AFAD_MOUSE
ID AFAD_MOUSE Reviewed; 1820 AA.
AC Q9QZQ1;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 3.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Afadin;
DE AltName: Full=Afadin adherens junction formation factor {ECO:0000312|MGI:MGI:1314653};
DE AltName: Full=Protein Af-6;
GN Name=Afdn {ECO:0000312|MGI:MGI:1314653}; Synonyms=Af6, Mllt4;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-320 (ISOFORM 1), FUNCTION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=C57BL/6J;
RX PubMed=10477764; DOI=10.1083/jcb.146.5.1117;
RA Ikeda W., Nakanishi H., Miyoshi J., Mandai K., Ishizaki H., Tanaka M.,
RA Togawa A., Takahashi K., Nishioka H., Yoshida H., Mizoguchi A.,
RA Nishikawa S., Takai Y.;
RT "Afadin: a key molecule essential for structural organization of cell-cell
RT junctions of polarized epithelia during embryogenesis.";
RL J. Cell Biol. 146:1117-1132(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 36-900 (ISOFORM 3).
RC TISSUE=Leukemia;
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 [4]
RP INTERACTION WITH NECTIN3.
RX PubMed=10744716; DOI=10.1074/jbc.275.14.10291;
RA Satoh-Horikawa K., Nakanishi H., Takahashi K., Miyahara M., Nishimura M.,
RA Tachibana K., Mizoguchi A., Takai Y.;
RT "Nectin-3: a new member of immunoglobulin-like cell adhesion molecules that
RT shows homophilic and heterophilic cell-cell adhesion activities.";
RL J. Biol. Chem. 275:10291-10299(2000).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-557, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1107 AND SER-1182, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216; SER-1083; SER-1107;
RP SER-1126; SER-1143; SER-1172; SER-1182; SER-1510; SER-1719; SER-1770 AND
RP SER-1795, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1803, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [11]
RP INTERACTION WITH ADAM10, AND SUBCELLULAR LOCATION.
RX PubMed=30463011; DOI=10.1016/j.celrep.2018.10.088;
RA Shah J., Rouaud F., Guerrera D., Vasileva E., Popov L.M., Kelley W.L.,
RA Rubinstein E., Carette J.E., Amieva M.R., Citi S.;
RT "A Dock-and-Lock Mechanism Clusters ADAM10 at Cell-Cell Junctions to
RT Promote alpha-Toxin Cytotoxicity.";
RL Cell Rep. 25:2132-2147(2018).
RN [12]
RP STRUCTURE BY NMR OF 246-487.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the FHA domain and RAS-binding domain in mouse AF-6
RT protein.";
RL Submitted (JUL-2005) to the PDB data bank.
CC -!- FUNCTION: Belongs to an adhesion system, probably together with the E-
CC cadherin-catenin system, which plays a role in the organization of
CC homotypic, interneuronal and heterotypic cell-cell adherens junctions
CC (AJs) (By similarity). Nectin- and actin-filament-binding protein that
CC connects nectin to the actin cytoskeleton (By similarity). May play a
CC key role in the organization of epithelial structures of the embryonic
CC ectoderm (PubMed:10477764). Essential for the organization of adherens
CC junctions (By similarity). {ECO:0000250|UniProtKB:O35889,
CC ECO:0000250|UniProtKB:P55196, ECO:0000269|PubMed:10477764}.
CC -!- SUBUNIT: Homodimer. Interacts with F-actin, nectin and NECTIN3.
CC Essential for the association of nectin and E-cadherin. Isoform 2/s-
CC afadin does not interact with F-actin. Interacts with ZO-1 and
CC occludin, but probably in an indirect manner. Interacts with RIT1,
CC RIT2, NRXN1 and BCR (By similarity). Interacts with ADAM10; the
CC interaction locks ADAM10 at adherens junctions following ADAM10
CC recruitment to adherens junctions by TSPAN33 (PubMed:30463011).
CC {ECO:0000250, ECO:0000269|PubMed:30463011}.
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC {ECO:0000269|PubMed:30463011}. Note=Not found at cell-matrix AJs.
CC {ECO:0000250|UniProtKB:O35889}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=3;
CC IsoId=Q9QZQ1-3; Sequence=Displayed;
CC Name=1; Synonyms=l-afadin;
CC IsoId=Q9QZQ1-2; Sequence=VSP_026731;
CC Name=2; Synonyms=s-afadin;
CC IsoId=Q9QZQ1-1; Sequence=Not described;
CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed only in a restricted set of
CC epithelial structures during early embryogenesis.
