DAB2_MOUSE
ID DAB2_MOUSE Reviewed; 766 AA.
AC P98078; Q3U3K1; Q91W56; Q923E1;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Disabled homolog 2;
DE AltName: Full=Adaptor molecule disabled-2;
DE AltName: Full=Differentially expressed in ovarian carcinoma 2;
DE Short=DOC-2;
DE AltName: Full=Mitogen-responsive phosphoprotein;
GN Name=Dab2; Synonyms=Doc2;
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] (ISOFORMS P67; P93 AND P96).
RC STRAIN=BALB/cJ; TISSUE=Macrophage;
RX PubMed=7775479; DOI=10.1074/jbc.270.23.14184;
RA Xu X.-X., Yang W., Jackowski S., Rock C.O.;
RT "Cloning of a novel phosphoprotein regulated by colony-stimulating factor 1
RT shares a domain with the Drosophila disabled gene product.";
RL J. Biol. Chem. 270:14184-14191(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM P96).
RC STRAIN=129/Sv;
RX PubMed=11368898; DOI=10.1016/s0378-1119(01)00401-2;
RA Sheng Z., Smith E.R., He J., Tuppen J.A., Martin W.D., Dong F.B., Xu X.X.;
RT "Chromosomal location of murine disabled-2 gene and structural comparison
RT with its human ortholog.";
RL Gene 268:31-39(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM P96).
RC STRAIN=NOD; TISSUE=Dendritic cell;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM P67).
RC TISSUE=Kidney;
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 [5]
RP INTERACTION WITH GRB2.
RX PubMed=9569023; DOI=10.1038/sj.onc.1201678;
RA Xu X.X., Yi T., Tang B., Lambeth J.D.;
RT "Disabled-2 (Dab2) is an SH3 domain-binding partner of Grb2.";
RL Oncogene 16:1561-1569(1998).
RN [6]
RP FUNCTION (ISOFORM P67), SUBCELLULAR LOCATION (ISOFORM P67), AND INTERACTION
RP WITH PIAS2.
RX PubMed=11104669; DOI=10.1042/bj3520645;
RA Cho S.-Y., Jeon J.W., Lee S.H., Park S.-S.;
RT "p67 isoform of mouse disabled 2 protein acts as a transcriptional
RT activator during the differentiation of F9 cells.";
RL Biochem. J. 352:645-650(2000).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH LDLR; APP; APLP; APLP2;
RP INPP5D; LRP1 AND AP2A2, AND DOMAIN.
RX PubMed=11247302; DOI=10.1034/j.1600-0854.2001.020206.x;
RA Morris S.M., Cooper J.A.;
RT "Disabled-2 colocalizes with the LDLR in clathrin-coated pits and interacts
RT with AP-2.";
RL Traffic 2:111-123(2001).
RN [8]
RP INTERACTION WITH MYO6.
RX PubMed=11906161; DOI=10.1006/bbrc.2002.6636;
RA Inoue A., Sato O., Homma K., Ikebe M.;
RT "DOC-2/DAB2 is the binding partner of myosin VI.";
RL Biochem. Biophys. Res. Commun. 292:300-307(2002).
RN [9]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=12413896; DOI=10.1006/dbio.2002.0810;
RA Yang D.H., Smith E.R., Roland I.H., Sheng Z., He J., Martin W.D.,
RA Hamilton T.C., Lambeth J.D., Xu X.X.;
RT "Disabled-2 is essential for endodermal cell positioning and structure
RT formation during mouse embryogenesis.";
RL Dev. Biol. 251:27-44(2002).
RN [10]
RP FUNCTION.
RX PubMed=11823414; DOI=10.1093/emboj/21.3.211;
RA Rosenbauer F., Kallies A., Scheller M., Knobeloch K.P., Rock C.O.,
RA Schwieger M., Stocking C., Horak I.;
RT "Disabled-2 is transcriptionally regulated by ICSBP and augments macrophage
RT spreading and adhesion.";
RL EMBO J. 21:211-220(2002).
RN [11]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=11927540; DOI=10.1093/emboj/21.7.1555;
RA Morris S.M., Tallquist M.D., Rock C.O., Cooper J.A.;
RT "Dual roles for the Dab2 adaptor protein in embryonic development and
RT kidney transport.";
RL EMBO J. 21:1555-1564(2002).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CLATHRIN AND
RP PHOSPHATIDYLINOSITIDES, AND DOMAIN.
RX PubMed=12234931; DOI=10.1093/emboj/cdf487;
RA Mishra S.K., Keyel P.A., Hawryluk M.J., Agostinelli N.R., Watkins S.C.,
RA Traub L.M.;
RT "Disabled-2 exhibits the properties of a cargo-selective endocytic clathrin
RT adaptor.";
RL EMBO J. 21:4915-4926(2002).
