DP13A_MOUSE
ID DP13A_MOUSE Reviewed; 707 AA.
AC Q8K3H0; Q3UJP7; Q69ZJ9; Q8BWZ8; Q8VCJ8; Q9CUW4;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=DCC-interacting protein 13-alpha {ECO:0000305};
DE Short=Dip13-alpha {ECO:0000303|Ref.1};
DE AltName: Full=Adapter protein containing PH domain, PTB domain and leucine zipper motif 1 {ECO:0000305};
GN Name=Appl1 {ECO:0000312|MGI:MGI:1920243};
GN Synonyms=Dip13a, Kiaa1428 {ECO:0000312|EMBL:BAD32447.1};
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:AAM55531.1}
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and DBA/2J;
RC TISSUE=Cecum, Corpora quadrigemina, Embryonic stem cell, and Hippocampus;
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 [3] {ECO:0000312|EMBL:AAH63751.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Limb {ECO:0000312|EMBL:AAH63751.1}, and Mammary gland;
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] {ECO:0000305, ECO:0000312|EMBL:BAD32447.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 485-707.
RC TISSUE=Pancreatic islet;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [6]
RP IDENTIFICATION BY 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 INTERACTION WITH ADIPOR1, AND TISSUE SPECIFICITY.
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-691 AND SER-694, AND
RP 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 [9]
RP INTERACTION WITH OCRL.
RX PubMed=20133602; DOI=10.1073/pnas.0914658107;
RA Swan L.E., Tomasini L., Pirruccello M., Lunardi J., De Camilli P.;
RT "Two closely related endocytic proteins that share a common OCRL-binding
RT motif with APPL1.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:3511-3516(2010).
RN [10]
RP INTERACTION WITH NTRK2, AND SUBCELLULAR LOCATION.
RX PubMed=21849472; DOI=10.1091/mbc.e11-04-0308;
RA Fu X., Yang Y., Xu C., Niu Y., Chen T., Zhou Q., Liu J.J.;
RT "Retrolinkin cooperates with endophilin A1 to mediate BDNF-TrkB early
RT endocytic trafficking and signaling from early endosomes.";
RL Mol. Biol. Cell 22:3684-3698(2011).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH PIK3R1 AND APPL2.
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 [12]
RP 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 [13]
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 [14]
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).
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 (By similarity) (PubMed:25328665,
CC PubMed:25568335, PubMed:27219021). Regulates signaling pathway leading
CC to cell proliferation through interaction with RAB5A and subunits of
CC the NuRD/MeCP1 complex (By similarity). Functions as a positive
CC regulator of innate immune response via activation of AKT1 signaling
CC pathway by forming a complex with APPL1 and PIK3R1 (PubMed:25328665).
CC Inhibits Fc-gamma receptor-mediated phagocytosis through PI3K/Akt
CC signaling in macrophages (PubMed:25568335). Regulates TLR4 signaling in
CC activated macrophages (PubMed:27219021). Involved in trafficking of the
CC TGFBR1 from the endosomes to the nucleus via microtubules in a TRAF6-
CC dependent manner. Plays a role in cell metabolism by regulating
CC adiponecting and insulin signaling pathways (By similarity). Required
CC for fibroblast migration through HGF cell signaling (PubMed:26445298).
CC Positive regulator of beta-catenin/TCF-dependent transcription through
CC direct interaction with RUVBL2/reptin resulting in the relief of
CC RUVBL2-mediated repression of beta-catenin/TCF target genes by
CC modulating the interactions within the beta-catenin-reptin-HDAC complex
CC (By similarity). {ECO:0000250|UniProtKB:Q9UKG1,
CC ECO:0000269|PubMed:25328665, ECO:0000269|PubMed:25568335,
CC ECO:0000269|PubMed:26445298, ECO:0000269|PubMed:27219021}.
CC -!- SUBUNIT: Homodimer. Binds RAB5A/Rab5 through an N-terminal domain. This
CC interaction is essential for its recruitment to endosomal membranes as
CC well as its role in cell proliferation. Binds DCC and the catalytic
CC domain of the inactive form of AKT2 through its PID domain. Binds
CC PIK3CA and subunits of the NuRD/MeCP1 complex (By similarity).
CC Interacts with OCRL and INPP5B (PubMed:20133602) (By similarity).
CC Interacts with NTRK2 (PubMed:21849472). Interacts with APPL2;
CC interaction is independent of follicle stimulating hormone stimulation;
CC interaction is decreased by adiponectin in a time-dependent manner
CC (PubMed:25328665). Forms a complex with APPL2 and RUVBL2. Forms a
CC complex comprising APPL2, RUVBL2, CTNNB1, HDAC1 and HDAC2; interaction
CC reduces interaction between CTNNB1, HDAC1, HDAC2 and RUVBL2 leading to
CC the decrease of deacetylase activity of this complex; affects the
CC recruitment of repressive complexes to the Wnt target genes. Interacts
CC with ANXA2. Interacts with TGFBR1; interaction is TGF beta dependent;
CC mediates trafficking of the TGFBR1 from the endosomes to the nucleus
CC via microtubules in a TRAF6-dependent manner. Interacts with PRKCZ (By
CC similarity). Interacts with PIK3R1 and APPL2 (PubMed:25328665).
