreonine By similarity
Modified residue921Phosphoserine Ref.7
Modified residue961Phosphoserine Ref.7
Modified residue1051Phosphoserine Ref.7
Modified residue1561Phosphoserine Ref.7
Modified residue2261Phosphoserine Ref.7 Ref.8
Modified residue2891Phosphoserine Ref.7
Modified residue3331Phosphoserine Ref.7
Modified residue3721Phosphoserine Ref.7
Modified residue4031Phosphoserine; by PKA

Natural variations

Alternative sequence320 – 34122Missing in isoform Short.
VSP_004189

Experimental info

Sequence conflict811S → Q in AAA58438. Ref.1
Sequence conflict811S → Q in AAC50223. Ref.2
Sequence conflict2921A → R in AAA58438. Ref.1
Sequence conflict2921A → R in AAC50223. Ref.2
Sequence conflict3471M → V in AAA58438. Ref.1
Sequence conflict3801F → S in AAA58438. Ref.1

Secondary structure

.............. 405
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified August 30, 2002. Version 3.
Checksum: 77D6372E5B16EFF4

FASTA40545,514
        10         20         30         40         50         60 
MERLQKQPLT SPGSVSPSRD SSVPGSPSSI VAKMDNQVLG YKDLAAIPKD KAILDIERPD 

        70         80         90        100        110        120 
LMIYEPHFTY SLLEHVELPR SRERSLSPKS TSPPPSPEVW ADSRSPGIIS QASAPRTTGT 

       130        140        150        160        170        180 
PRTSLPHFHH PETSRPDSNI YKKPPIYKQR ESVGGSPQTK HLIEDLIIES SKFPAAQPPD 

       190        200        210        220        230        240 
PNQPAKIETD YWPCPPSLAV VETEWRKRKA SRRGAEEEEE EEDDDSGEEM KALRERQREE 

       250        260        270        280        290        300 
LSKVTSNLGK MILKEEMEKS LPIRRKTRSL PDRTPFHTSL HQGTSKSSSL PAYGRTTLSR 

       310        320        330        340        350        360 
LQSTEFSPSG SETGSPGLQN GEGQRGRMDR GNSLPCVLEQ KIYPYEMLVV TNKGRTKLPP 

       370        380        390        400 
GVDRMRLERH LSAEDFSRVF AMSPEEFGKL ALWKRNELKK KASLF 

« Hide

Isoform Short.

Checksum: 3C46AB7704507B6E
Show »

FASTA38343,088

References

« Hide 'large scale' references
[1]"Cloning of human erythroid dematin reveals another member of the villin family."
Rana A.P., Ruff P., Maalouf G.J., Speicher D.W., Chishti A.H.
Proc. Natl. Acad. Sci. U.S.A. 90:6651-6655(1993) [PubMed: 8341682] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), PARTIAL PROTEIN SEQUENCE.
Tissue: Reticulocyte.
[2]"Isoform cloning, actin binding, and chromosomal localization of human erythroid dematin, a member of the villin superfamily."
Azim A.C., Knoll J.H.M., Beggs A.H., Chishti A.H.
J. Biol. Chem. 270:17407-17413(1995) [PubMed: 7615546] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), PHOSPHORYLATION BY CAPK, SUBUNIT, ALTERNATIVE SPLICING.
Tissue: Reticulocyte.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS LONG AND SHORT).
Tissue: Amygdala and Kidney.
[4]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS LONG AND SHORT).
Tissue: Brain and Liver.
[6]"Dematin interacts with the Ras-guanine nucleotide exchange factor Ras-GRF2 and modulates mitogen-activated protein kinase pathways."
Lutchman M., Kim A.C., Cheng L., Whitehead I.P., Oh S.S., Hanspal M., Boukharov A.A., Hanada T., Chishti A.H.
Eur. J. Biochem. 269:638-649(2002) [PubMed: 11856323] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RASGRF2, SUBCELLULAR LOCATION.
[7]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-10; SER-14; SER-16; SER-22; SER-26; SER-28; SER-92; SER-96; SER-105; SER-156; SER-226; SER-289; SER-333 AND SER-372, MASS SPECTROMETRY.
Tissue: Platelet.
[8]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed: 18318008] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, MASS SPECTROMETRY.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

L19713 mRNA. Translation: AAA58438.1.
U28389 mRNA. Translation: AAC50223.1.
AK055842 mRNA. Translation: BAG51582.1.
AK289650 mRNA. Translation: BAF82339.1.
BT007396 mRNA. Translation: AAP36060.1.
BC006318 mRNA. Translation: AAH06318.1.
BC017445 mRNA. Translation: AAH17445.1.
BC052805 mRNA. Translation: AAH52805.1.
IPIIPI00292290.
IPI00796556.
PIRA48222.
I39062.
RefSeqNP_001107607.1.
NP_001107608.1.
NP_001107609.1.
NP_001107610.1.
NP_001969.2.
UniGeneHs.106124
Hs.186350

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1QZPNMR-A342-405[»]
1ZV6NMR-A342-405[»]
ModBaseSearch...

Protein-protein interaction databases

IntActQ08495. 4 interactions.

PTM databases

PhosphoSiteQ08495.

Proteomic databases

PRIDEQ08495.

Genome annotation databases

EnsemblENSG00000158856. Homo sapiens. [Contig view]
GeneID2039.
KEGGhsa:2039.

Organism-specific databases

GeneCardsGC08P021967.
H-InvDBHIX0007358.
HGNCHGNC:3382. EPB49.
MIM125305. gene.
PharmGKBPA27815.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ08495.
OMAQ08495. PSYGRTT.

Gene expression databases

ArrayExpressQ08495.
BgeeQ08495.
CleanExHS_EPB49.
GermOnlineENSG00000158856. Homo sapiens.

Family and domain databases

InterProIPR003128. Villin_headpiece.
[Graphical view]
Gene3DG3DSA:1.10.950.10. VHP. 1 hit.
PfamPF02209. VHP. 1 hit.
[Graphical view]
SMARTSM00153. VHP. 1 hit.
[Graphical view]
PROSITEPS51089. HP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio8281.
SOURCESearch...

Entry information

Entry nameDEMA_HUMAN
AccessionPrimary (citable) accession number: Q08495
Secondary accession number(s): A8K0T5 expand/collapse secondary AC list , B3KP70, Q13215, Q9BRE3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: August 30, 2002
Last modified: June 16, 2009
This is version 100 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents