Full text data of DAAM1
DAAM1
(KIAA0666)
[Confidence: high (present in two of the MS resources)]
Disheveled-associated activator of morphogenesis 1
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Disheveled-associated activator of morphogenesis 1
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00337800
IPI00337800 Splice isoform 1 of Q9Y4D1 Disheveled associated activator of morphogenesis 1 Splice isoform 1 of Q9Y4D1 Disheveled associated activator of morphogenesis 1 membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 5 3 2 2 n/a n/a n/a n/a 2 n/a not mentioned splice isoforms 1 and 2 found at its expected molecular weight found at molecular weight
IPI00337800 Splice isoform 1 of Q9Y4D1 Disheveled associated activator of morphogenesis 1 Splice isoform 1 of Q9Y4D1 Disheveled associated activator of morphogenesis 1 membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 5 3 2 2 n/a n/a n/a n/a 2 n/a not mentioned splice isoforms 1 and 2 found at its expected molecular weight found at molecular weight
Comments
Isoform Q9Y4D1-2 was detected.
Isoform Q9Y4D1-2 was detected.
UniProt
Q9Y4D1
ID DAAM1_HUMAN Reviewed; 1078 AA.
AC Q9Y4D1; Q86U34; Q8N1Z8; Q8TB39;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 15-AUG-2003, sequence version 2.
DT 22-JAN-2014, entry version 120.
DE RecName: Full=Disheveled-associated activator of morphogenesis 1;
GN Name=DAAM1; Synonyms=KIAA0666;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X.
RT The complete sequences of 100 new cDNA clones from brain which can
RT code for large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
RA Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
RA Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
RA Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
RA Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
RA Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
RA Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
RA Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
RA Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
RA Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
RA Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
RA Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
RA Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
RA Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
RA Quetier F., Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta, and Uterus;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-497 (ISOFORM 1).
RC TISSUE=Fetal brain;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 706-1078 (ISOFORM 3).
RC TISSUE=Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP CHARACTERIZATION.
RX PubMed=11779461; DOI=10.1016/S0092-8674(01)00614-6;
RA Habas R., Kato Y., He X.;
RT "Wnt/Frizzled activation of Rho regulates vertebrate gastrulation and
RT requires a novel Formin homology protein Daam1.";
RL Cell 107:843-854(2001).
RN [7]
RP FUNCTION, INTERACTION WITH ABL1; BTK; CDC42; CIP4; ENDOPHILIN; FNBP1;
RP FNBP1L; RHOA; SPECTRIN AND SRC, AND SUBCELLULAR LOCATION.
RX PubMed=16630611; DOI=10.1016/j.yexcr.2006.03.013;
RA Aspenstroem P., Richnau N., Johansson A.-S.;
RT "The diaphanous-related formin DAAM1 collaborates with the Rho GTPases
RT RhoA and Cdc42, CIP4 and Src in regulating cell morphogenesis and
RT actin dynamics.";
RL Exp. Cell Res. 312:2180-2194(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 596-1078, SUBUNIT,
RP MUTAGENESIS OF ILE-698, AND FUNCTION.
RX PubMed=17482208; DOI=10.1016/j.jmb.2007.04.002;
RA Lu J., Meng W., Poy F., Maiti S., Goode B.L., Eck M.J.;
RT "Structure of the FH2 domain of Daam1: implications for formin
RT regulation of actin assembly.";
RL J. Mol. Biol. 369:1258-1269(2007).
CC -!- FUNCTION: Binds to disheveled (Dvl) and Rho, and mediates Wnt-
CC induced Dvl-Rho complex formation. May play a role as a
CC scaffolding protein to recruit Rho-GDP and Rho-GEF, thereby
CC enhancing Rho-GTP formation. Can direct nucleation and elongation
CC of new actin filaments.
CC -!- SUBUNIT: Homodimer. Interacts with CIP4, FNBP1 and FNBP1L.
CC Interacts with the SH3 domains of Abl, BTK, endophilin, spectrin
CC and SRC. Binds specifically to GTP-bound CDC42 and RHOA.
CC -!- INTERACTION:
CC Self; NbExp=2; IntAct=EBI-2817289, EBI-2817289;
CC Q5T0N5:FNBP1L; NbExp=2; IntAct=EBI-2817289, EBI-714058;
CC P61586:RHOA; NbExp=4; IntAct=EBI-2817289, EBI-446668;
CC P00523:SRC (xeno); NbExp=3; IntAct=EBI-2817289, EBI-848039;
CC Q15642-2:TRIP10; NbExp=2; IntAct=EBI-2817289, EBI-6550597;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Perinuclear.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9Y4D1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y4D1-2; Sequence=VSP_008000;
CC Name=3;
CC IsoId=Q9Y4D1-3; Sequence=VSP_008001, VSP_008002, VSP_008003;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined.