CC Interacts with ADIPOR1; ADIPOQ enhances this interaction; inhibites
CC adiponectin-stimulated binding of APPL2 to ADIPOR1 (PubMed:19661063).
CC {ECO:0000250|UniProtKB:Q9UKG1, ECO:0000269|PubMed:19661063,
CC ECO:0000269|PubMed:20133602, ECO:0000269|PubMed:21849472,
CC ECO:0000269|PubMed:25328665}.
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000269|PubMed:21849472}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9UKG1}. Nucleus {ECO:0000250|UniProtKB:Q9UKG1}.
CC Cytoplasm {ECO:0000250|UniProtKB:Q9UKG1}. Endosome
CC {ECO:0000269|PubMed:25568335, ECO:0000269|PubMed:27219021}. Cell
CC projection, ruffle {ECO:0000269|PubMed:25568335}. Cytoplasmic vesicle,
CC phagosome {ECO:0000269|PubMed:25568335}. Note=Early endosomal membrane-
CC bound and nuclear. Translocated into the nucleus upon release from
CC endosomal membranes following internalization of EGF.
CC {ECO:0000250|UniProtKB:Q9UKG1}.
CC -!- TISSUE SPECIFICITY: Expressed in insulin-target tissues including
CC skeletal muscle, liver, fat, and brain. {ECO:0000269|PubMed:19661063}.
CC -!- DOMAIN: Overexpression of an N-terminal domain (residues 1-319) or a C-
CC terminal region (residues 273-707) has a proapoptotic effect.
CC {ECO:0000250|UniProtKB:Q9UKG1}.
CC -!- DOMAIN: The F&H motif, an approximately 12-13 amino-acid sequence
CC centered around Phe and His residues, is essential for binding to OCRL
CC and INPP5B. {ECO:0000250|UniProtKB:Q9UKG1}.
CC -!- PTM: Phosphorylation at Ser-410 by PKA severely impairs binding to
CC OCRL. {ECO:0000250|UniProtKB:Q9UKG1}.
CC -!- DISRUPTION PHENOTYPE: Reduced survival rate after injection of LPS
CC (PubMed:25328665). Appl1 and Appl2 double knockout mice are viable and
CC grossly normal with regard to reproductive potential and postnatal
CC growth (PubMed:26445298). {ECO:0000269|PubMed:25328665,
CC ECO:0000269|PubMed:26445298}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH19708.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH19708.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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; AY113705; AAM55531.1; -; mRNA.
DR EMBL; AK013715; BAB28966.3; -; mRNA.
DR EMBL; AK033566; BAC28364.1; -; mRNA.
DR EMBL; AK045438; BAC32367.1; -; mRNA.
DR EMBL; AK049307; BAC33672.2; -; mRNA.
DR EMBL; AK146356; BAE27108.1; -; mRNA.
DR EMBL; BC019708; AAH19708.1; ALT_INIT; mRNA.
DR EMBL; BC063751; AAH63751.1; -; mRNA.
DR EMBL; AK173169; BAD32447.1; -; mRNA.
DR CCDS; CCDS26883.1; -.
DR RefSeq; NP_660256.1; NM_145221.2.
DR AlphaFoldDB; Q8K3H0; -.
DR SMR; Q8K3H0; -.
DR BioGRID; 215698; 23.
DR IntAct; Q8K3H0; 8.
DR MINT; Q8K3H0; -.
DR STRING; 10090.ENSMUSP00000042875; -.
DR iPTMnet; Q8K3H0; -.
DR PhosphoSitePlus; Q8K3H0; -.
DR SwissPalm; Q8K3H0; -.
DR EPD; Q8K3H0; -.
DR jPOST; Q8K3H0; -.
DR MaxQB; Q8K3H0; -.
DR PaxDb; Q8K3H0; -.
DR PeptideAtlas; Q8K3H0; -.
DR PRIDE; Q8K3H0; -.
DR ProteomicsDB; 279800; -.
DR Antibodypedia; 2775; 391 antibodies from 37 providers.
DR DNASU; 72993; -.
DR Ensembl; ENSMUST00000036570; ENSMUSP00000042875; ENSMUSG00000040760.
DR GeneID; 72993; -.
DR KEGG; mmu:72993; -.
DR UCSC; uc007sth.1; mouse.
DR CTD; 26060; -.
DR MGI; MGI:1920243; Appl1.
DR VEuPathDB; HostDB:ENSMUSG00000040760; -.
DR eggNOG; KOG0521; Eukaryota.