RN [13]
RP INTERACTION WITH DAB2IP.
RX PubMed=12877983; DOI=10.1016/s0169-328x(03)00176-1;
RA Homayouni R., Magdaleno S., Keshvara L., Rice D.S., Curran T.;
RT "Interaction of Disabled-1 and the GTPase activating protein Dab2IP in
RT mouse brain.";
RL Brain Res. Mol. Brain Res. 115:121-129(2003).
RN [14]
RP INTERACTION WITH SH3KBP1.
RX PubMed=14596919; DOI=10.1016/s0014-5793(03)01111-6;
RA Kowanetz K., Terzic J., Dikic I.;
RT "Dab2 links CIN85 with clathrin-mediated receptor internalization.";
RL FEBS Lett. 554:81-87(2003).
RN [15]
RP INTERACTION WITH ITGB3 AND ITGB5.
RX PubMed=12606711; DOI=10.1073/pnas.262791999;
RA Calderwood D.A., Fujioka Y., de Pereda J.M., Garcia-Alvarez B.,
RA Nakamoto T., Margolis B., McGlade C.J., Liddington R.C., Ginsberg M.H.;
RT "Integrin beta cytoplasmic domain interactions with phosphotyrosine-binding
RT domains: a structural prototype for diversity in integrin signaling.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:2272-2277(2003).
RN [16]
RP INTERACTION WITH NOSTRIN.
RX PubMed=15596140; DOI=10.1016/j.bbrc.2004.11.079;
RA Choi Y.-J., Cho S.-Y., Kim H.-W., Kim J.-A., Bae S.-H., Park S.-S.;
RT "Cloning and characterization of mouse disabled 2-interacting protein 2, a
RT mouse orthologue of human NOSTRIN.";
RL Biochem. Biophys. Res. Commun. 326:594-599(2005).
RN [17]
RP FUNCTION, AND INTERACTION WITH ITGB1.
RX PubMed=15734730; DOI=10.1074/jbc.m500974200;
RA Prunier C., Howe P.H.;
RT "Disabled-2 (Dab2) is required for transforming growth factor beta-induced
RT epithelial to mesenchymal transition (EMT).";
RL J. Biol. Chem. 280:17540-17548(2005).
RN [18]
RP FUNCTION, AND INTERACTION WITH MAP3K7.
RX PubMed=15894542; DOI=10.1074/jbc.m501150200;
RA Hocevar B.A., Prunier C., Howe P.H.;
RT "Disabled-2 (Dab2) mediates transforming growth factor beta (TGFbeta)-
RT stimulated fibronectin synthesis through TGFbeta-activated kinase 1 and
RT activation of the JNK pathway.";
RL J. Biol. Chem. 280:25920-25927(2005).
RN [19]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16263760; DOI=10.1242/jcs.02650;
RA Maurer M.E., Cooper J.A.;
RT "Endocytosis of megalin by visceral endoderm cells requires the Dab2
RT adaptor protein.";
RL J. Cell Sci. 118:5345-5355(2005).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [21]
RP FUNCTION, AND MUTAGENESIS OF LYS-53 AND SER-122.
RX PubMed=16984970; DOI=10.1242/jcs.03217;
RA Maurer M.E., Cooper J.A.;
RT "The adaptor protein Dab2 sorts LDL receptors into coated pits
RT independently of AP-2 and ARH.";
RL J. Cell Sci. 119:4235-4246(2006).
RN [22]
RP FUNCTION, AND MUTAGENESIS OF SER-122.
RX PubMed=16870701; DOI=10.1091/mbc.e06-05-0421;
RA Keyel P.A., Mishra S.K., Roth R., Heuser J.E., Watkins S.C., Traub L.M.;
RT "A single common portal for clathrin-mediated endocytosis of distinct cargo
RT governed by cargo-selective adaptors.";
RL Mol. Biol. Cell 17:4300-4317(2006).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323 AND SER-727, AND
RP IDENTIFICATION BY 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 [24]
RP FUNCTION, AND INTERACTION WITH AXIN1 AND PPP1CA.
RX PubMed=19581931; DOI=10.1038/onc.2009.157;
RA Jiang Y., Luo W., Howe P.H.;
RT "Dab2 stabilizes Axin and attenuates Wnt/beta-catenin signaling by
RT preventing protein phosphatase 1 (PP1)-Axin interactions.";
RL Oncogene 28:2999-3007(2009).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-170; SER-193; THR-671;
RP SER-727 AND SER-759, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC 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 [26]
RP FUNCTION.
