DAAM2_CHICK
ID DAAM2_CHICK Reviewed; 1075 AA.
AC A0A1D5P556; A0A1D5P1Y2; A0A1D5PPK5; E1BS28;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2018, sequence version 2.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=Disheveled-associated activator of morphogenesis 2 {ECO:0000303|PubMed:22227309};
GN Name=DAAM2 {ECO:0000303|PubMed:22227309};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
RN [2]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=22227309; DOI=10.1016/j.devcel.2011.10.025;
RA Lee H.K., Deneen B.;
RT "Daam2 is required for dorsal patterning via modulation of canonical Wnt
RT signaling in the developing spinal cord.";
RL Dev. Cell 22:183-196(2012).
RN [3]
RP FUNCTION.
RX PubMed=24091014; DOI=10.1016/j.devcel.2013.07.019;
RA Welsh I.C., Thomsen M., Gludish D.W., Alfonso-Parra C., Bai Y.,
RA Martin J.F., Kurpios N.A.;
RT "Integration of left-right Pitx2 transcription and Wnt signaling drives
RT asymmetric gut morphogenesis via Daam2.";
RL Dev. Cell 26:629-644(2013).
RN [4]
RP FUNCTION.
RX PubMed=25754822; DOI=10.1016/j.neuron.2015.02.024;
RA Lee H.K., Chaboub L.S., Zhu W., Zollinger D., Rasband M.N., Fancy S.P.,
RA Deneen B.;
RT "Daam2-PIP5K is a regulatory pathway for Wnt signaling and therapeutic
RT target for remyelination in the CNS.";
RL Neuron 85:1227-1243(2015).
CC -!- FUNCTION: Key regulator of the Wnt signaling pathway, which is required
CC for various processes during development, such as dorsal patterning,
CC determination of left/right symmetry or myelination in the central
CC nervous system (PubMed:22227309, PubMed:24091014, PubMed:25754822).
CC Acts downstream of Wnt ligands and upstream of beta-catenin (CTNNB1)
CC (PubMed:22227309, PubMed:25754822). Required for canonical Wnt
CC signaling pathway during patterning in the dorsal spinal cord by
CC promoting the aggregation of Disheveled (Dvl) complexes, thereby
CC clustering and formation of Wnt receptor signalosomes and potentiating
CC Wnt activity (PubMed:22227309). During dorsal patterning of the spinal
CC cord, inhibits oligodendrocytes differentiation via interaction with
CC PIP5K1A (PubMed:25754822). Also regulates non-canonical Wnt signaling
CC pathway (PubMed:24091014). Acts downstream of PITX2 in the developing
CC gut and is required for left/right asymmetry within dorsal mesentery:
CC affects mesenchymal condensation by lengthening cadherin-based
CC junctions through WNT5A and non-canonical Wnt signaling, inducing
CC polarized condensation in the left dorsal mesentery necessary to
CC initiate gut rotation (PubMed:24091014). Together with DAAM1, required
CC for myocardial maturation and sarcomere assembly (By similarity).
CC {ECO:0000250|UniProtKB:Q80U19, ECO:0000269|PubMed:22227309,
CC ECO:0000269|PubMed:24091014, ECO:0000269|PubMed:25754822}.
CC -!- TISSUE SPECIFICITY: Expressed in progenitor populations of the
CC embryonic spinal cord (at protein level).
CC {ECO:0000269|PubMed:22227309}.
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 -!- SIMILARITY: Belongs to the formin homology family. {ECO:0000305}.
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DR EMBL; AADN04000139; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A1D5P556; -.
DR SMR; A0A1D5P556; -.
DR STRING; 9031.ENSGALP00000037454; -.
DR VEuPathDB; HostDB:geneid_421422; -.
DR eggNOG; KOG1922; Eukaryota.
DR OrthoDB; 1204639at2759; -.
DR TreeFam; TF314602; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:0021516; P:dorsal spinal cord development; IMP:UniProtKB.
DR GO; GO:0048715; P:negative regulation of oligodendrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IDA:UniProtKB.
DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:2000050; P:regulation of non-canonical Wnt signaling pathway; ISS:UniProtKB.
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; Coiled coil; Reference proteome; Wnt signaling pathway.
FT CHAIN 1..1075
FT /note="Disheveled-associated activator of morphogenesis 2"
FT /id="PRO_0000443450"
FT DOMAIN 40..416
FT /note="GBD/FH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00579"
FT DOMAIN 605..1075
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT DOMAIN 1025..1075
FT /note="DAD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00577"
FT REGION 517..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1006..1025
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1048..1075
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 437..517
FT /evidence="ECO:0000255"
FT COMPBIAS 548..588
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..611
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1048..1062
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1075 AA; 123875 MW; 560A248895831513 CRC64;
MAPRKRNRHA LGFLCCFGGS DLPEINLKDN NPLQFLDFTV PIPPTEELNA RFSELVDELD
LTDKNREAMF ALPPEKKWQI YCSKKKEQED PNKLATSWPD YYIDRINSMA AMQTLYAFDE
EETEMKNKIV EDLKTALRTQ PMRFVMRFIE LDGLSCLLNF LKSMDYETSE SRIHTSVIGC
IKALMNNSQG RAHVLAHPES INIISQSLRT ENIKTKIAVL EILGAVCLVP DGHKKVLQAM
LHYQVYAAER TRFQTLLNEL DRSMGRYRDE VNLKTAIMSF INAVLNAGAG EDNLEFRLHL
RYEFLMLGIQ PVIDKLREHE NATLDRHLDF FEMVRNEDDL ELAKRFDLIH IDTKSASQMF
ELIKKRLKHT DAYPYLLSIL QHCLQMPYKR NGGNFQQWQL LDRILQQIVL QDERGDDPDI
APLENFNVKN IIKMLVNENE VKQWRDQAEK FRKDHAELMS KLEKKERECE TKTQEKDEMM
KTLNKMKDKL QKESLELRQA RDQMNDLVAQ LNEYSQGGSI SFPAPPPPPP GGPLALSSAL
SSALTSENLP PLPPPLPFSS CPPPPAPPPP PGGPPPPPGA PPFFSLGVPP PSTTTFSSAG
TSLKKKSIPQ PSHPLKSFNW AKLSEERIHG TIWNEIDDLK AFKVLDLEDF EKMFSAYQRH
QKEMGSTEDL YLSTRKVKEL SVIDGRRAQN CVILLSKLKL SNEEIRQAIL KMDEQEDLAK
DMLEQLLKFV PEKSDTDLLE EHKHEIERMA RADRFLFEMS RIDHYQQRLQ ALFFKKKFPE
RLAEAKPKVE AILLASKELI RSKRLRQLLE VVLAFGNYMN KGQRGSAYGF KVSSLNKIAD
TKSSIDRNIT LLHYLIMIFE KNYPDILDIQ TELQHLPEAA KVNLVELEKE VNNIKTGLKA
VEAELDYQKR RIRESGDRFV PVMSDFITVA SFSFSELEDL LNDARDKYAK ALKHFGENEG
KMQPDEFFGI FDTFLQSFAE AKQDLENMRK KKEEEERRAR MEAMLKEQRE KERRQKKAKA
GSISEETGEF DDLVSALRSG EVFDKDLSKL KRNRKRSGNQ GLETSRERVV TKLNY
