APC_MOUSE
ID APC_MOUSE Reviewed; 2845 AA.
AC Q61315; Q62044;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Adenomatous polyposis coli protein;
DE Short=Protein APC;
DE Short=mAPC;
GN Name=Apc;
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 1 AND 2), AND VARIANTS.
RC STRAIN=C57BL/6J, and CAST/EiJ; TISSUE=Brain;
RX PubMed=1350108; DOI=10.1126/science.1350108;
RA Su L.-K., Kinzler K.W., Vogelstein B., Preisinger A.C., Moser A.R.,
RA Luongo C., Gould K.A., Dove W.F.;
RT "Multiple intestinal neoplasia caused by a mutation in the murine homolog
RT of the APC gene.";
RL Science 256:668-670(1992).
RN [2]
RP ERRATUM OF PUBMED:1350108.
RA Su L.-K., Kinzler K.W., Vogelstein B., Preisinger A.C., Moser A.R.,
RA Luongo C., Gould K.A., Dove W.F.;
RL Science 256:1114-1114(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45.
RC STRAIN=BALB/cJ; TISSUE=Liver;
RA Dicker F., Lambertz S., Reitmair A., Ballhausen W.G.;
RT "The murine APC gene: alternative splicing of 5' untranslated region
RT segments.";
RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 1795-1810, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP ALTERNATIVE SPLICING.
RX PubMed=8242607;
RA Oshima M., Sugiyama H., Kitagawa K., Taketo M.;
RT "APC gene messenger RNA: novel isoforms that lack exon 7.";
RL Cancer Res. 53:5589-5591(1993).
RN [6]
RP INTERACTION WITH DIAPH1; DIAPH2 AND MAPRE1.
RX PubMed=15311282; DOI=10.1038/ncb1160;
RA Wen Y., Eng C.H., Schmoranzer J., Cabrera-Poch N., Morris E.J.S., Chen M.,
RA Wallar B.J., Alberts A.S., Gundersen G.G.;
RT "EB1 and APC bind to mDia to stabilize microtubules downstream of Rho and
RT promote cell migration.";
RL Nat. Cell Biol. 6:820-830(2004).
RN [7]
RP INTERACTION WITH SCRIB.
RX PubMed=16611247; DOI=10.1111/j.1365-2443.2006.00954.x;
RA Takizawa S., Nagasaka K., Nakagawa S., Yano T., Nakagawa K., Yasugi T.,
RA Takeuchi T., Kanda T., Huibregtse J.M., Akiyama T., Taketani Y.;
RT "Human scribble, a novel tumor suppressor identified as a target of high-
RT risk HPV E6 for ubiquitin-mediated degradation, interacts with adenomatous
RT polyposis coli.";
RL Genes Cells 11:453-464(2006).
RN [8]
RP FUNCTION.
RX PubMed=19893577; DOI=10.1038/embor.2009.233;
RA Kawasaki Y., Tsuji S., Muroya K., Furukawa S., Shibata Y., Okuno M.,
RA Ohwada S., Akiyama T.;
RT "The adenomatous polyposis coli-associated exchange factors Asef and Asef2
RT are required for adenoma formation in Apc(Min/+)mice.";
RL EMBO Rep. 10:1355-1362(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105; SER-109; SER-778;
RP SER-1036; SER-1370; SER-1391; SER-1394; THR-1437; SER-1772; SER-1859;
RP SER-1862; SER-1969; SER-1971; SER-2125; THR-2151; SER-2674 AND SER-2726,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, 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).
CC -!- FUNCTION: Tumor suppressor. Promotes rapid degradation of CTNNB1 and
CC participates in Wnt signaling as a negative regulator. APC activity is
CC correlated with its phosphorylation state. Activates the GEF activity
CC of SPATA13 and ARHGEF4. Plays a role in hepatocyte growth factor (HGF)-
CC induced cell migration (By similarity). Required for MMP9 up-regulation
CC via the JNK signaling pathway in colorectal tumor cells. Acts as a
CC mediator of ERBB2-dependent stabilization of microtubules at the cell
CC cortex. It is required for the localization of MACF1 to the cell
CC membrane and this localization of MACF1 is critical for its function in
CC microtubule stabilization (By similarity).
