DAAM1_HUMAN
ID DAAM1_HUMAN Reviewed; 1078 AA.
AC Q9Y4D1; Q86U34; Q8N1Z8; Q8TB39;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 188.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT 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., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., 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., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA 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 project:
RT 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 RhoA
RT and Cdc42, CIP4 and Src in regulating cell morphogenesis and actin
RT 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., Buerckstuemmer T.,
RA 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1027, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34 AND SER-1027, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 596-1078, SUBUNIT, MUTAGENESIS OF
RP 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 regulation
RT of actin assembly.";
RL J. Mol. Biol. 369:1258-1269(2007).
RN [12]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH INTU AND NPHP4.
RX PubMed=26644512; DOI=10.1083/jcb.201502043;
RA Yasunaga T., Hoff S., Schell C., Helmstaedter M., Kretz O., Kuechlin S.,
RA Yakulov T.A., Engel C., Mueller B., Bensch R., Ronneberger O., Huber T.B.,
RA Lienkamp S.S., Walz G.;
RT "The polarity protein Inturned links NPHP4 to Daam1 to control the
RT subapical actin network in multiciliated cells.";
RL J. Cell Biol. 211:963-973(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. Involved in
CC building functional cilia (PubMed:16630611, PubMed:17482208). Involved
CC in the organization of the subapical actin network in multiciliated
CC epithelial cells (By similarity). Together with DAAM2, required for
CC myocardial maturation and sarcomere assembly (By similarity).
CC {ECO:0000250|UniProtKB:B0DOB5, ECO:0000250|UniProtKB:Q8BPM0,
CC ECO:0000269|PubMed:16630611, ECO:0000269|PubMed:17482208}.
CC -!- SUBUNIT: Homodimer. Interacts with CIP4, FNBP1 and FNBP1L. Interacts
CC with the SH3 domains of Abl, BTK, endophilin, spectrin and SRC. Binds
CC specifically to GTP-bound CDC42 and RHOA. Interacts with INTU; INTU
CC mediates the indirect interaction between DAAM1 and NPHP4.
CC {ECO:0000269|PubMed:16630611, ECO:0000269|PubMed:17482208}.
CC -!- INTERACTION:
CC Q9Y4D1; Q9Y4D1: DAAM1; NbExp=2; IntAct=EBI-2817289, EBI-2817289;
CC Q9Y4D1; Q5T0N5: FNBP1L; NbExp=2; IntAct=EBI-2817289, EBI-714058;
CC Q9Y4D1; Q9ULD6: INTU; NbExp=3; IntAct=EBI-2817289, EBI-11762696;
CC Q9Y4D1; P61586: RHOA; NbExp=5; IntAct=EBI-2817289, EBI-446668;
CC Q9Y4D1; Q15642-2: TRIP10; NbExp=2; IntAct=EBI-2817289, EBI-6550597;
CC Q9Y4D1; P00523: SRC; Xeno; NbExp=3; IntAct=EBI-2817289, EBI-848039;
CC Q9Y4D1-1; Q9Y4D1-1: DAAM1; NbExp=3; IntAct=EBI-15677700, EBI-15677700;
CC Q9Y4D1-1; Q60838: Dvl2; Xeno; NbExp=4; IntAct=EBI-15677700, EBI-641940;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16630611}.
CC Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000269|PubMed:26644512}. 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 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 -!- SIMILARITY: Belongs to the formin homology family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA31641.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC04230.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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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 CCDS; CCDS58323.1; -. [Q9Y4D1-2]
DR CCDS; CCDS9737.1; -. [Q9Y4D1-1]
DR RefSeq; NP_001257449.1; NM_001270520.1. [Q9Y4D1-2]
DR RefSeq; NP_055807.1; NM_014992.2. [Q9Y4D1-1]
DR RefSeq; XP_005267487.1; XM_005267430.1. [Q9Y4D1-1]
DR RefSeq; XP_005267488.1; XM_005267431.1. [Q9Y4D1-1]
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 AlphaFoldDB; Q9Y4D1; -.