CC -!- DOMAIN: The C-terminal DAD domain may participate in
CC intramolecular interactions with the N-terminus.
CC -!- DOMAIN: The DAD domain regulates activation via by an
CC autoinhibitory interaction with the GBD/FH3 domain. This
CC autoinhibition is released upon competitive binding of an
CC activated GTPase. The release of DAD allows the FH2 domain to then
CC nucleate and elongate nonbranched actin filaments (By similarity).
CC -!- SIMILARITY: Belongs to the formin homology family.
CC -!- SIMILARITY: Contains 1 DAD (diaphanous autoregulatory) domain.
CC -!- SIMILARITY: Contains 1 FH1 (formin homology 1) domain.
CC -!- SIMILARITY: Contains 1 FH2 (formin homology 2) domain.
CC -!- SIMILARITY: Contains 1 GBD/FH3 (Rho GTPase-binding/formin homology
CC 3) domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA31641.1; Type=Erroneous initiation;
CC Sequence=BAC04230.1; Type=Erroneous initiation;
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DR EMBL; AB014566; BAA31641.1; ALT_INIT; mRNA.
DR EMBL; AL133502; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC024781; AAH24781.1; -; mRNA.
DR EMBL; BC038428; AAH38428.1; -; mRNA.
DR EMBL; BC064999; AAH64999.1; -; mRNA.
DR EMBL; BX247986; CAD62320.1; -; mRNA.
DR EMBL; AK093813; BAC04230.1; ALT_INIT; mRNA.
DR RefSeq; NP_001257449.1; NM_001270520.1.
DR RefSeq; NP_055807.1; NM_014992.2.
DR RefSeq; XP_005267487.1; XM_005267430.1.
DR RefSeq; XP_005267488.1; XM_005267431.1.
DR UniGene; Hs.19156; -.
DR PDB; 2J1D; X-ray; 2.55 A; G=596-1078.
DR PDB; 2Z6E; X-ray; 2.80 A; A/B/C/D=594-1012.
DR PDBsum; 2J1D; -.
DR PDBsum; 2Z6E; -.
DR ProteinModelPortal; Q9Y4D1; -.
DR SMR; Q9Y4D1; 55-446, 593-1048.
DR DIP; DIP-29641N; -.
DR IntAct; Q9Y4D1; 21.
DR MINT; MINT-1180756; -.
DR STRING; 9606.ENSP00000247170; -.
DR PhosphoSite; Q9Y4D1; -.
DR DMDM; 34098767; -.
DR PaxDb; Q9Y4D1; -.
DR PRIDE; Q9Y4D1; -.
DR Ensembl; ENST00000351081; ENSP00000247170; ENSG00000100592.
DR Ensembl; ENST00000360909; ENSP00000354162; ENSG00000100592.
DR Ensembl; ENST00000395125; ENSP00000378557; ENSG00000100592.
DR GeneID; 23002; -.
DR KEGG; hsa:23002; -.
DR UCSC; uc031qou.1; human.
DR CTD; 23002; -.
DR GeneCards; GC14P059655; -.
DR H-InvDB; HIX0011701; -.
DR HGNC; HGNC:18142; DAAM1.
DR HPA; HPA026605; -.
DR MIM; 606626; gene.
DR neXtProt; NX_Q9Y4D1; -.
DR PharmGKB; PA27129; -.
DR eggNOG; NOG149898; -.
DR HOGENOM; HOG000237318; -.
DR HOVERGEN; HBG101333; -.
DR InParanoid; Q9Y4D1; -.
DR KO; K04512; -.
DR OMA; SAMAPRK; -.
DR OrthoDB; EOG7B8S37; -.
DR PhylomeDB; Q9Y4D1; -.
DR SignaLink; Q9Y4D1; -.
DR ChiTaRS; DAAM1; human.
DR EvolutionaryTrace; Q9Y4D1; -.
DR GeneWiki; DAAM1; -.
DR GenomeRNAi; 23002; -.
DR NextBio; 43908; -.
DR PRO; PR:Q9Y4D1; -.
DR ArrayExpress; Q9Y4D1; -.