CC {ECO:0000250|UniProtKB:P25054, ECO:0000269|PubMed:19893577}.
CC -!- SUBUNIT: Forms homooligomers and heterooligomers with APC2. Interacts
CC with PDZ domains of DLG1 and DLG3. Associates with catenins. Binds
CC axin. Interacts with MAPRE2 and MAPRE3 (via C-terminus). Found in a
CC complex consisting of ARHGEF4, APC and CTNNB1. Interacts with ARHGEF4
CC (via N-terminus) (By similarity). Interacts with MAPRE1 (via C-
CC terminus); probably required for APC targeting to the growing
CC microtubule plus ends (PubMed:15311282). Interacts with DIAPH1 and
CC DIAPH2 (PubMed:15311282). Interacts with SCRIB; may mediate targeting
CC to adherens junctions of epithelial cells (PubMed:16611247). Interacts
CC with SPATA13 (via N-terminus and SH3 domain). Interacts with ASAP1 (via
CC SH3 domain) (By similarity). Found in a complex composed of MACF1, APC,
CC AXIN1, CTNNB1 and GSK3B. Interacts at the cell membrane with AMER1 and
CC AMER2 (via ARM repeats) (By similarity). Interacts with KHDRBS1 (By
CC similarity). The complex composed, at least, of APC, CTNNB1 and GSK3B
CC interacts with JPT1; the interaction requires the inactive form of
CC GSK3B (phosphorylated at 'Ser-9') (By similarity).
CC {ECO:0000250|UniProtKB:P25054, ECO:0000269|PubMed:15311282,
CC ECO:0000269|PubMed:16611247}.
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC {ECO:0000250|UniProtKB:P25054}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P25054}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:P25054}. Cell projection, ruffle membrane
CC {ECO:0000250|UniProtKB:P25054}. Cytoplasm
CC {ECO:0000250|UniProtKB:P25054}. Cell membrane
CC {ECO:0000250|UniProtKB:P25054}. Note=Associated with the microtubule
CC network at the growing distal tip of microtubules. Accumulates in the
CC lamellipodium and ruffle membrane in response to hepatocyte growth
CC factor (HGF) treatment. The MEMO1-RHOA-DIAPH1 signaling pathway
CC controls localization of the phosphorylated form to the cell membrane.
CC {ECO:0000250|UniProtKB:P25054}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q61315-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q61315-2; Sequence=VSP_004116;
CC Name=3;
CC IsoId=Q61315-3; Sequence=VSP_004117;
CC Name=4;
CC IsoId=Q61315-4; Sequence=VSP_004116, VSP_004117;
CC -!- TISSUE SPECIFICITY: Expressed in liver, spleen, kidney, heart, lung,
CC brain, stomach, intestine, testis and ovary.
CC -!- DOMAIN: The microtubule tip localization signal (MtLS) motif; mediates
CC interaction with MAPRE1 and targeting to the growing microtubule plus
CC ends. {ECO:0000250}.
CC -!- PTM: Phosphorylated by GSK3B. {ECO:0000250}.
CC -!- PTM: Ubiquitinated, leading to its degradation by the proteasome.
CC Ubiquitination is facilitated by Axin. Deubiquitinated by ZRANB1/TRABID
CC (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the adenomatous polyposis coli (APC) family.
CC {ECO:0000305}.
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DR EMBL; M88127; AAB59632.1; -; mRNA.
DR EMBL; U02937; AAA03443.1; -; Unassigned_DNA.
DR PIR; I49505; I49505.
DR PDB; 1VJ6; NMR; -; B=2834-2845.