RX PubMed=20881059; DOI=10.1091/mbc.e09-12-1019;
RA Penheiter S.G., Singh R.D., Repellin C.E., Wilkes M.C., Edens M.,
RA Howe P.H., Pagano R.E., Leof E.B.;
RT "Type II transforming growth factor-beta receptor recycling is dependent
RT upon the clathrin adaptor protein Dab2.";
RL Mol. Biol. Cell 21:4009-4019(2010).
RN [27]
RP INTERACTION WITH FCHO2, AND MUTAGENESIS OF PRO-294 AND PRO-299.
RX PubMed=22323290; DOI=10.1091/mbc.e11-09-0812;
RA Mulkearns E.E., Cooper J.A.;
RT "FCH domain only-2 organizes clathrin-coated structures and interacts with
RT Disabled-2 for low-density lipoprotein receptor endocytosis.";
RL Mol. Biol. Cell 23:1330-1342(2012).
RN [28]
RP INTERACTION WITH EPS15, EPS15L1 AND ITSN1, AND MUTAGENESIS OF PHE-255;
RP PHE-398; PHE-589; PHE-736 AND PHE-765.
RX PubMed=22648170; DOI=10.1091/mbc.e11-12-1007;
RA Teckchandani A., Mulkearns E.E., Randolph T.W., Toida N., Cooper J.A.;
RT "The clathrin adaptor Dab2 recruits EH domain scaffold proteins to regulate
RT integrin beta1 endocytosis.";
RL Mol. Biol. Cell 23:2905-2916(2012).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 33-191, AND MUTAGENESIS OF LYS-53
RP AND LYS-90.
RX PubMed=12826668; DOI=10.1074/jbc.m304384200;
RA Yun M., Keshvara L., Park C.G., Zhang Y.M., Dickerson J.B., Zheng J.,
RA Rock C.O., Curran T., Park H.W.;
RT "Crystal structures of the Dab homology domains of mouse disabled 1 and
RT 2.";
RL J. Biol. Chem. 278:36572-36581(2003).
CC -!- FUNCTION: Adapter protein that functions as clathrin-associated sorting
CC protein (CLASP) required for clathrin-mediated endocytosis of selected
CC cargo proteins. Can bind and assemble clathrin, and binds
CC simultaneously to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2)
CC and cargos containing non-phosphorylated NPXY internalization motifs,
CC such as the LDL receptor, to recruit them to clathrin-coated pits. Can
CC function in clathrin-mediated endocytosis independently of the AP-2
CC complex. Involved in endocytosis of integrin beta-1; this function
CC seems to redundant with the AP-2 complex and seems to require DAB2
CC binding to endocytosis accessory EH domain-containing proteins such as
CC EPS15, EPS15L1 and ITSN1. Involved in endocytosis of cystic fibrosis
CC transmembrane conductance regulator/CFTR. Isoform p96 is involved in
CC endocytosis of megalin/LRP2 lipoprotein receptor during embryonal
CC development. Required for recycling of the TGF-beta receptor. Isoform
CC p67 is not involved in LDL receptor endocytosis. Involved in CFTR
CC trafficking to the late endosome. Involved in several receptor-mediated
CC signaling pathways. Involved in TGF-beta receptor signaling and
CC facilitates phosphorylation of the signal transducer SMAD2. Mediates
CC TFG-beta-stimulated JNK activation. May inhibit the canoniocal
CC Wnt/beta-catenin signaling pathway by stabilizing the beta-catenin
CC destruction complex through a competing association with axin
CC preventing its dephosphorylation through protein phosphatase 1 (PP1).
CC Sequesters LRP6 towards clathrin-mediated endocytosis, leading to
CC inhibition of Wnt/beta-catenin signaling. May activate non-canonical
CC Wnt signaling. In cell surface growth factor/Ras signaling pathways
CC proposed to inhibit ERK activation by interrupting the binding of GRB2
CC to SOS1 and to inhibit SRC by preventing its activating phosphorylation
CC at 'Tyr-419'. Proposed to be involved in modulation of androgen
CC receptor (AR) signaling mediated by SRC activation; seems to compete
CC with AR for interaction with SRC. Plays a role in the CSF-1 signal
CC transduction pathway. Plays a role in cellular differentiation.
CC Involved in cell positioning and formation of visceral endoderm (VE)
CC during embryogenesis and proposed to be required in the VE to respond
CC to Nodal signaling coming from the epiblast. Required for the
CC epithelial to mesenchymal transition, a process necessary for proper
CC embryonic development. May be involved in myeloid cell differentiation
CC and can induce macrophage adhesion and spreading. Isoform p67 may be
CC involved in transcriptional regulation. May act as a tumor suppressor.