DR Bgee; Q9Y4D1; -.
DR CleanEx; HS_DAAM1; -.
DR Genevestigator; Q9Y4D1; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0001725; C:stress fiber; IDA:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR027650; DAAM1/DAAM2.
DR InterPro; IPR014767; Diaphanous_autoregulatory.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR010472; FH3_dom.
DR InterPro; IPR010473; GTPase-bd.
DR InterPro; IPR014768; GTPase-bd/formin_homology_3.
DR PANTHER; PTHR23213:SF20; PTHR23213:SF20; 1.
DR Pfam; PF06367; Drf_FH3; 1.
DR Pfam; PF06371; Drf_GBD; 1.
DR Pfam; PF02181; FH2; 1.
DR SMART; SM00498; FH2; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS51231; DAD; 1.
DR PROSITE; PS51444; FH2; 1.
DR PROSITE; PS51232; GBD_FH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Alternative splicing; Coiled coil;
KW Complete proteome; Cytoplasm; Reference proteome.
FT CHAIN 1 1078 Disheveled-associated activator of
FT morphogenesis 1.
FT /FTId=PRO_0000194907.
FT DOMAIN 45 420 GBD/FH3.
FT DOMAIN 528 599 FH1.
FT DOMAIN 600 1009 FH2.
FT DOMAIN 1027 1058 DAD.
FT REGION 693 702 Actin-binding.
FT COILED 437 526 Potential.
FT COMPBIAS 528 593 Pro-rich.
FT VAR_SEQ 656 665 Missing (in isoform 2).
FT /FTId=VSP_008000.
FT VAR_SEQ 788 818 Missing (in isoform 3).
FT /FTId=VSP_008001.
FT VAR_SEQ 888 916 NMTELDKEISTLRSGLKAVETELEYQKSQ -> KSWNIRSL
FT SPHSPEISLCLLSASSSQ (in isoform 3).
FT /FTId=VSP_008002.
FT VAR_SEQ 917 1078 Missing (in isoform 3).
FT /FTId=VSP_008003.
FT MUTAGEN 698 698 I->A: Abolishes actin-binding.
FT CONFLICT 940 940 S -> F (in Ref. 3; AAH24781).
FT HELIX 620 622
FT STRAND 624 626
FT HELIX 627 630
FT HELIX 633 635
FT HELIX 636 639
FT HELIX 642 648
FT STRAND 650 652
FT HELIX 690 703
FT HELIX 707 715
FT HELIX 725 733
FT HELIX 738 745
FT TURN 746 749
FT HELIX 751 753
FT HELIX 756 765
FT HELIX 770 806
FT HELIX 808 824
FT STRAND 827 829
FT HELIX 837 845
FT HELIX 856 867
FT HELIX 869 873
FT HELIX 874 877
FT TURN 878 880
FT HELIX 881 885
FT HELIX 889 914
FT HELIX 924 959
FT HELIX 969 994
FT HELIX 996 999
FT HELIX 1001 1022
SQ SEQUENCE 1078 AA; 123473 MW; E82D9892390254B6 CRC64;
MAPRKRGGRG ISFIFCCFRN NDHPEITYRL RNDSNFALQT MEPALPMPPV EELDVMFSEL
VDELDLTDKH REAMFALPAE KKWQIYCSKK KDQEENKGAT SWPEFYIDQL NSMAARKSLL
ALEKEEEEER SKTIESLKTA LRTKPMRFVT RFIDLDGLSC ILNFLKTMDY ETSESRIHTS
LIGCIKALMN NSQGRAHVLA HSESINVIAQ SLSTENIKTK VAVLEILGAV CLVPGGHKKV
LQAMLHYQKY ASERTRFQTL INDLDKSTGR YRDEVSLKTA IMSFINAVLS QGAGVESLDF
RLHLRYEFLM LGIQPVIDKL REHENSTLDR HLDFFEMLRN EDELEFAKRF ELVHIDTKSA
TQMFELTRKR LTHSEAYPHF MSILHHCLQM PYKRSGNTVQ YWLLLDRIIQ QIVIQNDKGQ
DPDSTPLENF NIKNVVRMLV NENEVKQWKE QAEKMRKEHN ELQQKLEKKE RECDAKTQEK
EEMMQTLNKM KEKLEKETTE HKQVKQQVAD LTAQLHELSR RAVCASIPGG PSPGAPGGPF
PSSVPGSLLP PPPPPPLPGG MLPPPPPPLP PGGPPPPPGP PPLGAIMPPP GAPMGLALKK
KSIPQPTNAL KSFNWSKLPE NKLEGTVWTE IDDTKVFKIL DLEDLERTFS AYQRQQDFFV
NSNSKQKEAD AIDDTLSSKL KVKELSVIDG RRAQNCNILL SRLKLSNDEI KRAILTMDEQ
EDLPKDMLEQ LLKFVPEKSD IDLLEEHKHE LDRMAKADRF LFEMSRINHY QQRLQSLYFK
KKFAERVAEV KPKVEAIRSG SEEVFRSGAL KQLLEVVLAF GNYMNKGQRG NAYGFKISSL
NKIADTKSSI DKNITLLHYL ITIVENKYPS VLNLNEELRD IPQAAKVNMT ELDKEISTLR
SGLKAVETEL EYQKSQPPQP GDKFVSVVSQ FITVASFSFS DVEDLLAEAK DLFTKAVKHF
GEEAGKIQPD EFFGIFDQFL QAVSEAKQEN ENMRKKKEEE ERRARMEAQL KEQRERERKM
RKAKENSEES GEFDDLVSAL RSGEVFDKDL SKLKRNRKRI TNQMTDSSRE RPITKLNF
//
ID DAAM1_HUMAN Reviewed; 1078 AA.