DR PDBsum; 1VJ6; -.
DR SMR; Q61315; -.
DR ComplexPortal; CPX-103; Beta-catenin destruction core complex, variant 1.
DR ComplexPortal; CPX-449; Beta-catenin destruction core complex, variant 3.
DR ComplexPortal; CPX-453; Beta-catenin destruction core complex, variant 5.
DR ComplexPortal; CPX-457; Beta-catenin destruction core complex, variant 7.
DR CORUM; Q61315; -.
DR ELM; Q61315; -.
DR IntAct; Q61315; 13.
DR MINT; Q61315; -.
DR STRING; 10090.ENSMUSP00000078337; -.
DR iPTMnet; Q61315; -.
DR PhosphoSitePlus; Q61315; -.
DR jPOST; Q61315; -.
DR MaxQB; Q61315; -.
DR PaxDb; Q61315; -.
DR PeptideAtlas; Q61315; -.
DR PRIDE; Q61315; -.
DR ProteomicsDB; 296330; -. [Q61315-1]
DR ProteomicsDB; 296331; -. [Q61315-2]
DR ProteomicsDB; 296332; -. [Q61315-3]
DR ProteomicsDB; 296333; -. [Q61315-4]
DR MGI; MGI:88039; Apc.
DR eggNOG; KOG2122; Eukaryota.
DR InParanoid; Q61315; -.
DR PhylomeDB; Q61315; -.
DR Reactome; R-MMU-111465; Apoptotic cleavage of cellular proteins.
DR Reactome; R-MMU-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-MMU-196299; Beta-catenin phosphorylation cascade.
DR Reactome; R-MMU-3769402; Deactivation of the beta-catenin transactivating complex.
DR Reactome; R-MMU-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR Reactome; R-MMU-5689896; Ovarian tumor domain proteases.
DR ChiTaRS; Apc; mouse.
DR EvolutionaryTrace; Q61315; -.
DR PRO; PR:Q61315; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q61315; protein.
DR GO; GO:0005912; C:adherens junction; ISO:MGI.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0044295; C:axonal growth cone; IDA:MGI.
DR GO; GO:0030877; C:beta-catenin destruction complex; ISS:UniProtKB.
DR GO; GO:0005923; C:bicellular tight junction; ISO:MGI.
DR GO; GO:0016342; C:catenin complex; ISO:MGI.
DR GO; GO:0070852; C:cell body fiber; ISO:MGI.
DR GO; GO:0005938; C:cell cortex; ISO:MGI.
DR GO; GO:0042995; C:cell projection; IDA:MGI.
DR GO; GO:0031253; C:cell projection membrane; IDA:MGI.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:CAFA.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0030426; C:growth cone; IDA:MGI.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0016328; C:lateral plasma membrane; ISO:MGI.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0044306; C:neuron projection terminus; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:CAFA.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0032587; C:ruffle membrane; ISS:UniProtKB.
DR GO; GO:0034750; C:Scrib-APC-beta-catenin complex; IDA:BHF-UCL.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0030672; C:synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0008013; F:beta-catenin binding; IDA:MGI.
DR GO; GO:0070840; F:dynein complex binding; IPI:CAFA.
DR GO; GO:0045295; F:gamma-catenin binding; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0051010; F:microtubule plus-end binding; IDA:MGI.
DR GO; GO:0002020; F:protease binding; IPI:BHF-UCL.
DR GO; GO:0019901; F:protein kinase binding; IPI:CAFA.
DR GO; GO:0019887; F:protein kinase regulator activity; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:1990863; P:acinar cell proliferation; IMP:MGI.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0009798; P:axis specification; IMP:MGI.
DR GO; GO:0007409; P:axonogenesis; IMP:MGI.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IMP:MGI.
DR GO; GO:0044336; P:canonical Wnt signaling pathway involved in negative regulation of apoptotic process; IGI:MGI.
