DP13B_MOUSE
ID DP13B_MOUSE Reviewed; 662 AA.
AC Q8K3G9; Q99LT7;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=DCC-interacting protein 13-beta {ECO:0000250|UniProtKB:Q8NEU8};
DE Short=Dip13-beta {ECO:0000303|Ref.1};
DE AltName: Full=Adapter protein containing PH domain, PTB domain and leucine zipper motif 2 {ECO:0000305};
GN Name=Appl2 {ECO:0000312|MGI:MGI:2384914};
GN Synonyms=Dip13b, Dip3b {ECO:0000312|EMBL:AAH02232.1,
GN ECO:0000312|MGI:MGI:2384914};
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] {ECO:0000312|EMBL:AAM55532.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Chen Y.Q.;
RT "Cloning of mouse DIP13 alpha and beta.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAH48906.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH48906.1};
RC TISSUE=Colon {ECO:0000312|EMBL:AAH48906.1}, and
RC Mammary tumor {ECO:0000312|EMBL:AAH02232.1};
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 [3]
RP INTERACTION WITH APPL1; ADIPOR1 AND ADIPOR2, DOMAIN, TISSUE SPECIFICITY,
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19661063; DOI=10.1074/jbc.m109.010355;
RA Wang C., Xin X., Xiang R., Ramos F.J., Liu M., Lee H.J., Chen H., Mao X.,
RA Kikani C.K., Liu F., Dong L.Q.;
RT "Yin-Yang regulation of adiponectin signaling by APPL isoforms in muscle
RT cells.";
RL J. Biol. Chem. 284:31608-31615(2009).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, Pancreas, 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 [5]
RP INDUCTION, DISRUPTION PHENOTYPE, INTERACTION WITH PIK3R1 AND APPL1, AND
RP FUNCTION.
RX PubMed=25328665; DOI=10.1186/2045-3701-4-60;
RA Mao L., Lin W., Nie T., Hui X., Gao X., Li K., Ding M., Tang X., Li P.,
RA Wang Y., Xu A., Liu P., Wu D.;
RT "Absence of Appl2 sensitizes endotoxin shock through activation of PI3K/Akt
RT pathway.";
RL Cell Biosci. 4:60-60(2014).
RN [6]
RP DISRUPTION PHENOTYPE, INTERACTION WITH TBC1D1, AND DOMAIN.
RX PubMed=24879834; DOI=10.2337/db14-0337;
RA Cheng K.K., Zhu W., Chen B., Wang Y., Wu D., Sweeney G., Wang B., Lam K.S.,
RA Xu A.;
RT "The adaptor protein APPL2 inhibits insulin-stimulated glucose uptake by
RT interacting with TBC1D1 in skeletal muscle.";
RL Diabetes 63:3748-3758(2014).
RN [7]
RP INTERACTION WITH RAB31 AND RAB5A, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=25568335; DOI=10.1091/mbc.e14-10-1457;
RA Yeo J.C., Wall A.A., Luo L., Stow J.L.;
RT "Rab31 and APPL2 enhance FcgammaR-mediated phagocytosis through PI3K/Akt
RT signaling in macrophages.";
RL Mol. Biol. Cell 26:952-965(2015).
RN [8]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=26445298; DOI=10.1002/jcp.25211;
RA Tan Y., Xin X., Coffey F.J., Wiest D.L., Dong L.Q., Testa J.R.;
RT "Appl1 and Appl2 are Expendable for Mouse Development But Are Essential for
RT HGF-Induced Akt Activation and Migration in Mouse Embryonic Fibroblasts.";
RL J. Cell. Physiol. 231:1142-1150(2016).
RN [9]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=27219021; DOI=10.1111/tra.12415;
RA Yeo J.C., Wall A.A., Luo L., Condon N.D., Stow J.L.;
RT "Distinct Roles for APPL1 and APPL2 in Regulating Toll-like Receptor 4
RT Signaling in Macrophages.";
RL Traffic 17:1014-1026(2016).
RN [10]
RP FUNCTION.
RX PubMed=28965332; DOI=10.1007/s12035-017-0785-y;
RA Gao C., Chen X., Xu A., Cheng K., Shen J.;
RT "Adaptor Protein APPL2 Affects Adult Antidepressant Behaviors and
RT Hippocampal Neurogenesis via Regulating the Sensitivity of Glucocorticoid
RT Receptor.";
RL Mol. Neurobiol. 55:5537-5547(2018).
RN [11]
RP FUNCTION.