CC {ECO:0000269|PubMed:10477764}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed at restricted set of epithelial
CC structures and highly concentrated at their junctional complex regions.
CC At 6.5 dpc, localized at the most apical regions of cell-cell adhesion
CC sites of the entire embryonic ectoderm; not detected in the
CC extraembryonic regions. At 7.0 dpc, expressed in the primitive streak
CC and the migrating paraxial mesoderm. At 7.5 dpc, highly expressed at
CC the junctional complex regions in the primitive streak region
CC (neuroepithelium) and the neural fold/grove region, but hardly detected
CC in other areas of the ectoderm. By 8.5 dpc, highly expressed in the
CC tail bud, somites and the paraxial mesoderm, concentrated at the
CC junctional complex regions in neural tube, somites and
CC pericardioperitoneal canal. {ECO:0000269|PubMed:10477764}.
CC -!- DISRUPTION PHENOTYPE: Mice show developmental defects at stages during
CC and after gastrulation, including disorganization of the ectoderm,
CC impaired migration of the mesoderm and loss of somites and other
CC structures derived from both the ectoderm and mesoderm. Cell-cell
CC adherens juntions and tight junctions are improperly organized in the
CC ectoderm-derived cells. No redundancy exists in the function of afadin
CC during gastrulation. {ECO:0000269|PubMed:10477764}.
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DR EMBL; AC155253; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CAAA01106165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CAAA01134612; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CAAA01201738; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CAAA01218165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF172447; AAD54283.1; -; mRNA.
DR EMBL; AK016557; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS49955.1; -. [Q9QZQ1-3]
DR RefSeq; NP_034936.1; NM_010806.1. [Q9QZQ1-3]
DR PDB; 1WLN; NMR; -; A=381-502.
DR PDB; 1WXA; NMR; -; A=246-348.
DR PDB; 3AXA; X-ray; 2.78 A; A/B=1003-1095.
DR PDB; 6AMB; X-ray; 2.50 A; B=38-136.
DR PDBsum; 1WLN; -.
DR PDBsum; 1WXA; -.
DR PDBsum; 3AXA; -.
DR PDBsum; 6AMB; -.
DR AlphaFoldDB; Q9QZQ1; -.
DR BMRB; Q9QZQ1; -.
DR SMR; Q9QZQ1; -.
DR BioGRID; 201438; 19.
DR DIP; DIP-60737N; -.
DR IntAct; Q9QZQ1; 6.
DR MINT; Q9QZQ1; -.
DR STRING; 10090.ENSMUSP00000118318; -.
DR iPTMnet; Q9QZQ1; -.
DR PhosphoSitePlus; Q9QZQ1; -.
DR SwissPalm; Q9QZQ1; -.
DR EPD; Q9QZQ1; -.
DR jPOST; Q9QZQ1; -.
DR MaxQB; Q9QZQ1; -.
DR PaxDb; Q9QZQ1; -.
DR PeptideAtlas; Q9QZQ1; -.
DR PRIDE; Q9QZQ1; -.
DR ProteomicsDB; 281948; -. [Q9QZQ1-3]
DR ProteomicsDB; 281949; -. [Q9QZQ1-2]
DR Antibodypedia; 4608; 279 antibodies from 32 providers.
DR DNASU; 17356; -.
DR Ensembl; ENSMUST00000139666; ENSMUSP00000118318; ENSMUSG00000068036. [Q9QZQ1-3]
DR Ensembl; ENSMUST00000150848; ENSMUSP00000122447; ENSMUSG00000068036. [Q9QZQ1-2]
DR GeneID; 17356; -.
DR KEGG; mmu:17356; -.
DR UCSC; uc008amr.1; mouse. [Q9QZQ1-3]
DR CTD; 4301; -.
DR MGI; MGI:1314653; Afdn.
DR VEuPathDB; HostDB:ENSMUSG00000068036; -.
DR eggNOG; KOG1892; Eukaryota.
DR GeneTree; ENSGT00940000155237; -.
DR InParanoid; Q9QZQ1; -.
DR OMA; YRCAQDE; -.
DR OrthoDB; 23029at2759; -.
DR PhylomeDB; Q9QZQ1; -.
DR TreeFam; TF350731; -.
DR Reactome; R-MMU-418990; Adherens junctions interactions.