CC {ECO:0000269|PubMed:11247302, ECO:0000269|PubMed:11823414,
CC ECO:0000269|PubMed:11927540, ECO:0000269|PubMed:12234931,
CC ECO:0000269|PubMed:12413896, ECO:0000269|PubMed:15734730,
CC ECO:0000269|PubMed:15894542, ECO:0000269|PubMed:16263760,
CC ECO:0000269|PubMed:16870701, ECO:0000269|PubMed:16984970,
CC ECO:0000269|PubMed:19581931, ECO:0000269|PubMed:20881059}.
CC -!- SUBUNIT: Interacts (via NPXY motif) with DAB2 (via PID domain). Can
CC interact (via PID domain) with LDLR, APP, APLP1 and APLP2, and weakly
CC with INPP5D (via NPXY motifs); the interaction is impaired by tyrosine
CC phosphorylation of the respective NPXY motifs. Can weakly interact (via
CC PID domain) with LRP1 (via NPXY motif); the interaction is enhanced by
CC tyrosine phosphorylation of the NPXY motif. Interacts with LRP2 (via
CC NPXY motif); the interaction is not affected by tyrosine
CC phosphorylation of the NPXY motif. Interacts with clathrin; in vitro
CC can assemble clathrin triskelia into polyhedral coats. Interacts with
CC AP2A2, ITGB1, ITGB3, ITGB5, PIAS2, DAB2IP, NOSTRIN, FCHO1, DVL3 and
CC EPS15L1. Interacts with SH3KBP1 (via SH3 domains). Interacts with GRB2;
CC competes with SOS1 for binding to GRB2 and the interaction is enhanced
CC by EGF and NT-3 stimulation. Isoform p96 interacts with EPS15 and
CC ITSN1; isoform p67 does not interact with EPS15 and only weakly
CC interacts with ITSN1. Interacts with MAP3K7; the interaction is induced
CC by TGF-beta stimulation and may mediate TGF-beta stimulated JNK
CC activation. Interacts with AXIN1 and PPP1CA; the interactions are
CC mutually exclusive. Interacts with the globular tail of MYO6. Interacts
CC (via DPF motifs) with FCHO2; the interaction is direct and required for
CC DAB2-mediated LDLR endocytosis. Interacts with LRP6; the interaction
CC involves LRP6 phosphorylation by CK2 and sequesters LRP6 towards
CC clathrin-mediated endocytosis. Associates with the TGF-beta receptor
CC complex (Probable). Interacts with SMAD2 and SMAD3; the interactions
CC are enhanced upon TGF-beta stimulation. Interacts with GRB2; the
CC interaction is enhanced by EGF and NT-3 stimulation. Interacts with
CC SRC; the interaction is enhanced by EGF stimulation.
CC {ECO:0000269|PubMed:11104669, ECO:0000269|PubMed:11247302,
CC ECO:0000269|PubMed:11906161, ECO:0000269|PubMed:12234931,
CC ECO:0000269|PubMed:12606711, ECO:0000269|PubMed:12877983,
CC ECO:0000269|PubMed:14596919, ECO:0000269|PubMed:15596140,
CC ECO:0000269|PubMed:15734730, ECO:0000269|PubMed:15894542,
CC ECO:0000269|PubMed:19581931, ECO:0000269|PubMed:22323290,
CC ECO:0000269|PubMed:22648170, ECO:0000269|PubMed:9569023, ECO:0000305}.
CC -!- INTERACTION:
CC P98078; O35625: Axin1; NbExp=4; IntAct=EBI-1391846, EBI-2365912;
CC P98078; P42567: Eps15; NbExp=2; IntAct=EBI-1391846, EBI-443923;
CC P98078; Q60902: Eps15l1; NbExp=2; IntAct=EBI-1391846, EBI-443931;
CC P98078; P35917: Flt4; NbExp=3; IntAct=EBI-1391846, EBI-7845747;
CC P98078; Q60631: Grb2; NbExp=4; IntAct=EBI-1391846, EBI-1688;
CC P98078; Q9CR95: Necap1; NbExp=2; IntAct=EBI-1391846, EBI-7592476;
CC P98078; Q6WKZ7: Nostrin; NbExp=2; IntAct=EBI-1391846, EBI-1391878;
CC P98078; Q99NH2-1: Pard3; NbExp=2; IntAct=EBI-1391846, EBI-15946047;
CC P98078; Q8C5D8: Pias2; NbExp=2; IntAct=EBI-1391846, EBI-6305825;
CC P98078; O94973: AP2A2; Xeno; NbExp=2; IntAct=EBI-1391846, EBI-1642835;
CC P98078; Q92997: DVL3; Xeno; NbExp=2; IntAct=EBI-1391846, EBI-739789;
CC P98078; Q0JRZ9: FCHO2; Xeno; NbExp=4; IntAct=EBI-1391846, EBI-2609756;
CC P98078; P62993: GRB2; Xeno; NbExp=4; IntAct=EBI-1391846, EBI-401755;
CC P98078; Q9I8D1: MYO6; Xeno; NbExp=2; IntAct=EBI-1391846, EBI-6307292;
CC P98078; Q9UM54: MYO6; Xeno; NbExp=4; IntAct=EBI-1391846, EBI-350606;
CC P98078; Q96B97: SH3KBP1; Xeno; NbExp=9; IntAct=EBI-1391846, EBI-346595;
CC P98078-3; Q8C5D8: Pias2; NbExp=3; IntAct=EBI-6305891, EBI-6305825;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
CC membrane. Membrane, clathrin-coated pit. Note=Colocalizes with large
CC insert-containing isoforms of MYO6 at clathrin-coated pits/vesicles.