RX PubMed=29675572; DOI=10.1007/s12035-018-1042-8;
RA Gao C., Du Q., Li W., Deng R., Wang Q., Xu A., Shen J.;
RT "Baicalin Modulates APPL2/Glucocorticoid Receptor Signaling Cascade,
RT Promotes Neurogenesis, and Attenuates Emotional and Olfactory Dysfunctions
RT in Chronic Corticosterone-Induced Depression.";
RL Mol. Neurobiol. 55:9334-9348(2018).
RN [12]
RP TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=29467283; DOI=10.15252/embr.201744977;
RA Wang B., Li A., Li X., Ho P.W., Wu D., Wang X., Liu Z., Wu K.K., Yau S.S.,
RA Xu A., Cheng K.K.;
RT "Activation of hypothalamic RIP-Cre neurons promotes beiging of WAT via
RT sympathetic nervous system.";
RL EMBO Rep. 19:0-0(2018).
CC -!- FUNCTION: Multifunctional adapter protein that binds to various
CC membrane receptors, nuclear factors and signaling proteins to regulate
CC many processes, such as cell proliferation, immune response, endosomal
CC trafficking and cell metabolism (PubMed:25568335, PubMed:27219021,
CC PubMed:25328665, PubMed:19661063, PubMed:29467283). Regulates signaling
CC pathway leading to cell proliferation through interaction with RAB5A
CC and subunits of the NuRD/MeCP1 complex (By similarity). Plays a role in
CC immune response by modulating phagocytosis, inflammatory and innate
CC immune responses (PubMed:25568335, PubMed:27219021, PubMed:25328665).
CC In macrophages, enhances Fc-gamma receptor-mediated phagocytosis
CC through interaction with RAB31 leading to activation of PI3K/Akt
CC signaling (PubMed:25568335). In response to LPS, modulates inflammatory
CC responses by playing a key role on the regulation of TLR4 signaling and
CC in the nuclear translocation of RELA/NF-kappa-B p65 and the secretion
CC of pro- and anti-inflammatory cytokines (PubMed:27219021). Also
CC functions as a negative regulator of innate immune response via
CC inhibition of AKT1 signaling pathway by forming a complex with APPL1
CC and PIK3R1 (PubMed:25328665). Plays a role in endosomal trafficking of
CC TGFBR1 from the endosomes to the nucleus (By similarity). plays a role
CC in cell metabolism by regulating adiponecting ans insulin signaling
CC pathways and adaptative thermogenesis (PubMed:19661063,
CC PubMed:29467283) (By similarity). In muscle, negatively regulates
CC adiponectin-simulated glucose uptake and fatty acid oxidation by
CC inhibiting adiponectin signaling pathway through APPL1 sequestration
CC thereby antagonizing APPL1 action (PubMed:19661063). In muscles,
CC negativeliy regulates insulin-induced plasma membrane recruitment of
CC GLUT4 and glucose uptake through interaction with TBC1D1 (By
CC similarity). Plays a role in cold and diet-induced adaptive
CC thermogenesis by activating ventromedial hypothalamus (VMH) neurons
CC throught AMPK inhibition which enhances sympathetic outflow to
CC subcutaneous white adipose tissue (sWAT), sWAT beiging and cold
CC tolerance (PubMed:29467283). Also plays a role in other signaling
CC pathways namely Wnt/beta-catenin, HGF and glucocorticoid receptor
CC signaling (PubMed:28965332, PubMed:29675572, PubMed:26445298). Positive
CC regulator of beta-catenin/TCF-dependent transcription through direct
CC interaction with RUVBL2/reptin resulting in the relief of RUVBL2-
CC mediated repression of beta-catenin/TCF target genes by modulating the
CC interactions within the beta-catenin-reptin-HDAC complex (By
CC similarity). May affect adult neurogenesis in hippocampus and olfactory
CC system via regulating the sensitivity of glucocorticoid receptor
CC (PubMed:28965332, PubMed:29675572). Required for fibroblast migration
CC through HGF cell signaling (PubMed:26445298).
CC {ECO:0000250|UniProtKB:Q8NEU8, ECO:0000269|PubMed:19661063,
CC ECO:0000269|PubMed:25328665, ECO:0000269|PubMed:25568335,
CC ECO:0000269|PubMed:26445298, ECO:0000269|PubMed:27219021,
CC ECO:0000269|PubMed:28965332, ECO:0000269|PubMed:29467283,
CC ECO:0000269|PubMed:29675572}.