AC Q9Y4D1; Q86U34; Q8N1Z8; Q8TB39;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 15-AUG-2003, sequence version 2.
DT 22-JAN-2014, entry version 120.
DE RecName: Full=Disheveled-associated activator of morphogenesis 1;
GN Name=DAAM1; Synonyms=KIAA0666;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X.
RT The complete sequences of 100 new cDNA clones from brain which can
RT code for large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
RA Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
RA Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
RA Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
RA Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
RA Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
RA Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
RA Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
RA Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
RA Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
RA Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
RA Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
RA Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
RA Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
RA Quetier F., Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta, and Uterus;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-497 (ISOFORM 1).
RC TISSUE=Fetal brain;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 706-1078 (ISOFORM 3).
RC TISSUE=Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP CHARACTERIZATION.
RX PubMed=11779461; DOI=10.1016/S0092-8674(01)00614-6;
RA Habas R., Kato Y., He X.;
RT "Wnt/Frizzled activation of Rho regulates vertebrate gastrulation and
RT requires a novel Formin homology protein Daam1.";
RL Cell 107:843-854(2001).
RN [7]
RP FUNCTION, INTERACTION WITH ABL1; BTK; CDC42; CIP4; ENDOPHILIN; FNBP1;
RP FNBP1L; RHOA; SPECTRIN AND SRC, AND SUBCELLULAR LOCATION.
RX PubMed=16630611; DOI=10.1016/j.yexcr.2006.03.013;
RA Aspenstroem P., Richnau N., Johansson A.-S.;
RT "The diaphanous-related formin DAAM1 collaborates with the Rho GTPases
RT RhoA and Cdc42, CIP4 and Src in regulating cell morphogenesis and
RT actin dynamics.";
RL Exp. Cell Res. 312:2180-2194(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 596-1078, SUBUNIT,
RP MUTAGENESIS OF ILE-698, AND FUNCTION.
RX PubMed=17482208; DOI=10.1016/j.jmb.2007.04.002;
RA Lu J., Meng W., Poy F., Maiti S., Goode B.L., Eck M.J.;
RT "Structure of the FH2 domain of Daam1: implications for formin
RT regulation of actin assembly.";
RL J. Mol. Biol. 369:1258-1269(2007).
CC -!- FUNCTION: Binds to disheveled (Dvl) and Rho, and mediates Wnt-
CC induced Dvl-Rho complex formation. May play a role as a
CC scaffolding protein to recruit Rho-GDP and Rho-GEF, thereby
CC enhancing Rho-GTP formation. Can direct nucleation and elongation
CC of new actin filaments.
CC -!- SUBUNIT: Homodimer. Interacts with CIP4, FNBP1 and FNBP1L.
CC Interacts with the SH3 domains of Abl, BTK, endophilin, spectrin
CC and SRC. Binds specifically to GTP-bound CDC42 and RHOA.