CC During mitosis is progressively displaced from the membrane and
CC translocated to the cytoplasm (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform p96]: Membrane, clathrin-coated pit.
CC Note=Colocalizes with LDLR at clathrin-coated pits.
CC -!- SUBCELLULAR LOCATION: [Isoform p67]: Cytoplasm
CC {ECO:0000269|PubMed:11104669}. Nucleus {ECO:0000269|PubMed:11104669}.
CC Note=Diffuse localization in the cytoplasm; does not localize to
CC clathrin-coated pits.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=p96;
CC IsoId=P98078-1; Sequence=Displayed;
CC Name=p93;
CC IsoId=P98078-2; Sequence=VSP_004182;
CC Name=p67;
CC IsoId=P98078-3; Sequence=VSP_004183;
CC -!- TISSUE SPECIFICITY: Isoform p96 and isoform p67 are expressed in adult
CC kidney and fibroblasts with isoform p96 being the predominant form.
CC Isoform p67 is the predominant isoform expressed in embryonic visceral
CC endoderm. {ECO:0000269|PubMed:16263760}.
CC -!- DEVELOPMENTAL STAGE: At 6.5 dpc specifically expressed in the cells of
CC the visceral endoderm. {ECO:0000269|PubMed:11927540,
CC ECO:0000269|PubMed:12413896}.
CC -!- DOMAIN: The PID domain binds to predominantly non-phosphorylated NPXY
CC internalization motifs present in members of the LDLR and APP family;
CC it also mediates simultaneous binding to phosphatidylinositol 4,5-
CC bisphosphate (PubMed:11247302, PubMed:12234931).
CC {ECO:0000269|PubMed:11247302, ECO:0000269|PubMed:12234931}.
CC -!- DOMAIN: The Asn-Pro-Phe (NPF) motifs, which are found in proteins
CC involved in the endocytic pathway, mediate the interaction with the EH
CC domain of EPS15, EPS15R and ITSN1. {ECO:0000269|PubMed:22648170}.
CC -!- PTM: Phosphorylated on serine residues in response to mitogenic growth-
CC factor stimulation. Phosphorylation during mitosis is leading to
CC membrane displacement (By similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethal; embryos arrest prior to
CC gastrulation and show lack of endodermal organization, failure to thin
CC the distal tip visceral endoderm (VE), elongate the extra-embryonic
CC portion of the egg cylinder and properly organize the epiblast. Loss of
CC the specific megalin/LRP2 lipoprotein receptor distribution at the
CC brush border at the apical cell edge in presumptive VE cells.
CC Conditionally mutant mice are overtly normal, but have reduced
CC clathrin-coated pits in kidney proximal tubule cells and excrete
CC specific plasma proteins in the urine, consistent with reduced
CC transport by LRP2 in the proximal tubule. {ECO:0000269|PubMed:11927540,
CC ECO:0000269|PubMed:12413896}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U18869; AAB02646.1; -; mRNA.
DR EMBL; U18869; AAB02647.1; -; mRNA.
DR EMBL; U18869; AAB02645.1; -; mRNA.
DR EMBL; AF260580; AAG44669.1; -; Genomic_DNA.
DR EMBL; AK154716; BAE32784.1; -; mRNA.
DR EMBL; BC016887; AAH16887.1; -; mRNA.
DR EMBL; BC006588; AAH06588.1; -; mRNA.
DR CCDS; CCDS37029.1; -. [P98078-1]
DR CCDS; CCDS37030.1; -. [P98078-3]
DR CCDS; CCDS79357.1; -. [P98078-2]
DR RefSeq; NP_001008702.1; NM_001008702.2.
DR RefSeq; NP_001032994.1; NM_001037905.3.