DR GO; GO:0044337; P:canonical Wnt signaling pathway involved in positive regulation of apoptotic process; IGI:MGI.
DR GO; GO:0007155; P:cell adhesion; IMP:MGI.
DR GO; GO:0051301; P:cell division; IMP:MGI.
DR GO; GO:0001708; P:cell fate specification; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IMP:MGI.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0051276; P:chromosome organization; IMP:MGI.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IGI:MGI.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:MGI.
DR GO; GO:0001935; P:endothelial cell proliferation; IMP:MGI.
DR GO; GO:1904019; P:epithelial cell apoptotic process; IMP:MGI.
DR GO; GO:0050673; P:epithelial cell proliferation; IMP:MGI.
DR GO; GO:0060767; P:epithelial cell proliferation involved in prostate gland development; IMP:MGI.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; ISO:MGI.
DR GO; GO:0044346; P:fibroblast apoptotic process; IMP:MGI.
DR GO; GO:0010761; P:fibroblast migration; IMP:MGI.
DR GO; GO:0001942; P:hair follicle development; IMP:MGI.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IMP:CAFA.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:0000165; P:MAPK cascade; IMP:MGI.
DR GO; GO:0007091; P:metaphase/anaphase transition of mitotic cell cycle; IMP:MGI.
DR GO; GO:0007019; P:microtubule depolymerization; IMP:MGI.
DR GO; GO:0046785; P:microtubule polymerization; IMP:MGI.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:MGI.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; ISO:MGI.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IGI:MGI.
DR GO; GO:1904698; P:negative regulation of acinar cell proliferation; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:MGI.
DR GO; GO:0060044; P:negative regulation of cardiac muscle cell proliferation; ISO:MGI.
DR GO; GO:1902807; P:negative regulation of cell cycle G1/S phase transition; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IMP:MGI.
DR GO; GO:1904036; P:negative regulation of epithelial cell apoptotic process; IMP:MGI.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:MGI.
DR GO; GO:0060770; P:negative regulation of epithelial cell proliferation involved in prostate gland development; IMP:MGI.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IMP:MGI.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IMP:MGI.
DR GO; GO:0042483; P:negative regulation of odontogenesis; IMP:MGI.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IMP:MGI.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0031175; P:neuron projection development; ISO:MGI.
DR GO; GO:0042476; P:odontogenesis; IMP:MGI.
DR GO; GO:0007389; P:pattern specification process; IMP:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0045785; P:positive regulation of cell adhesion; IMP:MGI.
DR GO; GO:0010942; P:positive regulation of cell death; ISO:MGI.
DR GO; GO:0045597; P:positive regulation of cell differentiation; IMP:MGI.
DR GO; GO:0051781; P:positive regulation of cell division; IMP:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:2000271; P:positive regulation of fibroblast apoptotic process; IMP:MGI.
DR GO; GO:0010763; P:positive regulation of fibroblast migration; IMP:MGI.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; IMP:MGI.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:MGI.
DR GO; GO:1904781; P:positive regulation of protein localization to centrosome; IMP:CAFA.
DR GO; GO:0031274; P:positive regulation of pseudopodium assembly; ISO:MGI.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IC:ComplexPortal.
DR GO; GO:0030163; P:protein catabolic process; IMP:MGI.
DR GO; GO:0065003; P:protein-containing complex assembly; ISS:UniProtKB.
DR GO; GO:0009954; P:proximal/distal pattern formation; IMP:MGI.
DR GO; GO:0051988; P:regulation of attachment of spindle microtubules to kinetochore; IMP:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:MGI.
DR GO; GO:0045595; P:regulation of cell differentiation; IGI:MGI.
DR GO; GO:0030334; P:regulation of cell migration; IGI:MGI.
DR GO; GO:0030856; P:regulation of epithelial cell differentiation; IMP:MGI.
DR GO; GO:0010632; P:regulation of epithelial cell migration; IMP:MGI.