CC -!- INTERACTION:
CC Self; NbExp=2; IntAct=EBI-2817289, EBI-2817289;
CC Q5T0N5:FNBP1L; NbExp=2; IntAct=EBI-2817289, EBI-714058;
CC P61586:RHOA; NbExp=4; IntAct=EBI-2817289, EBI-446668;
CC P00523:SRC (xeno); NbExp=3; IntAct=EBI-2817289, EBI-848039;
CC Q15642-2:TRIP10; NbExp=2; IntAct=EBI-2817289, EBI-6550597;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Perinuclear.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9Y4D1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y4D1-2; Sequence=VSP_008000;
CC Name=3;
CC IsoId=Q9Y4D1-3; Sequence=VSP_008001, VSP_008002, VSP_008003;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined.
CC -!- DOMAIN: The C-terminal DAD domain may participate in
CC intramolecular interactions with the N-terminus.
CC -!- DOMAIN: The DAD domain regulates activation via by an
CC autoinhibitory interaction with the GBD/FH3 domain. This
CC autoinhibition is released upon competitive binding of an
CC activated GTPase. The release of DAD allows the FH2 domain to then
CC nucleate and elongate nonbranched actin filaments (By similarity).
CC -!- SIMILARITY: Belongs to the formin homology family.
CC -!- SIMILARITY: Contains 1 DAD (diaphanous autoregulatory) domain.
CC -!- SIMILARITY: Contains 1 FH1 (formin homology 1) domain.
CC -!- SIMILARITY: Contains 1 FH2 (formin homology 2) domain.
CC -!- SIMILARITY: Contains 1 GBD/FH3 (Rho GTPase-binding/formin homology
CC 3) domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA31641.1; Type=Erroneous initiation;
CC Sequence=BAC04230.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
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DR EMBL; AB014566; BAA31641.1; ALT_INIT; mRNA.
DR EMBL; AL133502; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC024781; AAH24781.1; -; mRNA.
DR EMBL; BC038428; AAH38428.1; -; mRNA.
DR EMBL; BC064999; AAH64999.1; -; mRNA.
DR EMBL; BX247986; CAD62320.1; -; mRNA.
DR EMBL; AK093813; BAC04230.1; ALT_INIT; mRNA.
DR RefSeq; NP_001257449.1; NM_001270520.1.
DR RefSeq; NP_055807.1; NM_014992.2.
DR RefSeq; XP_005267487.1; XM_005267430.1.
DR RefSeq; XP_005267488.1; XM_005267431.1.
DR UniGene; Hs.19156; -.
DR PDB; 2J1D; X-ray; 2.55 A; G=596-1078.
DR PDB; 2Z6E; X-ray; 2.80 A; A/B/C/D=594-1012.
DR PDBsum; 2J1D; -.
DR PDBsum; 2Z6E; -.
DR ProteinModelPortal; Q9Y4D1; -.
DR SMR; Q9Y4D1; 55-446, 593-1048.
DR DIP; DIP-29641N; -.
DR IntAct; Q9Y4D1; 21.
DR MINT; MINT-1180756; -.
DR STRING; 9606.ENSP00000247170; -.
DR PhosphoSite; Q9Y4D1; -.
DR DMDM; 34098767; -.
DR PaxDb; Q9Y4D1; -.
DR PRIDE; Q9Y4D1; -.
DR Ensembl; ENST00000351081; ENSP00000247170; ENSG00000100592.
DR Ensembl; ENST00000360909; ENSP00000354162; ENSG00000100592.
DR Ensembl; ENST00000395125; ENSP00000378557; ENSG00000100592.
DR GeneID; 23002; -.
DR KEGG; hsa:23002; -.
DR UCSC; uc031qou.1; human.
DR CTD; 23002; -.
DR GeneCards; GC14P059655; -.
DR H-InvDB; HIX0011701; -.
DR HGNC; HGNC:18142; DAAM1.
DR HPA; HPA026605; -.
DR MIM; 606626; gene.
DR neXtProt; NX_Q9Y4D1; -.
DR PharmGKB; PA27129; -.
DR eggNOG; NOG149898; -.
DR HOGENOM; HOG000237318; -.
DR HOVERGEN; HBG101333; -.
DR InParanoid; Q9Y4D1; -.
DR KO; K04512; -.
DR OMA; SAMAPRK; -.
DR OrthoDB; EOG7B8S37; -.
DR PhylomeDB; Q9Y4D1; -.
DR SignaLink; Q9Y4D1; -.
DR ChiTaRS; DAAM1; human.
DR EvolutionaryTrace; Q9Y4D1; -.
DR GeneWiki; DAAM1; -.
DR GenomeRNAi; 23002; -.
DR NextBio; 43908; -.
DR PRO; PR:Q9Y4D1; -.