DR RefSeq; NP_075607.2; NM_023118.5.
DR RefSeq; XP_011243626.1; XM_011245324.1.
DR RefSeq; XP_017171913.1; XM_017316424.1.
DR PDB; 1M7E; X-ray; 2.45 A; A/B/C=33-191.
DR PDB; 1P3R; X-ray; 2.10 A; A/B/C=32-191.
DR PDBsum; 1M7E; -.
DR PDBsum; 1P3R; -.
DR AlphaFoldDB; P98078; -.
DR BMRB; P98078; -.
DR SMR; P98078; -.
DR BioGRID; 199043; 19.
DR DIP; DIP-39422N; -.
DR IntAct; P98078; 53.
DR MINT; P98078; -.
DR STRING; 10090.ENSMUSP00000079689; -.
DR iPTMnet; P98078; -.
DR PhosphoSitePlus; P98078; -.
DR SwissPalm; P98078; -.
DR jPOST; P98078; -.
DR MaxQB; P98078; -.
DR PaxDb; P98078; -.
DR PeptideAtlas; P98078; -.
DR PRIDE; P98078; -.
DR ProteomicsDB; 279873; -. [P98078-1]
DR ProteomicsDB; 279874; -. [P98078-2]
DR ProteomicsDB; 279875; -. [P98078-3]
DR DNASU; 13132; -.
DR GeneID; 13132; -.
DR KEGG; mmu:13132; -.
DR UCSC; uc007vde.1; mouse. [P98078-1]
DR CTD; 1601; -.
DR MGI; MGI:109175; Dab2.
DR eggNOG; KOG3535; Eukaryota.
DR InParanoid; P98078; -.
DR OrthoDB; 279276at2759; -.
DR PhylomeDB; P98078; -.
DR TreeFam; TF316724; -.
DR Reactome; R-MMU-190873; Gap junction degradation.
DR Reactome; R-MMU-196025; Formation of annular gap junctions.
DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 13132; 0 hits in 40 CRISPR screens.
DR ChiTaRS; Dab2; mouse.
DR EvolutionaryTrace; P98078; -.
DR PRO; PR:P98078; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P98078; protein.
DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR GO; GO:0030132; C:clathrin coat of coated pit; IDA:UniProtKB.
DR GO; GO:0005905; C:clathrin-coated pit; ISO:MGI.
DR GO; GO:0030136; C:clathrin-coated vesicle; ISO:MGI.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0035612; F:AP-2 adaptor complex binding; IDA:UniProtKB.
DR GO; GO:0038024; F:cargo receptor activity; IDA:UniProtKB.
DR GO; GO:0035615; F:clathrin adaptor activity; IDA:UniProtKB.
DR GO; GO:0030276; F:clathrin binding; IDA:UniProtKB.
DR GO; GO:0005178; F:integrin binding; IMP:UniProtKB.
DR GO; GO:0050750; F:low-density lipoprotein particle receptor binding; ISO:MGI.
DR GO; GO:0035091; F:phosphatidylinositol binding; IDA:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0046332; F:SMAD binding; ISO:MGI.
DR GO; GO:0000904; P:cell morphogenesis involved in differentiation; IMP:MGI.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISO:MGI.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IDA:UniProtKB.
DR GO; GO:0048268; P:clathrin coat assembly; IDA:UniProtKB.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IMP:MGI.
DR GO; GO:0071425; P:hematopoietic stem cell proliferation; IDA:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0035026; P:leading edge cell differentiation; ISO:MGI.
DR GO; GO:0030099; P:myeloid cell differentiation; IEP:UniProtKB.
DR GO; GO:0060766; P:negative regulation of androgen receptor signaling pathway; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISO:MGI.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IMP:MGI.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISO:MGI.
DR GO; GO:0032091; P:negative regulation of protein binding; ISO:MGI.
DR GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0032349; P:positive regulation of aldosterone biosynthetic process; ISO:MGI.
DR GO; GO:2000860; P:positive regulation of aldosterone secretion; ISO:MGI.
DR GO; GO:0045785; P:positive regulation of cell adhesion; IDA:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
DR GO; GO:2000370; P:positive regulation of clathrin-dependent endocytosis; IDA:UniProtKB.
DR GO; GO:2000643; P:positive regulation of early endosome to late endosome transport; ISO:MGI.
DR GO; GO:0045807; P:positive regulation of endocytosis; ISO:MGI.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IMP:UniProtKB.
DR GO; GO:2001046; P:positive regulation of integrin-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IDA:GO_Central.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IMP:UniProtKB.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0002092; P:positive regulation of receptor internalization; IMP:CACAO.