CC -!- SUBUNIT: Homodimer. Homotetramer (By similarity). Binds RAB5A/Rab5
CC through an N-terminal domain (PubMed:25568335). This interaction is
CC essential for its recruitment to endosomal membranes as well as its
CC role in cell proliferation. Binds subunits of the NuRD/MeCP1 complex
CC (By similarity). Interacts with FSHR; interaction is independent of
CC follicle stimulating hormone stimulation (By similarity). Interacts
CC with APPL1; the interaction is decreased by adiponectin in a time-
CC dependent manner (PubMed:19661063, PubMed:25328665). Forms a complex
CC comprising APPL1, RUVBL2, CTNNB1, HDAC1 and HDAC2; interaction reduces
CC interaction between CTNNB1, HDAC1, HDAC2 and RUVBL2 leading to the
CC decrease of deacetylase activity of this complex; affects the
CC recruitment of repressive complexes to the Wnt target genes (By
CC similarity). Interacts (via BAR domain) with TBC1D1; interaction is
CC dependent of TBC1D1 phosphorylation at 'Ser-235'; interaction
CC diminishes the phosphorylation of TBC1D1 at 'Thr-596', resulting in
CC inhibition of SLC2A4 translocation and glucose uptake
CC (PubMed:24879834). Interacts with ANXA2; targets APPL2 to endosomes and
CC acting in parallel to RAB5A (By similarity). Interacts with RAB31 (in
CC GTP-bound form); interaction contributes to or enhances recruitment of
CC APPL2 to the phagosomes; interaction enhances Fc-gamma receptor-
CC mediated phagocytosis through PI3K/Akt signaling in macrophages
CC (PubMed:25568335). Interacts with PIK3R1; forms a complex with PIK3R1
CC and APPL1 (PubMed:25328665). Interacts (via BAR domain) with ADIPOR1;
CC hinders the accessibility of APPL1 to ADIPOR1; negatively regulates
CC adiponectin signaling; ADIPOQ dissociates this interaction and
CC facilitates the recruitment of APPL1 to ADIPOR1 (PubMed:19661063).
CC Interacts (via BAR domain) with ADIPOR2; ADIPOQ dissociates this
CC interaction (PubMed:19661063). {ECO:0000250|UniProtKB:Q8NEU8,
CC ECO:0000269|PubMed:19661063, ECO:0000269|PubMed:24879834,
CC ECO:0000269|PubMed:25328665, ECO:0000269|PubMed:25568335}.
CC -!- INTERACTION:
CC Q8K3G9; Q60949: Tbc1d1; NbExp=2; IntAct=EBI-647007, EBI-21012140;
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000250|UniProtKB:Q8NEU8}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q8NEU8}. Nucleus {ECO:0000250|UniProtKB:Q8NEU8}.
CC Cell membrane {ECO:0000250|UniProtKB:Q8NEU8}. Endosome membrane
CC {ECO:0000250|UniProtKB:Q8NEU8}. Cytoplasm {ECO:0000269|PubMed:19661063,
CC ECO:0000269|PubMed:25568335}. Cytoplasmic vesicle, phagosome
CC {ECO:0000269|PubMed:25568335}. Cell projection, ruffle
CC {ECO:0000269|PubMed:25568335}. Cell projection, ruffle membrane
CC {ECO:0000269|PubMed:27219021}. Cell membrane
CC {ECO:0000269|PubMed:27219021}. Cytoplasmic vesicle, phagosome membrane
CC {ECO:0000269|PubMed:27219021}. Note=Early endosomal membrane-bound and
CC nuclear. Translocated into the nucleus upon release from endosomal
CC membranes following internalization of EGF (By similarity). Associates
CC dynamically with cytoplasmic membrane structures that undergo changes
CC in shape, movement, fusion and fission events. PI(4,5)P2 levels are
CC important for membrane association of APPL2 (By similarity). Absent of
CC endosome in macrophage. Colocalized with RAB31 at early-stage phagosome
CC (PubMed:25568335). Localized on macropinosomes in LPS-activated
CC macrophages. Associated with membrane domains in contact with pathogens
CC and pathogen-derived ligands like LPS. First recruited to the ruffles,
CC and accumulates on macropinosomes (PubMed:27219021).
CC {ECO:0000250|UniProtKB:Q8NEU8, ECO:0000269|PubMed:25568335,
CC ECO:0000269|PubMed:27219021}.
CC -!- TISSUE SPECIFICITY: Expressed in insulin-target tissues including
CC skeletal muscle, liver, fat, and brain. Highly expressed in kidney and
CC pancreas (PubMed:19661063). Abundantly expressed in the ventromedial
CC hypothalamus (VMH), barely detectable in the arcuate nucleus (ARC) and
CC paraventricular nucleus (PVN) of the hypothalamus. Also expressed in
CC pancreatic beta-cells (PubMed:29467283). {ECO:0000269|PubMed:19661063,
CC ECO:0000269|PubMed:29467283}.
