DAAM1_MOUSE
ID DAAM1_MOUSE Reviewed; 1077 AA.
AC Q8BPM0; Q3UHB4; Q6DFY0; Q6TAB8; Q80Y68; Q9CQQ2;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Disheveled-associated activator of morphogenesis 1;
GN Name=Daam1;
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] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=15533824; DOI=10.1016/j.modgep.2004.06.001;
RA Nakaya M.-A., Habas R., Biris K., Dunty W.C. Jr., Kato Y., He X.,
RA Yamaguchi T.P.;
RT "Identification and comparative expression analyses of Daam genes in mouse
RT and Xenopus.";
RL Gene Expr. Patterns 5:97-105(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Eye, Placenta, and Testis;
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 MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 592-1077 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Retina;
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 [4]
RP TISSUE SPECIFICITY.
RX PubMed=15464228; DOI=10.1016/j.devbrainres.2004.07.014;
RA Kida Y., Shiraishi T., Ogura T.;
RT "Identification of chick and mouse Daam1 and Daam2 genes and their
RT expression patterns in the central nervous system.";
RL Brain Res. Dev. Brain Res. 153:143-150(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1029, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, 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 [6]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=26526197; DOI=10.1016/j.ydbio.2015.10.003;
RA Ajima R., Bisson J.A., Helt J.C., Nakaya M.A., Habas R., Tessarollo L.,
RA He X., Morrisey E.E., Yamaguchi T.P., Cohen E.D.;
RT "DAAM1 and DAAM2 are co-required for myocardial maturation and sarcomere
RT assembly.";
RL Dev. Biol. 408:126-139(2015).
CC -!- FUNCTION: Binds to disheveled (Dvl) and Rho, and mediates Wnt-induced
CC Dvl-Rho complex formation. May play a role as a scaffolding protein to
CC recruit Rho-GDP and Rho-GEF, thereby enhancing Rho-GTP formation. Can
CC direct nucleation and elongation of new actin filaments (By
CC similarity). Involved in building functional cilia. Involved in the
CC organization of the subapical actin network in multiciliated epithelial
CC cells (By similarity). Together with DAAM2, required for myocardial
CC maturation and sarcomere assembly (PubMed:26526197).
CC {ECO:0000250|UniProtKB:B0DOB5, ECO:0000250|UniProtKB:Q9Y4D1,
CC ECO:0000269|PubMed:26526197}.
CC -!- SUBUNIT: Interacts with CIP4, FNBP1 and FNBP1L. Interacts with the SH3
CC domains of Abl, BTK, endophilin, spectrin and SRC. Binds specifically
CC to GTP-bound CDC42 and RHOA. Interacts with INTU; INTU mediates the
CC indirect interaction between DAAM1 and NPHP4 (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y4D1}.
CC -!- INTERACTION:
CC Q8BPM0; O15085-2: ARHGEF11; Xeno; NbExp=3; IntAct=EBI-772938, EBI-6169263;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y4D1}.
CC Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000250|UniProtKB:Q9Y4D1}. Note=Perinuclear.
CC {ECO:0000250|UniProtKB:Q9Y4D1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BPM0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BPM0-2; Sequence=VSP_027771;
CC Name=3;
CC IsoId=Q8BPM0-3; Sequence=VSP_027772, VSP_027773;
CC -!- TISSUE SPECIFICITY: In early embryogenesis, expressed in embryonic and
CC extraembryonic ectoderm. In later stages of gastrulation, expressed
CC also in somites and ribs and posterior vertebrae of developing skeletal
CC system. During organogenesis, expressed in CNS, PNS, stomach, liver and
CC limb bud. {ECO:0000269|PubMed:15464228, ECO:0000269|PubMed:15533824}.
CC -!- DEVELOPMENTAL STAGE: Detected throughout the myocardial layer of the
CC heart tube. Not expressed in the myocardium at 9.5 dpc but is present
CC in epicardial cells and the pro-epicardial organ. At 10.5 dpc,
CC expressed in the atrial and ventricular myocardia as well as the inter-
CC ventricular septum. Continues to localize to the atrial and ventricular
CC myocardia at 12.5 dpc as well as the ventricular trabeculae.
CC {ECO:0000269|PubMed:26526197}.