DR GO; GO:0001921; P:positive regulation of receptor recycling; IMP:UniProtKB.
DR GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; ISO:MGI.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IMP:UniProtKB.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; ISO:MGI.
DR GO; GO:2000096; P:positive regulation of Wnt signaling pathway, planar cell polarity pathway; ISO:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IBA:GO_Central.
DR GO; GO:2000298; P:regulation of Rho-dependent protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0097017; P:renal protein absorption; IMP:MGI.
DR GO; GO:0048545; P:response to steroid hormone; ISO:MGI.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR006020; PTB/PI_dom.
DR Pfam; PF00640; PID; 1.
DR SMART; SM00462; PTB; 1.
DR PROSITE; PS01179; PID; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Apoptosis; Coated pit;
KW Cytoplasm; Cytoplasmic vesicle; Developmental protein; Differentiation;
KW Endocytosis; Membrane; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Transport; Wnt signaling pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P98082"
FT CHAIN 2..766
FT /note="Disabled homolog 2"
FT /id="PRO_0000079771"
FT DOMAIN 45..196
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..447
FT /note="Required for localization to clathrin-coated pits"
FT REGION 284..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..730
FT /note="Sufficient for interaction with GRB2"
FT /evidence="ECO:0000269|PubMed:9569023"
FT REGION 617..625
FT /note="Required for interaction with CSK"
FT /evidence="ECO:0000250"
FT REGION 647..766
FT /note="Required for interaction with MYO6"
FT /evidence="ECO:0000269|PubMed:11906161"
FT REGION 659..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..669
FT /note="Required for interaction with GRB2 and CSK"
FT /evidence="ECO:0000250"
FT REGION 699..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..723
FT /note="Sufficient for interaction with SH3KBP1 SH3 domain"
FT MOTIF 293..295
FT /note="DPF 1"
FT MOTIF 298..300
FT /note="DPF 2"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..612
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..627
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..757
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P98082"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88797"
FT MOD_RES 170
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 326
FT /note="Phosphoserine; in mitosis"
FT /evidence="ECO:0000250|UniProtKB:O88797"
FT MOD_RES 328
FT /note="Phosphoserine; in mitosis"
FT /evidence="ECO:0000250|UniProtKB:O88797"
FT MOD_RES 401
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P98082"
FT MOD_RES 671
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 727
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 759
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 209..229
FT /note="Missing (in isoform p93)"
FT /evidence="ECO:0000303|PubMed:7775479"
FT /id="VSP_004182"
FT VAR_SEQ 230..447
FT /note="Missing (in isoform p67)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:7775479"
FT /id="VSP_004183"
FT MUTAGEN 53
FT /note="K->A: Abolishes binding to PtdIns(4,5)P2."
FT /evidence="ECO:0000269|PubMed:12826668,
FT ECO:0000269|PubMed:16984970"
FT MUTAGEN 53
FT /note="K->Q: Abolishes LDLR endocytosis."
FT /evidence="ECO:0000269|PubMed:12826668,
FT ECO:0000269|PubMed:16984970"
FT MUTAGEN 90
FT /note="K->A: Abolishes binding to PtdIns(4,5)P2."
FT /evidence="ECO:0000269|PubMed:12826668"
FT MUTAGEN 122
FT /note="S->T: Abolishes LDLR endocytosis."
FT /evidence="ECO:0000269|PubMed:16870701,
FT ECO:0000269|PubMed:16984970"
FT MUTAGEN 122
FT /note="S->Y: Impairs LDLR endocytosis."
FT /evidence="ECO:0000269|PubMed:16870701,
FT ECO:0000269|PubMed:16984970"
FT MUTAGEN 255
FT /note="F->V: Abolishes interaction with ITSN1, fails to
FT internalize integrin beta-1; when associated with V-398, V-
FT 589, V-736 and V-765."
FT /evidence="ECO:0000269|PubMed:22648170"
FT MUTAGEN 294
FT /note="P->A: Loss of interaction with FCHO2; when
FT associated with A-299."
FT /evidence="ECO:0000269|PubMed:22323290"
FT MUTAGEN 299
FT /note="P->A: Loss of interaction with FCHO2; when
FT associated with A-294."
FT /evidence="ECO:0000269|PubMed:22323290"
FT MUTAGEN 398
FT /note="F->V: Abolishes interaction with ITSN1, fails to
FT internalize integrin beta-1; when associated with V-255, V-
FT 589, V-736 and V-765."
FT /evidence="ECO:0000269|PubMed:22648170"
FT MUTAGEN 589
FT /note="F->V: Abolishes interaction with EPS15 and impairs
FT interaction with ITSN1, fails to internalize integrin beta-
FT 1; when associated with V-736 and V-765. Abolishes
FT interaction with ITSN1; when associated with V-255, V-398,
FT V-736 and V-765."