CC -!- INDUCTION: Decreases steadily in response to lipopolysaccharide (LPS).
CC {ECO:0000269|PubMed:25328665}.
CC -!- DOMAIN: The BAR domain is necessary and sufficient for mediating
CC homotypic and heterotypic interactions; associates with cytoplasmic
CC membrane structures; mediates interaction with TBC1D1 and ADIPOR1
CC (PubMed:24879834, PubMed:19661063). The PH and PID domains mediate
CC phosphoinositide binding. The PID domain mediates phosphatidylserine
CC binding and allows localization to cytosolic membrane structures and
CC nucleus. The PH domain allows localization to the plasma membrane,
CC cytosolic vesicles and distinct nuclear and perinuclear structures and
CC is sufficient for RUVBL2 interaction (By similarity).
CC {ECO:0000250|UniProtKB:Q8NEU8, ECO:0000269|PubMed:19661063,
CC ECO:0000269|PubMed:24879834}.
CC -!- DISRUPTION PHENOTYPE: Mice have normal food intake, body weight, and
CC fasting glucose and insulin levels (PubMed:24879834). Mice are viable
CC and grow normally to adulthood (PubMed:26445298). Appl1 and Appl2
CC double knockout mice are viable and grossly normal with regard to
CC reproductive potential and postnatal growth (PubMed:26445298). Reduced
CC survival rate after injection of LPS (PubMed:25328665). Conditional
CC knockout mice Appl2 in pancreatic beta-cells and/or ventromedial
CC hypothalamus (VMH) have no obvious effect on circulating level of
CC insulin, body weight, food intake, respiratory exchange ratio (RER),
CC and locomotor activity, but gradually increased adiposity and
CC diminished energy expenditure. Mice exhibit cold intolerance and
CC impairment of cold-induced thermogenesis, beiging program, and SNS
CC outflow in subcutaneous white adipose tissue (sWAT). Conditionnal
CC knockout mice Appl2 in ventromedial hypothalamus (VMH) have the same
CC phenotype as above (PubMed:29467283). {ECO:0000269|PubMed:24879834,
CC ECO:0000269|PubMed:25328665, ECO:0000269|PubMed:26445298,
CC ECO:0000269|PubMed:29467283}.
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DR EMBL; AY113706; AAM55532.1; -; mRNA.
DR EMBL; BC002232; AAH02232.1; -; mRNA.
DR EMBL; BC048906; AAH48906.1; -; mRNA.
DR CCDS; CCDS24078.1; -.
DR RefSeq; NP_660255.1; NM_145220.2.
DR AlphaFoldDB; Q8K3G9; -.
DR SMR; Q8K3G9; -.
DR BioGRID; 229720; 7.
DR IntAct; Q8K3G9; 3.
DR STRING; 10090.ENSMUSP00000020500; -.
DR iPTMnet; Q8K3G9; -.
DR PhosphoSitePlus; Q8K3G9; -.
DR EPD; Q8K3G9; -.
DR MaxQB; Q8K3G9; -.
DR PaxDb; Q8K3G9; -.
DR PRIDE; Q8K3G9; -.
DR ProteomicsDB; 277376; -.
DR Antibodypedia; 30637; 158 antibodies from 22 providers.
DR DNASU; 216190; -.
DR Ensembl; ENSMUST00000020500; ENSMUSP00000020500; ENSMUSG00000020263.
DR GeneID; 216190; -.
DR KEGG; mmu:216190; -.
DR UCSC; uc007gkk.1; mouse.
DR CTD; 55198; -.
DR MGI; MGI:2384914; Appl2.
DR VEuPathDB; HostDB:ENSMUSG00000020263; -.
DR eggNOG; KOG0521; Eukaryota.
DR eggNOG; KOG3536; Eukaryota.
DR GeneTree; ENSGT00940000158319; -.
DR HOGENOM; CLU_025935_0_0_1; -.
DR InParanoid; Q8K3G9; -.
DR OMA; ENDEWIC; -.
DR OrthoDB; 253010at2759; -.
DR PhylomeDB; Q8K3G9; -.
DR TreeFam; TF328669; -.
DR BioGRID-ORCS; 216190; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Appl2; mouse.
DR PRO; PR:Q8K3G9; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8K3G9; protein.
DR Bgee; ENSMUSG00000020263; Expressed in pigmented layer of retina and 270 other tissues.