DR GO; GO:2000211; P:regulation of glutamate metabolic process; ISO:MGI.
DR GO; GO:0032886; P:regulation of microtubule-based process; ISS:UniProtKB.
DR GO; GO:0051171; P:regulation of nitrogen compound metabolic process; IMP:MGI.
DR GO; GO:0045667; P:regulation of osteoblast differentiation; IMP:MGI.
DR GO; GO:0045670; P:regulation of osteoclast differentiation; IMP:MGI.
DR GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
DR GO; GO:0043588; P:skin development; IMP:MGI.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IMP:MGI.
DR GO; GO:0019827; P:stem cell population maintenance; IMP:MGI.
DR GO; GO:0033077; P:T cell differentiation in thymus; IMP:MGI.
DR GO; GO:0048538; P:thymus development; IMP:MGI.
DR GO; GO:0016055; P:Wnt signaling pathway; IDA:MGI.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR026836; APC.
DR InterPro; IPR009240; APC_15aa_rpt.
DR InterPro; IPR009234; APC_basic_dom.
DR InterPro; IPR026831; APC_dom.
DR InterPro; IPR026818; Apc_fam.
DR InterPro; IPR032038; APC_N.
DR InterPro; IPR036149; APC_N_sf.
DR InterPro; IPR041257; APC_rep.
DR InterPro; IPR009223; APC_rpt.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR009232; EB1-bd.
DR InterPro; IPR009224; SAMP.
DR PANTHER; PTHR12607; PTHR12607; 1.
DR PANTHER; PTHR12607:SF11; PTHR12607:SF11; 1.
DR Pfam; PF05972; APC_15aa; 3.
DR Pfam; PF05956; APC_basic; 1.
DR Pfam; PF16689; APC_N_CC; 1.
DR Pfam; PF05923; APC_r; 7.
DR Pfam; PF18797; APC_rep; 1.
DR Pfam; PF00514; Arm; 2.
DR Pfam; PF05937; EB1_binding; 1.
DR Pfam; PF05924; SAMP; 3.
DR SMART; SM00185; ARM; 7.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF58050; SSF58050; 1.
DR SUPFAM; SSF82931; SSF82931; 1.
DR PROSITE; PS50176; ARM_REPEAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell junction;
KW Cell membrane; Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Membrane; Microtubule; Phosphoprotein;
KW Reference proteome; Repeat; Tumor suppressor; Ubl conjugation;
KW Wnt signaling pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P25054"
FT CHAIN 2..2845
FT /note="Adenomatous polyposis coli protein"
FT /id="PRO_0000064628"
FT REPEAT 451..493
FT /note="ARM 1"
FT REPEAT 503..545
FT /note="ARM 2"
FT REPEAT 546..589
FT /note="ARM 3"
FT REPEAT 590..636
FT /note="ARM 4"
FT REPEAT 637..681
FT /note="ARM 5"
FT REPEAT 682..723
FT /note="ARM 6"
FT REPEAT 724..765
FT /note="ARM 7"
FT REGION 238..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 828..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 921..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 956..986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1058..1079
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1092..1168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1189..1247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1307..1375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1400..1474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1525..1568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1587..1606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1746..2010
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1864..1891
FT /note="Highly charged"
FT REGION 2042..2069
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2146..2190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2202..2652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2664..2845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2..61
FT /evidence="ECO:0000255"
FT COILED 125..245
FT /evidence="ECO:0000255"
FT MOTIF 2805..2808
FT /note="Microtubule tip localization signal"
FT MOTIF 2843..2845
FT /note="PDZ-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 242..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..855
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..942
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 956..973