FT /evidence="ECO:0000269|PubMed:22648170"
FT MUTAGEN 736
FT /note="F->V: Abolishes interaction with EPS15 and impairs
FT interaction with ITSN1, fails to internalize integrin beta-
FT 1; when associated with V-589 and V-765. Abolishes
FT interaction with ITSN1; when associated with V-255, V-398,
FT V-589, and V-765."
FT /evidence="ECO:0000269|PubMed:22648170"
FT MUTAGEN 765
FT /note="F->V: Abolishes interaction with EPS15 and impairs
FT interaction with ITSN1, fails to internalize integrin beta-
FT 1; when associated with V-589 and V-736. Abolishes
FT interaction with ITSN1; when associated with V-255, V-398,
FT V-589 and V-736."
FT /evidence="ECO:0000269|PubMed:22648170"
FT CONFLICT 10
FT /note="T -> A (in Ref. 4; AAH06588)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="D -> G (in Ref. 4; AAH06588)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="G -> V (in Ref. 1; AAB02646/AAB02645)"
FT /evidence="ECO:0000305"
FT CONFLICT 454
FT /note="L -> P (in Ref. 1; AAB02645/AAB02646/AAB02647 and 2;
FT AAG44669)"
FT /evidence="ECO:0000305"
FT CONFLICT 490
FT /note="A -> P (in Ref. 1; AAB02645/AAB02646/AAB02647 and 2;
FT AAG44669)"
FT /evidence="ECO:0000305"
FT CONFLICT 536
FT /note="R -> G (in Ref. 3; BAE32784 and 4; AAH16887/
FT AAH06588)"
FT /evidence="ECO:0000305"
FT CONFLICT 553
FT /note="S -> P (in Ref. 4; AAH06588)"
FT /evidence="ECO:0000305"
FT HELIX 36..43
FT /evidence="ECO:0007829|PDB:1P3R"
FT STRAND 48..63
FT /evidence="ECO:0007829|PDB:1P3R"
FT HELIX 66..84
FT /evidence="ECO:0007829|PDB:1P3R"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:1P3R"
FT STRAND 91..98
FT /evidence="ECO:0007829|PDB:1P3R"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:1P3R"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:1P3R"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:1P3R"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:1P3R"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:1P3R"
FT STRAND 133..140
FT /evidence="ECO:0007829|PDB:1P3R"
FT STRAND 144..153
FT /evidence="ECO:0007829|PDB:1P3R"
FT HELIX 156..177
FT /evidence="ECO:0007829|PDB:1P3R"
SQ SEQUENCE 766 AA; 82312 MW; 856C946BD43C4B07 CRC64;
MSNEVETSTT NGQPDQQAAP KAPSKKEKKK GSEKTDEYLL ARFKGDGVKY KAKLIGIDDV
PDARGDKMSQ DSMMKLKGMA AAGRSQGQHK QRIWVNISLS GIKIIDEKTG VIEHEHPVNK
ISFIARDVTD NRAFGYVCGG EGQHQFFAIK TGQQAEPLVV DLKDLFQVIY NVKKKEEDKK
KVEEANKAEE NGSEALMTLD DQANKLKLGV DQMDLFGDMS TPPDLNSPTE SKDILLVDLN
SEIDTNQNSL RENPFLTNGV TSCSLPRPKP QASFLPENAF SANLNFFPTP NPDPFRDDPF
AQPDQSAPSS FDSLTSPDQK KASLSSSSTP QSKGPLNGDT DYFGQQFDQL SNRTGKPEAQ
GGPWPYPSSQ TQQAVRTQNG VSEREQNGFH IKSSPNPFVG SPPKGLSVPN GVKQDLESSV
QSSAHDSIAI IPPPQSTKPG RGRRTAKSSA NDLLASDIFA SEPPGQMSPT GQPAVPQSNF
LDLFKGNAPA PVGPLVGLGT VPVTPPQAGP WTPVVYSPST TVVPGAIISG QPPSFRQPLV
FGTTPAVQVW NQSPSFATPA SPPPPTVWCP TTSVAPNAWS STSPLGNPFQ SNNIFPPPTM
STQSSPQPMM SSVLATPPQP PPRNGPLKDI PSDAFTGLDP LGDKEVKEVK EMFKDFQLRQ
PPLVPSRKGE TPPSGTSSAF SSYFNNKVGI PQEHVDHDDF DANQLLNKIN EPPKPAPRQG
VLLGTKSADN SLENPFSKGF SSSNPSVVSQ PASSDPHRSP FGNPFA