DR BioGRID-ORCS; 17356; 2 hits in 43 CRISPR screens.
DR ChiTaRS; Mllt4; mouse.
DR EvolutionaryTrace; Q9QZQ1; -.
DR PRO; PR:Q9QZQ1; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9QZQ1; protein.
DR Bgee; ENSMUSG00000068036; Expressed in tail skin and 239 other tissues.
DR ExpressionAtlas; Q9QZQ1; baseline and differential.
DR Genevisible; Q9QZQ1; MM.
DR GO; GO:0005912; C:adherens junction; IDA:MGI.
DR GO; GO:0043296; C:apical junction complex; IDA:MGI.
DR GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0030054; C:cell junction; IDA:MGI.
DR GO; GO:0044291; C:cell-cell contact zone; ISO:MGI.
DR GO; GO:0005911; C:cell-cell junction; IDA:ARUK-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0060076; C:excitatory synapse; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0046930; C:pore complex; IMP:UniProtKB.
DR GO; GO:0036477; C:somatodendritic compartment; ISO:MGI.
DR GO; GO:0070160; C:tight junction; ISO:MGI.
DR GO; GO:0051015; F:actin filament binding; ISO:MGI.
DR GO; GO:0050839; F:cell adhesion molecule binding; IPI:BHF-UCL.
DR GO; GO:0030274; F:LIM domain binding; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0034334; P:adherens junction maintenance; IMP:MGI.
DR GO; GO:0070830; P:bicellular tight junction assembly; ISO:MGI.
DR GO; GO:0048854; P:brain morphogenesis; IGI:MGI.
DR GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; IMP:ARUK-UCL.
DR GO; GO:0021987; P:cerebral cortex development; IMP:MGI.
DR GO; GO:0140059; P:dendrite arborization; ISO:MGI.
DR GO; GO:0090557; P:establishment of endothelial intestinal barrier; ISO:MGI.
DR GO; GO:0061951; P:establishment of protein localization to plasma membrane; IMP:ARUK-UCL.
DR GO; GO:0048872; P:homeostasis of number of cells; IGI:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
DR GO; GO:0060563; P:neuroepithelial cell differentiation; IGI:MGI.
DR GO; GO:0046931; P:pore complex assembly; IMP:UniProtKB.
DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; ISO:MGI.
DR GO; GO:2000049; P:positive regulation of cell-cell adhesion mediated by cadherin; ISO:MGI.
DR GO; GO:1903861; P:positive regulation of dendrite extension; ISO:MGI.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; ISO:MGI.
DR GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:MGI.
DR GO; GO:0061885; P:positive regulation of mini excitatory postsynaptic potential; ISO:MGI.
DR GO; GO:1902414; P:protein localization to cell junction; IMP:MGI.
DR GO; GO:0060019; P:radial glial cell differentiation; IGI:MGI.
DR GO; GO:0070445; P:regulation of oligodendrocyte progenitor proliferation; IGI:MGI.
DR GO; GO:0032880; P:regulation of protein localization; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0021537; P:telencephalon development; IGI:MGI.
DR CDD; cd00060; FHA; 1.
DR CDD; cd15471; Myo5p-like_CBD_afadin; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR037977; CBD_Afadin.
DR InterPro; IPR002710; Dilute_dom.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF01843; DIL; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF00788; RA; 2.
DR SMART; SM01132; DIL; 1.
DR SMART; SM00240; FHA; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00314; RA; 2.
DR SUPFAM; SSF49879; SSF49879; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF54236; SSF54236; 2.