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1064..1078
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1130..1147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1329..1373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1432..1446
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1543..1559
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1746..1761
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1785..1808
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1809..1823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1861..1893
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1894..1935
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1950..1976
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2170..2190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2202..2226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2234..2249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2261..2438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2461..2499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2519..2533
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2557..2580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2581..2596
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2621..2636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2669..2690
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2691..2705
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2706..2732
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2759..2815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2825..2845
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P25054"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 742
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25054"
FT MOD_RES 746
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25054"
FT MOD_RES 778
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 906
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25054"
FT MOD_RES 985
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70478"
FT MOD_RES 1036
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1040
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25054"
FT MOD_RES 1359
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25054"
FT MOD_RES 1370
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1384
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25054"
FT MOD_RES 1391
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1394
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1437
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1565
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70478"
FT MOD_RES 1772
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1859
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1861
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25054"
FT MOD_RES 1862
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1969
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1971
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2087
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70478"
FT MOD_RES 2092
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70478"
FT MOD_RES 2125
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2129
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70478"
FT MOD_RES 2130
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70478"
FT MOD_RES 2132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70478"
FT MOD_RES 2151
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2260
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25054"
FT MOD_RES 2270
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25054"
FT MOD_RES 2283
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25054"
FT MOD_RES 2473
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25054"