DR ExpressionAtlas; Q8K3G9; baseline and differential.
DR Genevisible; Q8K3G9; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032009; C:early phagosome; IDA:UniProtKB.
DR GO; GO:0036186; C:early phagosome membrane; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR GO; GO:0044354; C:macropinosome; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0001726; C:ruffle; IDA:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
DR GO; GO:0031982; C:vesicle; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
DR GO; GO:0001786; F:phosphatidylserine binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0033211; P:adiponectin-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0008283; P:cell population proliferation; ISO:MGI.
DR GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; IMP:UniProtKB.
DR GO; GO:0009631; P:cold acclimation; IMP:UniProtKB.
DR GO; GO:0002024; P:diet induced thermogenesis; IMP:UniProtKB.
DR GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
DR GO; GO:1900077; P:negative regulation of cellular response to insulin stimulus; IMP:UniProtKB.
DR GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; IMP:UniProtKB.
DR GO; GO:0046322; P:negative regulation of fatty acid oxidation; IMP:UniProtKB.
DR GO; GO:0046325; P:negative regulation of glucose import; IMP:UniProtKB.
DR GO; GO:2000178; P:negative regulation of neural precursor cell proliferation; IMP:UniProtKB.
DR GO; GO:0050768; P:negative regulation of neurogenesis; IMP:UniProtKB.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:UniProtKB.
DR GO; GO:1905451; P:positive regulation of Fc-gamma receptor signaling pathway involved in phagocytosis; IMP:UniProtKB.
DR GO; GO:1905303; P:positive regulation of macropinocytosis; IMP:UniProtKB.
DR GO; GO:0060100; P:positive regulation of phagocytosis, engulfment; IMP:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR GO; GO:0006606; P:protein import into nucleus; ISS:UniProtKB.
DR GO; GO:0010762; P:regulation of fibroblast migration; IMP:UniProtKB.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0045088; P:regulation of innate immune response; IMP:UniProtKB.
DR GO; GO:0034143; P:regulation of toll-like receptor 4 signaling pathway; IMP:UniProtKB.
DR GO; GO:0023052; P:signaling; IBA:GO_Central.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
DR Gene3D; 1.20.1270.60; -; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR006020; PTB/PI_dom.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00640; PID; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00462; PTB; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS01179; PID; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell membrane; Cell projection; Cytoplasm; Cytoplasmic vesicle;
KW Endosome; Membrane; Nucleus; Reference proteome.
FT CHAIN 1..662
FT /note="DCC-interacting protein 13-beta"
FT /id="PRO_0000079988"
FT DOMAIN 3..268
FT /note="BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT DOMAIN 277..375
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 486..635
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT REGION 1..428
FT /note="Required for RAB5A binding"
FT /evidence="ECO:0000250"
FT REGION 642..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 428
FT /note="V -> D (in Ref. 2; AAH02232)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 662 AA; 73854 MW; 8917BDE1CF13FC3B CRC64;
MPAVDKLLLE EALQDSPQAR SLLSVFEEDA GTLTDYTNQL LQAMQRVYGA QNEMCLATQQ
LSRQLLAYEK QNFALGKGDE EVISTLHYFS KVMDELNGLH TELAKQLADT MVLPVIQFRE
KDLTEVSTLK DLFGLASSEH DLSMAKYSRL PKKKENEKAK TEIVKEVAAA RRKQHLSSLQ
YYCALNALQY RKRAAMMEPL IGFAHGQINF FKRGAEMFSK SMDGFLSSVK DMVQSIQVEL
EAEADKMRVS QQELLSVSES VYTPDIDVAT AQINRNLIQK TGYLNLRNKT GLVTTTWERL
YFFTQGGNLM CQPRGAVAGG LIQDLDNCSV MAVDCEDRRY CFQISTPSGK PGIILQAESR
KEYEEWICAV NNISRQIYLT DNPEAVAIKL NQTALQAVTP ITSFGKKQES SCSSQNIKNS
DIEDDNIVPK ATASIPETEE LIAPGTPIQF DIVLPATEFL DQNRGGRRTN PFGETEDGSF
PEAEDSLLQQ MFIVRFLGSM AVKTDSTAEV IYEAMRQVLA ARAIHNIFRM TESHLMVTSQ
TLRLIDPQTQ VSRACFELTS VTQFAAHQEN KRLVGFVIRV PESTGEESLS TYIFESNSEG
EKICYAINLG KEIIEVQKDP EALARLMLSV PLTNDGKYVL LNDQADDTGG SPSENRGAES
EA