DR PROSITE; PS51126; DILUTE; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50200; RA; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell adhesion;
KW Cell junction; Coiled coil; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1820
FT /note="Afadin"
FT /id="PRO_0000215919"
FT DOMAIN 39..133
FT /note="Ras-associating 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT DOMAIN 246..348
FT /note="Ras-associating 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT DOMAIN 426..492
FT /note="FHA"
FT DOMAIN 653..908
FT /note="Dilute"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00503"
FT DOMAIN 1007..1093
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 129..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1107..1194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1203..1222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1235..1278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1308..1527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1567..1716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1734..1820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 146..186
FT /evidence="ECO:0000255"
FT COILED 1410..1446
FT /evidence="ECO:0000255"
FT COILED 1523..1561
FT /evidence="ECO:0000255"
FT COILED 1593..1665
FT /evidence="ECO:0000255"
FT COMPBIAS 143..196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..568
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1130..1147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1154..1169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1171..1194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1308..1340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1360..1376
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1406..1441
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1442..1490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1512..1527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1588..1684
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1685..1709
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1802..1820
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55196"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55196"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35889"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55196"
FT MOD_RES 512
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55196"
FT MOD_RES 557
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 562
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55196"
FT MOD_RES 655
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55196"
FT MOD_RES 1083
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35889"
FT MOD_RES 1143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1172
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1173
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55196"
FT MOD_RES 1182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1199
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55196"
FT MOD_RES 1232
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P55196"
FT MOD_RES 1238
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55196"
FT MOD_RES 1275
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55196"
FT MOD_RES 1328
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55196"
FT MOD_RES 1330
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P55196"
FT MOD_RES 1499
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55196"
FT MOD_RES 1510
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1694
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55196"
FT MOD_RES 1719
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1770
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1795
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1803
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT VAR_SEQ 393..407
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:10477764"
FT /id="VSP_026731"
FT CONFLICT 23
FT /note="N -> Y (in Ref. 2; AAD54283)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="E -> EE (in Ref. 3; AK016557)"
FT /evidence="ECO:0000305"
FT CONFLICT 694
FT /note="N -> D (in Ref. 3; AK016557)"
FT /evidence="ECO:0000305"
FT CONFLICT 897..900
FT /note="DLIE -> PEMR (in Ref. 3; AK016557)"