DR SMR; Q9Y4D1; -.
DR BioGRID; 116648; 48.
DR DIP; DIP-29641N; -.
DR IntAct; Q9Y4D1; 38.
DR MINT; Q9Y4D1; -.
DR STRING; 9606.ENSP00000378557; -.
DR iPTMnet; Q9Y4D1; -.
DR PhosphoSitePlus; Q9Y4D1; -.
DR SwissPalm; Q9Y4D1; -.
DR BioMuta; DAAM1; -.
DR DMDM; 34098767; -.
DR EPD; Q9Y4D1; -.
DR jPOST; Q9Y4D1; -.
DR MassIVE; Q9Y4D1; -.
DR MaxQB; Q9Y4D1; -.
DR PaxDb; Q9Y4D1; -.
DR PeptideAtlas; Q9Y4D1; -.
DR PRIDE; Q9Y4D1; -.
DR ProteomicsDB; 86164; -. [Q9Y4D1-1]
DR ProteomicsDB; 86165; -. [Q9Y4D1-2]
DR ProteomicsDB; 86166; -. [Q9Y4D1-3]
DR Antibodypedia; 11379; 358 antibodies from 30 providers.
DR DNASU; 23002; -.
DR Ensembl; ENST00000360909.8; ENSP00000354162.3; ENSG00000100592.16. [Q9Y4D1-2]
DR Ensembl; ENST00000395125.1; ENSP00000378557.1; ENSG00000100592.16. [Q9Y4D1-1]
DR GeneID; 23002; -.
DR KEGG; hsa:23002; -.
DR MANE-Select; ENST00000360909.8; ENSP00000354162.3; NM_001270520.2; NP_001257449.1. [Q9Y4D1-2]
DR UCSC; uc001xea.3; human. [Q9Y4D1-1]
DR CTD; 23002; -.
DR DisGeNET; 23002; -.
DR GeneCards; DAAM1; -.
DR HGNC; HGNC:18142; DAAM1.
DR HPA; ENSG00000100592; Low tissue specificity.
DR MIM; 606626; gene.
DR neXtProt; NX_Q9Y4D1; -.
DR OpenTargets; ENSG00000100592; -.
DR PharmGKB; PA27129; -.
DR VEuPathDB; HostDB:ENSG00000100592; -.
DR eggNOG; KOG1922; Eukaryota.
DR GeneTree; ENSGT00940000156452; -.
DR HOGENOM; CLU_002356_1_0_1; -.
DR InParanoid; Q9Y4D1; -.
DR OMA; HSERTRF; -.
DR OrthoDB; 1204639at2759; -.
DR PhylomeDB; Q9Y4D1; -.
DR TreeFam; TF314602; -.
DR PathwayCommons; Q9Y4D1; -.
DR Reactome; R-HSA-4086400; PCP/CE pathway.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013026; RHOB GTPase cycle.
DR Reactome; R-HSA-9013106; RHOC GTPase cycle.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR SignaLink; Q9Y4D1; -.
DR SIGNOR; Q9Y4D1; -.
DR BioGRID-ORCS; 23002; 9 hits in 1077 CRISPR screens.
DR ChiTaRS; DAAM1; human.
DR EvolutionaryTrace; Q9Y4D1; -.
DR GeneWiki; DAAM1; -.
DR GenomeRNAi; 23002; -.
DR Pharos; Q9Y4D1; Tbio.
DR PRO; PR:Q9Y4D1; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9Y4D1; protein.
DR Bgee; ENSG00000100592; Expressed in oocyte and 210 other tissues.
DR ExpressionAtlas; Q9Y4D1; baseline and differential.
DR Genevisible; Q9Y4D1; HS.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0031514; C:motile cilium; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
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; IPI:IntAct.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; NAS:ParkinsonsUK-UCL.