DR ArrayExpress; Q9Y4D1; -.
DR Bgee; Q9Y4D1; -.
DR CleanEx; HS_DAAM1; -.
DR Genevestigator; Q9Y4D1; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0001725; C:stress fiber; IDA:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR027650; DAAM1/DAAM2.
DR InterPro; IPR014767; Diaphanous_autoregulatory.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR010472; FH3_dom.
DR InterPro; IPR010473; GTPase-bd.
DR InterPro; IPR014768; GTPase-bd/formin_homology_3.
DR PANTHER; PTHR23213:SF20; PTHR23213:SF20; 1.
DR Pfam; PF06367; Drf_FH3; 1.
DR Pfam; PF06371; Drf_GBD; 1.
DR Pfam; PF02181; FH2; 1.
DR SMART; SM00498; FH2; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS51231; DAD; 1.
DR PROSITE; PS51444; FH2; 1.
DR PROSITE; PS51232; GBD_FH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Alternative splicing; Coiled coil;
KW Complete proteome; Cytoplasm; Reference proteome.
FT CHAIN 1 1078 Disheveled-associated activator of
FT morphogenesis 1.
FT /FTId=PRO_0000194907.
FT DOMAIN 45 420 GBD/FH3.
FT DOMAIN 528 599 FH1.
FT DOMAIN 600 1009 FH2.
FT DOMAIN 1027 1058 DAD.
FT REGION 693 702 Actin-binding.
FT COILED 437 526 Potential.
FT COMPBIAS 528 593 Pro-rich.
FT VAR_SEQ 656 665 Missing (in isoform 2).
FT /FTId=VSP_008000.
FT VAR_SEQ 788 818 Missing (in isoform 3).
FT /FTId=VSP_008001.
FT VAR_SEQ 888 916 NMTELDKEISTLRSGLKAVETELEYQKSQ -> KSWNIRSL
FT SPHSPEISLCLLSASSSQ (in isoform 3).
FT /FTId=VSP_008002.
FT VAR_SEQ 917 1078 Missing (in isoform 3).
FT /FTId=VSP_008003.
FT MUTAGEN 698 698 I->A: Abolishes actin-binding.
FT CONFLICT 940 940 S -> F (in Ref. 3; AAH24781).
FT HELIX 620 622
FT STRAND 624 626
FT HELIX 627 630
FT HELIX 633 635
FT HELIX 636 639
FT HELIX 642 648
FT STRAND 650 652
FT HELIX 690 703
FT HELIX 707 715
FT HELIX 725 733
FT HELIX 738 745
FT TURN 746 749
FT HELIX 751 753
FT HELIX 756 765
FT HELIX 770 806
FT HELIX 808 824
FT STRAND 827 829
FT HELIX 837 845
FT HELIX 856 867
FT HELIX 869 873
FT HELIX 874 877
FT TURN 878 880
FT HELIX 881 885
FT HELIX 889 914
FT HELIX 924 959
FT HELIX 969 994
FT HELIX 996 999
FT HELIX 1001 1022
SQ SEQUENCE 1078 AA; 123473 MW; E82D9892390254B6 CRC64;
MAPRKRGGRG ISFIFCCFRN NDHPEITYRL RNDSNFALQT MEPALPMPPV EELDVMFSEL
VDELDLTDKH REAMFALPAE KKWQIYCSKK KDQEENKGAT SWPEFYIDQL NSMAARKSLL
ALEKEEEEER SKTIESLKTA LRTKPMRFVT RFIDLDGLSC ILNFLKTMDY ETSESRIHTS
LIGCIKALMN NSQGRAHVLA HSESINVIAQ SLSTENIKTK VAVLEILGAV CLVPGGHKKV
LQAMLHYQKY ASERTRFQTL INDLDKSTGR YRDEVSLKTA IMSFINAVLS QGAGVESLDF
RLHLRYEFLM LGIQPVIDKL REHENSTLDR HLDFFEMLRN EDELEFAKRF ELVHIDTKSA
TQMFELTRKR LTHSEAYPHF MSILHHCLQM PYKRSGNTVQ YWLLLDRIIQ QIVIQNDKGQ
DPDSTPLENF NIKNVVRMLV NENEVKQWKE QAEKMRKEHN ELQQKLEKKE RECDAKTQEK
EEMMQTLNKM KEKLEKETTE HKQVKQQVAD LTAQLHELSR RAVCASIPGG PSPGAPGGPF
PSSVPGSLLP PPPPPPLPGG MLPPPPPPLP PGGPPPPPGP PPLGAIMPPP GAPMGLALKK
KSIPQPTNAL KSFNWSKLPE NKLEGTVWTE IDDTKVFKIL DLEDLERTFS AYQRQQDFFV
NSNSKQKEAD AIDDTLSSKL KVKELSVIDG RRAQNCNILL SRLKLSNDEI KRAILTMDEQ
EDLPKDMLEQ LLKFVPEKSD IDLLEEHKHE LDRMAKADRF LFEMSRINHY QQRLQSLYFK
KKFAERVAEV KPKVEAIRSG SEEVFRSGAL KQLLEVVLAF GNYMNKGQRG NAYGFKISSL