FT /evidence="ECO:0000305"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:6AMB"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:6AMB"
FT HELIX 68..79
FT /evidence="ECO:0007829|PDB:6AMB"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:6AMB"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:6AMB"
FT HELIX 110..114
FT /evidence="ECO:0007829|PDB:6AMB"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:6AMB"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:1WXA"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:1WXA"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:1WXA"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:1WXA"
FT HELIX 274..285
FT /evidence="ECO:0007829|PDB:1WXA"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:1WXA"
FT TURN 292..294
FT /evidence="ECO:0007829|PDB:1WXA"
FT STRAND 295..301
FT /evidence="ECO:0007829|PDB:1WXA"
FT STRAND 308..311
FT /evidence="ECO:0007829|PDB:1WXA"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:1WXA"
FT HELIX 325..330
FT /evidence="ECO:0007829|PDB:1WXA"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:1WXA"
FT STRAND 339..345
FT /evidence="ECO:0007829|PDB:1WXA"
FT HELIX 381..383
FT /evidence="ECO:0007829|PDB:1WLN"
FT STRAND 386..390
FT /evidence="ECO:0007829|PDB:1WLN"
FT STRAND 418..420
FT /evidence="ECO:0007829|PDB:1WLN"
FT STRAND 423..427
FT /evidence="ECO:0007829|PDB:1WLN"
FT STRAND 429..431
FT /evidence="ECO:0007829|PDB:1WLN"
FT STRAND 450..457
FT /evidence="ECO:0007829|PDB:1WLN"
FT STRAND 459..464
FT /evidence="ECO:0007829|PDB:1WLN"
FT STRAND 466..468
FT /evidence="ECO:0007829|PDB:1WLN"
FT STRAND 470..474
FT /evidence="ECO:0007829|PDB:1WLN"
FT STRAND 481..483
FT /evidence="ECO:0007829|PDB:1WLN"
FT STRAND 488..491
FT /evidence="ECO:0007829|PDB:1WLN"
FT TURN 492..494
FT /evidence="ECO:0007829|PDB:1WLN"
FT STRAND 495..500
FT /evidence="ECO:0007829|PDB:1WLN"
FT STRAND 1007..1013
FT /evidence="ECO:0007829|PDB:3AXA"
FT STRAND 1015..1017
FT /evidence="ECO:0007829|PDB:3AXA"
FT STRAND 1019..1026
FT /evidence="ECO:0007829|PDB:3AXA"
FT STRAND 1031..1041
FT /evidence="ECO:0007829|PDB:3AXA"
FT HELIX 1045..1049
FT /evidence="ECO:0007829|PDB:3AXA"
FT STRAND 1057..1061
FT /evidence="ECO:0007829|PDB:3AXA"
FT HELIX 1071..1079
FT /evidence="ECO:0007829|PDB:3AXA"
FT STRAND 1083..1090
FT /evidence="ECO:0007829|PDB:3AXA"
SQ SEQUENCE 1820 AA; 206499 MW; 9FA4F378D840D8B1 CRC64;
MSAGGRDEER RKLADIIHHW NANRLDLFEI SQPTEDLEFH GVMRFYFQDK AAGNFATKCI
RVSSTATTQD VIETLAEKFR PDMRMLSSPK YSLYEVHVSG ERRLDIDEKP LVVQLNWNKD
DREGRFVLKN ENDAIPAKKA QSNGPEKQEK EGVIQNFKRT LSKKEKKEKK KKEKEALRQA
SDKEERPSQG DDSENSRLAA EVYKDMPETS FTRTISNPEV VMKRRRQQKL EKRMQEFRSS
DGRPDSGGTL RIYADSLKPN IPYKTILLST TDTADFAVAE SLEKYGLEKE NPKDYCIARV
MLPPGAQHSD ERGAKEIILD DDECPLQIFR EWPSDKGILV FQLKRRPPDY IPKKMKKHVE
GKSLKGKDRA DGSGYGSALP PEKLPYLVEL SPGRRNHFAY YSYHTYEDGS DSRDKPKLYR
LQLSVTEVGT EKFDDNSIQL FGPGIQPHHC DLTNMDGVVT VTPRSMDAET YVDGQRISET
TMLQSGMRLQ FGTSHVFKFV DPIQDHVLSK RSVDGGLMVK GPRHKPGAVQ ETTFELGGDV
HSGTALPASR STTRLDSDRV SSASSTAERG MVKPMIRLDQ EQEYRRRENR TQDATGPELI
LPASIEFRES SEDSFLSAII NYTNSSTVHF KLSPTYVLYM ACRYVLSSQH RPDISPTERT
HKAIAVVNKM VSMMEGVIQK QKNIAGALAF WMANASELLN FIKQDRDLSR ITLDAQDVLA
HLVQMAFKYL VHCLQSELNN YMPAFLDDPE ENSLQRPKID DVLHTLTGAM SLLRRCRVNA
ALTIQLFSQL FHFINMWLFN RLVTDPDSGL CSHYWGAIIR QQLGHIEAWA EKQGLELAAD
CHLSRIVQAT TLLTMDKYVP DDIPNINSTC FKLNSLQLQA LLQNYHCAPD EPFIPTDLIE
NVVAVAENTA DELARSDGRD VQLEEDPDLQ LPFLLPEDGY SCDVVRNIPN GLQEFLDPLC
QRGFCRLVPH TRSPGTWTIY FEGADYESHL MRENAELAQP LRKEPEIITV TLKKQNGMGL
SIVAAKGAGQ DKLGIYVKSV VKGGAADVDG RLAAGDQLLS VDGRSLVGLS QERAAELMTR
TSSVVTLEVA KQGAIYHGLA TLLNQPSPMM QRISDRRGSG KPRPKSEGFE LYNNSAQNGS
PESPQMPWTE YSEPKKLPGD DRLMKNRADH RSSPNVANQP PSPGGKGPYT SGTAAKITSV
STGNLCTEEQ SPPPRPEAYP IPTQTYTREY FTFPASKSQD RMAPPQSQWP NYEEKPHVHT
ESNHSSIAIQ RVTRSQEELR EEKVYQLERH RVEAGMDRKC DSDMWINQSS SVESSTSSQE
HLNHSSKSVT PASTLTKSGP GRWKTPAAVL PTPVAVSQPI RTDLPPPPPP PPVHYTSEFD
GIPMDLPLPP PPANQAGPQS AQVAAAEWKK REEHQRWYEK EKARLEEERE RKRREQERKL
GQMRSQTLNP ASFSPLATQA KPEKPSTLQR PQETVIRELQ PQQQPRTIER KDLQYITISK
EELSSGDSLS PDPWKRDARE KLEKQQQMHI VDMLSKEIHE LQNKVDRTAE ESDRLRKLML
EWQFQKRLQE SKQKDEDDDE EEDDDVDTML IMQRLEAERR ARMQDEERRR QQQLEEMRKR
EAEDRVRQEE DGRHQEEERV KRDAEEKRRQ EEGYYSRLEA ERRRQHEEAA RRLLEPEEPG
LSRPPLPRDY EPPSLSSAPC APPPPPQRNA SYLKTQVLSP DSLFTAKFVA YDEEEEDYGP
AGPNSYSGSA GTAVGAYDAP REAREKLTRS QDADLPGSSG APENLTFKER QRLFSQGQDV
SDKVKASRKL TELENELNTK