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 3D-structure; Actin-binding; Alternative splicing; Cell projection;
KW Coiled coil; Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome;
KW Wnt signaling pathway.
FT CHAIN 1..1078
FT /note="Disheveled-associated activator of morphogenesis 1"
FT /id="PRO_0000194907"
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..1009
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT DOMAIN 1027..1058
FT /note="DAD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00577"
FT REGION 456..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..702
FT /note="Actin-binding"
FT REGION 987..1034
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1055..1078
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 437..526
FT /evidence="ECO:0000255"
FT COMPBIAS 532..585
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1034
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1027
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1030
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BPM0"
FT VAR_SEQ 656..665
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_008000"
FT VAR_SEQ 788..818
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_008001"
FT VAR_SEQ 888..916
FT /note="NMTELDKEISTLRSGLKAVETELEYQKSQ -> KSWNIRSLSPHSPEISLCL
FT LSASSSQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_008002"
FT VAR_SEQ 917..1078
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_008003"
FT MUTAGEN 698
FT /note="I->A: Abolishes actin-binding."
FT /evidence="ECO:0000269|PubMed:17482208"
FT CONFLICT 940
FT /note="S -> F (in Ref. 3; AAH24781)"
FT /evidence="ECO:0000305"
FT STRAND 596..598
FT /evidence="ECO:0007829|PDB:2Z6E"
FT HELIX 620..622
FT /evidence="ECO:0007829|PDB:2J1D"
FT STRAND 624..626
FT /evidence="ECO:0007829|PDB:2J1D"
FT HELIX 627..630
FT /evidence="ECO:0007829|PDB:2J1D"
FT HELIX 633..635
FT /evidence="ECO:0007829|PDB:2J1D"
FT HELIX 636..639
FT /evidence="ECO:0007829|PDB:2J1D"
FT HELIX 642..648
FT /evidence="ECO:0007829|PDB:2J1D"
FT STRAND 650..652
FT /evidence="ECO:0007829|PDB:2J1D"
FT HELIX 690..703
FT /evidence="ECO:0007829|PDB:2J1D"
FT HELIX 707..715
FT /evidence="ECO:0007829|PDB:2J1D"
FT HELIX 725..733
FT /evidence="ECO:0007829|PDB:2J1D"
FT HELIX 738..745
FT /evidence="ECO:0007829|PDB:2J1D"
FT TURN 746..749
FT /evidence="ECO:0007829|PDB:2J1D"
FT HELIX 751..753
FT /evidence="ECO:0007829|PDB:2J1D"
FT HELIX 756..765
FT /evidence="ECO:0007829|PDB:2J1D"
FT HELIX 770..806
FT /evidence="ECO:0007829|PDB:2J1D"
FT HELIX 808..824
FT /evidence="ECO:0007829|PDB:2J1D"
FT STRAND 827..829
FT /evidence="ECO:0007829|PDB:2J1D"
FT HELIX 837..845
FT /evidence="ECO:0007829|PDB:2J1D"
FT HELIX 856..867
FT /evidence="ECO:0007829|PDB:2J1D"
FT HELIX 869..873
FT /evidence="ECO:0007829|PDB:2J1D"
FT HELIX 874..877
FT /evidence="ECO:0007829|PDB:2J1D"
FT TURN 878..880
FT /evidence="ECO:0007829|PDB:2J1D"
FT HELIX 881..885
FT /evidence="ECO:0007829|PDB:2J1D"
FT HELIX 889..914
FT /evidence="ECO:0007829|PDB:2J1D"
FT HELIX 924..959
FT /evidence="ECO:0007829|PDB:2J1D"
FT HELIX 969..994
FT /evidence="ECO:0007829|PDB:2J1D"
FT HELIX 996..999
FT /evidence="ECO:0007829|PDB:2J1D"
FT HELIX 1001..1022
FT /evidence="ECO:0007829|PDB:2J1D"
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