NKIADTKSSI DKNITLLHYL ITIVENKYPS VLNLNEELRD IPQAAKVNMT ELDKEISTLR
SGLKAVETEL EYQKSQPPQP GDKFVSVVSQ FITVASFSFS DVEDLLAEAK DLFTKAVKHF
GEEAGKIQPD EFFGIFDQFL QAVSEAKQEN ENMRKKKEEE ERRARMEAQL KEQRERERKM
RKAKENSEES GEFDDLVSAL RSGEVFDKDL SKLKRNRKRI TNQMTDSSRE RPITKLNF
//
MIM
606626
*RECORD*
*FIELD* NO
606626
*FIELD* TI
*606626 DISHEVELLED-ASSOCIATED ACTIVATOR OF MORPHOGENESIS 1; DAAM1
;;KIAA0666
*FIELD* TX
read more
CLONING
By screening size-fractionated brain cDNA libraries for cDNAs with the
potential to encode proteins larger than 50 kD, Ishikawa et al. (1998)
identified a cDNA which they designated KIAA0666. KIAA0666 encodes a
1,085-amino acid protein predicted to function in cell division. It is
68% identical to the KIAA0381 protein (DAAM2; 606627). RT-PCR analysis
detected expression of KIAA0666 in all tissues tested.
Habas et al. (2001) identified a novel formin (see FMN1; 136535)
homology (FH) protein that they named DAAM1. DAAM1 is a widely expressed
protein that contains 1,078 amino acids and is identical to the KIAA0666
protein. Like other FH proteins, DAAM1 contains a central proline-rich
FH1 domain and a more C-terminal FH2 domain.
GENE FUNCTION
Wnt (see 164975) signaling via the frizzled receptor (Fz; see 600667)
controls cell polarity and movement during development. Habas et al.
(2001) reported that in human cells and during Xenopus embryogenesis,
Wnt/Fz signaling activated the small GTPase Rho (165390), a key
regulator of cytoskeleton architecture. Wnt/Fz activation of Rho
required the cytoplasmic protein dishevelled (DVL; see 601365) and
DAAM1. DAAM1 bound to both DVL and Rho and mediated Wnt-induced DVL-Rho
complex formation. Inhibition or depletion of DAAM1 prevented Wnt/Fz
activation of Rho and of Xenopus gastrulation, but did not prevent
activation of beta-catenin (116806) signaling.
Liu et al. (2008) showed that human DAAM1 was autoinhibited by an
intramolecular interaction between its N-terminal GTPase domain, which
includes an autoinhibitory domain, and its C-terminal autoregulatory
domain. Interaction of DAAM1 with DVL disrupted this autoinhibitory
interaction, resulting in DAAM1 activation. Mutations within or removal
of the autoregulatory domain converted DAAM1 into an active protein that
could induce Rho activation. Liu et al. (2008) also demonstrated that
Dvl synergized with Daam1 to regulate gastrulation during Xenopus
embryogenesis.
MAPPING
By radiation hybrid analysis, Ishikawa et al. (1998) mapped the DAAM1
gene to chromosome 14.
*FIELD* RF
1. Habas, R.; Kato, Y.; He, X.: Wnt/Frizzled activation of Rho regulates
vertebrate gastrulation and requires a novel Formin homology protein
Daam1. Cell 107: 843-854, 2001.
2. Ishikawa, K.; Nagase, T.; Suyama, M.; Miyajima, N.; Tanaka, A.;
Kotani, H.; Nomura, N.; Ohara, O.: Prediction of the coding sequences
of unidentified human genes. X. The complete sequences of 100 new
cDNA clones from brain which can code for large proteins in vitro. DNA
Res. 5: 169-176, 1998.