CC -!- DOMAIN: The C-terminal DAD domain may participate in intramolecular
CC interactions with the N-terminus.
CC -!- DOMAIN: The DAD domain regulates activation via by an autoinhibitory
CC interaction with the GBD/FH3 domain. This autoinhibition is released
CC upon competitive binding of an activated GTPase. The release of DAD
CC allows the FH2 domain to then nucleate and elongate nonbranched actin
CC filaments (By similarity). {ECO:0000250|UniProtKB:O08808}.
CC -!- DISRUPTION PHENOTYPE: Conditional knockout mice lacking Daam1 in
CC myocardial cells show cardiomyopathy. Conditional knockout mice lacking
CC Daam1 and Daam2 in myocardial cells show stronger cardiomyopathy.
CC {ECO:0000269|PubMed:26526197}.
CC -!- SIMILARITY: Belongs to the formin homology family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH48856.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY426535; AAR05118.1; -; mRNA.
DR EMBL; AK006902; BAB24785.1; -; mRNA.
DR EMBL; AK018919; BAB31482.1; -; mRNA.
DR EMBL; AK018950; BAB31491.1; -; mRNA.
DR EMBL; AK053785; BAC35522.1; -; mRNA.
DR EMBL; AK147480; BAE27943.1; -; mRNA.
DR EMBL; BC032287; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC048856; AAH48856.1; ALT_INIT; mRNA.
DR EMBL; BC076585; AAH76585.1; -; mRNA.
DR CCDS; CCDS25964.1; -. [Q8BPM0-1]
DR CCDS; CCDS88349.1; -. [Q8BPM0-2]
DR RefSeq; NP_001273381.1; NM_001286452.1. [Q8BPM0-2]
DR RefSeq; NP_080378.2; NM_026102.3. [Q8BPM0-1]
DR RefSeq; NP_766052.2; NM_172464.3. [Q8BPM0-1]
DR RefSeq; XP_006515705.1; XM_006515642.2. [Q8BPM0-1]
DR RefSeq; XP_006515706.1; XM_006515643.3. [Q8BPM0-2]
DR RefSeq; XP_006515707.1; XM_006515644.3. [Q8BPM0-2]
DR AlphaFoldDB; Q8BPM0; -.
DR SMR; Q8BPM0; -.
DR BioGRID; 229018; 16.
DR IntAct; Q8BPM0; 1.
DR STRING; 10090.ENSMUSP00000082406; -.
DR iPTMnet; Q8BPM0; -.
DR PhosphoSitePlus; Q8BPM0; -.
DR SwissPalm; Q8BPM0; -.
DR MaxQB; Q8BPM0; -.
DR PaxDb; Q8BPM0; -.
DR PeptideAtlas; Q8BPM0; -.
DR PRIDE; Q8BPM0; -.
DR ProteomicsDB; 279146; -. [Q8BPM0-1]
DR ProteomicsDB; 279147; -. [Q8BPM0-2]
DR ProteomicsDB; 279148; -. [Q8BPM0-3]
DR Antibodypedia; 11379; 358 antibodies from 30 providers.
DR DNASU; 208846; -.
DR Ensembl; ENSMUST00000085299; ENSMUSP00000082406; ENSMUSG00000034574. [Q8BPM0-1]
DR Ensembl; ENSMUST00000221317; ENSMUSP00000152532; ENSMUSG00000034574. [Q8BPM0-2]
DR Ensembl; ENSMUST00000223272; ENSMUSP00000152564; ENSMUSG00000034574. [Q8BPM0-1]
DR GeneID; 208846; -.
DR KEGG; mmu:208846; -.
DR UCSC; uc007nuw.2; mouse. [Q8BPM0-3]
DR UCSC; uc007nux.2; mouse. [Q8BPM0-1]
DR UCSC; uc007nuz.2; mouse. [Q8BPM0-2]
DR CTD; 23002; -.
DR MGI; MGI:1914596; Daam1.
DR VEuPathDB; HostDB:ENSMUSG00000034574; -.
DR eggNOG; KOG1922; Eukaryota.
DR GeneTree; ENSGT00940000156452; -.
DR HOGENOM; CLU_002356_1_0_1; -.
DR InParanoid; Q8BPM0; -.
DR OMA; HSERTRF; -.
DR OrthoDB; 1204639at2759; -.