DR eggNOG; KOG3536; Eukaryota.
DR GeneTree; ENSGT00940000156624; -.
DR HOGENOM; CLU_025935_0_0_1; -.
DR InParanoid; Q8K3H0; -.
DR OMA; XVRREMD; -.
DR OrthoDB; 253010at2759; -.
DR PhylomeDB; Q8K3H0; -.
DR TreeFam; TF328669; -.
DR Reactome; R-MMU-418889; Caspase activation via Dependence Receptors in the absence of ligand.
DR BioGRID-ORCS; 72993; 1 hit in 70 CRISPR screens.
DR ChiTaRS; Appl1; mouse.
DR PRO; PR:Q8K3H0; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8K3H0; protein.
DR Bgee; ENSMUSG00000040760; Expressed in primary oocyte and 244 other tissues.
DR Genevisible; Q8K3H0; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032009; C:early phagosome; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR GO; GO:0097708; C:intracellular vesicle; ISO:MGI.
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; ISS:UniProtKB.
DR GO; GO:0001726; C:ruffle; IDA:UniProtKB.
DR GO; GO:0012506; C:vesicle membrane; ISO:MGI.
DR GO; GO:0048487; F:beta-tubulin binding; ISS:UniProtKB.
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:0043422; F:protein kinase B binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0033211; P:adiponectin-activated signaling pathway; ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; IMP:UniProtKB.
DR GO; GO:0008286; P:insulin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:1905450; P:negative regulation of Fc-gamma receptor signaling pathway involved in phagocytosis; IMP:UniProtKB.
DR GO; GO:1900017; P:positive regulation of cytokine production involved in inflammatory response; IMP:UniProtKB.
DR GO; GO:0046326; P:positive regulation of glucose import; ISS:UniProtKB.
DR GO; GO:1905303; P:positive regulation of macropinocytosis; IMP:UniProtKB.
DR GO; GO:0048023; P:positive regulation of melanin biosynthetic process; 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:0046324; P:regulation of glucose import; ISO:MGI.
DR GO; GO:0045088; P:regulation of innate immune response; IMP:UniProtKB.
DR GO; GO:1903076; P:regulation of protein localization to plasma membrane; ISO:MGI.
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 CDD; cd07631; BAR_APPL1; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR037929; APPL1_BAR.
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 projection; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW Endosome; Membrane; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..707
FT /note="DCC-interacting protein 13-alpha"
FT /id="PRO_0000079986"
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 495..655
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 397..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 234..257
FT /evidence="ECO:0000255"
FT COILED 620..670
FT /evidence="ECO:0000255"
FT MOTIF 403..414
FT /note="F&H"
FT /evidence="ECO:0000250"
FT COMPBIAS 636..667
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 399
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKG1"
FT MOD_RES 401
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKG1"
FT MOD_RES 410
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:Q9UKG1"
FT MOD_RES 691
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 694
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 37
FT /note="M -> K (in Ref. 2; BAB28966)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="Q -> P (in Ref. 2; BAB28966)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="A -> T (in Ref. 2; BAB28966)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="S -> P (in Ref. 2; BAB28966)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 707 AA; 79328 MW; 7B0F4BF4B6247A7F CRC64;
MPGIDKLPIE ETLEDSPQTR SLLGVFEEDA TAISNYMNQL YQAMHRIYDA QNELSAATHL
TSKLLKEYEK QRFPLGGDDE VMSSTLQQFS KVIDELSSCH AVLSTQLADA MMFPISQFKE
RDLKEILTLK EVFQIASNDH DAAINRYSRL SKKRENDKVK YEVTEDVYTS RKKQHQTMMH
YFCALNTLQY KKKIALLEPL LGYMQAQISF FKMGSENLNG QLEEFLANIG TSVQNVRREM
DGDVETMQQT IEDLEVASDP LYLPDPDPTK FPINRNLTRK AGYLNARNKT GLVSSTWDRQ
FYFTQGGNLM SQARGDVAGG LAMDIDNCSV MAVDCEDRRY CFQITSFDGK KSSILQAESK
KDHEEWICTI NNISKQIYLS ENPEETAARV NQSALEAVTP SPSFQQRHES LRPGGQSRPP
TARTSSSGSL GSESTNLAAL SLDSLVAPDT PIQFDIISPV CEDQPGQAKA FGQGGRRTNP
FGESGGSTKS ETEDSILHQL FIVRFLGSME VKSDDHPDVV YETMRQILAA RAIHNIFRMT
ESHLLVTCDC LKLIDPQTQV TRLTFPLPCV VLYATHQENK RLFGFVLRTS GGRSESNLSS
VCYIFESNNE GEKICDSVGL AKQIALHAEL DRRASEKQKE IERVKEKQQK ELSKQKQIEK
DLEEQSRLIA ASSRPNQAGS EGQLVLSSSQ SEESDLGEEG KKRESEA