3. Liu, W.; Sato, A.; Khadka, D.; Bharti, R.; Diaz, H.; Runnels, L.
W.; Habas, R.: Mechanism of activation of the Formin protein Daam1. Proc.
Nat. Acad. Sci. 105: 210-215, 2008.
*FIELD* CN
Patricia A. Hartz - updated: 4/18/2008
Matthew B. Gross - updated: 1/23/2002
*FIELD* CD
Stylianos E. Antonarakis: 1/23/2002
*FIELD* ED
wwang: 04/02/2010
alopez: 10/2/2008
mgross: 4/18/2008
terry: 4/18/2008
mgross: 1/23/2002
carol: 1/23/2002
mgross: 1/23/2002
*RECORD*
*FIELD* NO
606626
*FIELD* TI
*606626 DISHEVELLED-ASSOCIATED ACTIVATOR OF MORPHOGENESIS 1; DAAM1
;;KIAA0666
*FIELD* TX
read more
CLONING
By screening size-fractionated brain cDNA libraries for cDNAs with the
potential to encode proteins larger than 50 kD, Ishikawa et al. (1998)
identified a cDNA which they designated KIAA0666. KIAA0666 encodes a
1,085-amino acid protein predicted to function in cell division. It is
68% identical to the KIAA0381 protein (DAAM2; 606627). RT-PCR analysis
detected expression of KIAA0666 in all tissues tested.
Habas et al. (2001) identified a novel formin (see FMN1; 136535)
homology (FH) protein that they named DAAM1. DAAM1 is a widely expressed
protein that contains 1,078 amino acids and is identical to the KIAA0666
protein. Like other FH proteins, DAAM1 contains a central proline-rich
FH1 domain and a more C-terminal FH2 domain.
GENE FUNCTION
Wnt (see 164975) signaling via the frizzled receptor (Fz; see 600667)
controls cell polarity and movement during development. Habas et al.
(2001) reported that in human cells and during Xenopus embryogenesis,
Wnt/Fz signaling activated the small GTPase Rho (165390), a key
regulator of cytoskeleton architecture. Wnt/Fz activation of Rho
required the cytoplasmic protein dishevelled (DVL; see 601365) and
DAAM1. DAAM1 bound to both DVL and Rho and mediated Wnt-induced DVL-Rho
complex formation. Inhibition or depletion of DAAM1 prevented Wnt/Fz
activation of Rho and of Xenopus gastrulation, but did not prevent
activation of beta-catenin (116806) signaling.
Liu et al. (2008) showed that human DAAM1 was autoinhibited by an
intramolecular interaction between its N-terminal GTPase domain, which
includes an autoinhibitory domain, and its C-terminal autoregulatory
domain. Interaction of DAAM1 with DVL disrupted this autoinhibitory
interaction, resulting in DAAM1 activation. Mutations within or removal
of the autoregulatory domain converted DAAM1 into an active protein that
could induce Rho activation. Liu et al. (2008) also demonstrated that
Dvl synergized with Daam1 to regulate gastrulation during Xenopus
embryogenesis.
MAPPING
By radiation hybrid analysis, Ishikawa et al. (1998) mapped the DAAM1
gene to chromosome 14.
*FIELD* RF
1. Habas, R.; Kato, Y.; He, X.: Wnt/Frizzled activation of Rho regulates
vertebrate gastrulation and requires a novel Formin homology protein
Daam1. Cell 107: 843-854, 2001.
2. Ishikawa, K.; Nagase, T.; Suyama, M.; Miyajima, N.; Tanaka, A.;
Kotani, H.; Nomura, N.; Ohara, O.: Prediction of the coding sequences
of unidentified human genes. X. The complete sequences of 100 new
cDNA clones from brain which can code for large proteins in vitro. DNA
Res. 5: 169-176, 1998.
3. Liu, W.; Sato, A.; Khadka, D.; Bharti, R.; Diaz, H.; Runnels, L.
W.; Habas, R.: Mechanism of activation of the Formin protein Daam1. Proc.
Nat. Acad. Sci. 105: 210-215, 2008.
*FIELD* CN
Patricia A. Hartz - updated: 4/18/2008
Matthew B. Gross - updated: 1/23/2002
*FIELD* CD
Stylianos E. Antonarakis: 1/23/2002
*FIELD* ED
wwang: 04/02/2010
alopez: 10/2/2008
mgross: 4/18/2008
terry: 4/18/2008
mgross: 1/23/2002
carol: 1/23/2002
mgross: 1/23/2002