DR PhylomeDB; Q8BPM0; -.
DR TreeFam; TF314602; -.
DR Reactome; R-MMU-4086400; PCP/CE pathway.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013026; RHOB GTPase cycle.
DR Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR BioGRID-ORCS; 208846; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Daam1; mouse.
DR PRO; PR:Q8BPM0; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8BPM0; protein.
DR Bgee; ENSMUSG00000034574; Expressed in otolith organ and 269 other tissues.
DR Genevisible; Q8BPM0; MM.
DR GO; GO:0036064; C:ciliary basal body; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0031514; C:motile cilium; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0001725; C:stress fiber; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 1.20.58.2220; -; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR014767; DAD_dom.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR InterPro; IPR010472; FH3_dom.
DR InterPro; IPR014768; GBD/FH3_dom.
DR InterPro; IPR010473; GTPase-bd.
DR Pfam; PF06367; Drf_FH3; 1.
DR Pfam; PF06371; Drf_GBD; 1.
DR Pfam; PF02181; FH2; 1.
DR SMART; SM01139; Drf_FH3; 1.
DR SMART; SM01140; Drf_GBD; 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 Actin-binding; Alternative splicing; Cell projection; Coiled coil;
KW Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome;
KW Wnt signaling pathway.
FT CHAIN 1..1077
FT /note="Disheveled-associated activator of morphogenesis 1"
FT /id="PRO_0000194908"
FT DOMAIN 45..420
FT /note="GBD/FH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00579"
FT DOMAIN 528..599
FT /note="FH1"
FT DOMAIN 600..1008
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT DOMAIN 1026..1057
FT /note="DAD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00577"
FT REGION 457..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 526..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..702
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 1007..1033
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1056..1077
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 437..526
FT /evidence="ECO:0000255"
FT COMPBIAS 545..589
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4D1"
FT MOD_RES 1026
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4D1"
FT MOD_RES 1029
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 657..665
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_027771"
FT VAR_SEQ 657..659
FT /note="EFF -> VTT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027772"
FT VAR_SEQ 660..1077
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027773"
FT CONFLICT 36
FT /note="F -> L (in Ref. 1; AAR05118)"
FT /evidence="ECO:0000305"
FT CONFLICT 571
FT /note="P -> A (in Ref. 2; BAC35522)"
FT /evidence="ECO:0000305"
FT CONFLICT 894
FT /note="E -> G (in Ref. 2; BAE27943)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1077 AA; 123370 MW; E16AC9DEF6E05B15 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
TQMFELTRRR LTHSEAYPHF MSILHHCLQM PYKRSGNTVQ YWLLLDRIIQ QIVIQNDKGQ
DPDSTPLENF NIKNVVRMLV NENEVKQWKE QAEKMRKEHN ELQQKLEKKE RECDAKTQEK
EEMMQTLNKM KEKLEKETTE HKQVKQQVAD LTAQLHELNR RAVCAAVPGG PSPGAPGGPF
PSSGLGSLLP PPPPPLLSGG ALPPPPPPLP PGGPPPPPGP PPLGGVLPPP GAPVSLTLKK
KNIPQPTNAL KSFNWSKLPE NKLDGTVWTE IDDTKVFKIL DLEDLERTFS AYQRQQEFFV
NNSKQKEADA IDDTLSSKLK VKELSVIDGR RAQNCNILLS RLKLSNDEIK RAILTMDEQE
DLPKDMLEQL LKFVPEKSDI DLLEEHKHEL DRMAKADRFL FEMSRINHYQ QRLQSLYFKK
KFAERVAEVK PKVEAIRSGS EEVFRSRALK QLLEVVLAFG NYMNKGQRGN AYGFKISSLN
KIADTKSSID KNITLLHYLI TIVENKYPKV LNLSEELRDI PQAAKVNMTE LDKEISTLRS
GLKAVETELE YQKSQPPQPG DKFVSVVSQF ITLASFSFSD VEDLLAEAKE LFTKAVKHFG
EEAGKIQPDE FFGIFDQFLQ AVAEAKQENE NMRKRKEEEE RRARLEAQLK EQRERERKVR
KAKESSEESG EFDDLVSALR SGEVFDKDLS KLKRNRKRIS NQVTDSSRER PITKLNF