FT MOD_RES 2535
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25054"
FT MOD_RES 2569
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25054"
FT MOD_RES 2671
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25054"
FT MOD_RES 2674
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2679
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P25054"
FT MOD_RES 2713
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70478"
FT MOD_RES 2726
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2791
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25054"
FT VAR_SEQ 243..276
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:1350108"
FT /id="VSP_004116"
FT VAR_SEQ 310..410
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_004117"
FT VARIANT 120
FT /note="T -> A (in strain: CAST/Ei)"
FT VARIANT 493
FT /note="V -> I (in strain: CAST/Ei)"
FT VARIANT 797
FT /note="Y -> F (in strain: CAST/Ei)"
FT VARIANT 1330
FT /note="A -> T (in strain: CAST/Ei)"
FT VARIANT 1618
FT /note="A -> S (in strain: CAST/Ei)"
FT VARIANT 2294
FT /note="G -> A (in strain: CAST/Ei)"
FT VARIANT 2496
FT /note="H -> Q (in strain: CAST/Ei)"
FT VARIANT 2523
FT /note="T -> A (in strain: CAST/Ei)"
FT VARIANT 2813
FT /note="T -> S (in strain: CAST/Ei)"
SQ SEQUENCE 2845 AA; 311089 MW; 145CA73CF570A499 CRC64;
MAAASYDQLL KQVEALKMEN SNLRQELEDN SNHLTKLETE ASNMKEVLKQ LQGSIEDETM
TSGQIDLLER LKEFNLDSNF PGVKLRSKMS LRSYGSREGS VSSRSGECSP VPMGSFPRRT
FVNGSRESTG YLEELEKERS LLLADLDKEE KEKDWYYAQL QNLTKRIDSL PLTENFSLQT
DMTRRQLEYE ARQIRAAMEE QLGTCQDMEK RAQRRIARIQ QIEKDILRVR QLLQSQAAEA
ERSSQSRHDA ASHEAGRQHE GHGVAESNTA ASSSGQSPAT RVDHETASVL SSSGTHSAPR
RLTSHLGTKV EMVYSLLSML GTHDKDDMSR TLLAMSSSQD SCISMRQSGC LPLLIQLLHG
NDKDSVLLGN SRGSKEARAR ASAALHNIIH SQPDDKRGRR EIRVLHLLEQ IRAYCETCWE
WQEAHEQGMD QDKNPMPAPV EHQICPAVCV LMKLSFDEEH RHAMNELGGL QAIAELLQVD
CEMYGLTNDH YSVTLRRYAG MALTNLTFGD VANKATLCSM KGCMRALVAQ LKSESEDLQQ
VIASVLRNLS WRADVNSKKT LREVGSVKAL MECALEVKKE STLKSVLSAL WNLSAHCTEN
KADICAVDGA LAFLVGTLTY RSQTNTLAII ESGGGILRNV SSLIATNEDH RQILRENNCL
QTLLQHLKSH SLTIVSNACG TLWNLSARNP KDQEALWDMG AVSMLKNLIH SKHKMIAMGS
AAALRNLMAN RPAKYKDANI MSPGSSLPSL HVRKQKALEA ELDAQHLSET FDNIDNLSPK
ASHRSKQRHK QNLYGDYAFD ANRHDDSRSD NFNTGNMTVL SPYLNTTVLP SSSSSRGSLD
SSRSEKDRSL ERERGIGLSA YHPTTENAGT SSKRGLQITT TAAQIAKVME EVSAIHTSQD
DRSSASTTEF HCVADDRSAA RRSSASHTHS NTYNFTKSEN SNRTCSMPYA KVEYKRSSND
SLNSVTSSDG YGKRGQMKPS VESYSEDDES KFCSYGQYPA DLAHKIHSAN HMDDNDGELD
TPINYSLKYS DEQLNSGRQS PSQNERWARP KHVIEDEIKQ NEQRQARSQN TSYPVYSENT
DDKHLKFQPH FGQQECVSPY RSRGTSGSET NRMGSSHAIN QNVNQSLCQE DDYEDDKPTN
YSERYSEEEQ HEEEEERPTN YSIKYNEEKH HVDQPIDYSL KYATDISSSQ KPSFSFSKNS
SAQSTKPEHL SPSSENTAVP PSNAKRQNQL RPSSAQRNGQ TQKGTTCKVP SINQETIQTY
CVEDTPICFS RCSSLSSLSS ADDEIGCDQT TQEADSANTL QTAEVKENDV TRSAEDPATE
VPAVSQNARA KPSRLQASGL SSESTRHNKA VEFSSGAKSP SKSGAQTPKS PPEHYVQETP
LVFSRCTSVS SLDSFESRSI ASSVQSEPCS GMVSGIISPS DLPDSPGQTM PPSRSKTPPP
PPQTVQAKRE VPKSKVPAAE KRESGPKQTA VNAAVQRVQV LPDVDTLLHF ATESTPDGFS
CSSSLSALSL DEPFIQKDVE LRIMPPVQEN DNGNETESEQ PEESNENQDK EVEKPDSEKD
LLDDSDDDDI EILEECIISA MPTKSSRKAK KLAQTASKLP PPVARKPSQL PVYKLLPAQN
RLQAQKHVSF TPGDDVPRVY CVEGTPINFS TATSLSDLTI ESPPNELATG DGVRAGIQSG
EFEKRDTIPT EGRSTDDAQR GKISSIVTPD LDDNKAEEGD ILAECINSAM PKGKSHKPFR
VKKIMDQVQQ ASSTSSGANK NQVDTKKKKP TSPVKPMPQN TEYRTRVRKN TDSKVNVNTE
ETFSDNKDSK KPSLQTNAKA FNEKLPNNED RVRGTFALDS PHHYTPIEGT PYCFSRNDSL
SSLDFDDDDV DLSREKAELR KGKESKDSEA KVTCRPEPNS SQQAASKSQA SIKHPANRAQ
SKPVLQKQPT FPQSSKDGPD RGAATDEKLQ NLAIENTPVC FSRNSSLSSL SDIDQENNNN
KESEPIKEAE PANSQGEPSK PQASGYAPKS FHVEDTPVCF SRNSSLSSLS IDSEDDLLQE
CISSAMPKKK RPSRLKSESE KQSPRKVGGI LAEDLTLDLK DLQRPDSEHA FSPGSENFDW
KAIQEGANSI VSSLHQAAAA AACLSRQASS DSDSILSLKS GISLGSPFHL TPDQEEKPFT
SNKGPRILKP GEKSTLEAKK IESENKGIKG GKKVYKSLIT GKIRSNSEIS SQMKQPLPTN
MPSISRGRTM IHIPGLRNSS SSTSPVSKKG PPLKTPASKS PSEGPGATTS PRGTKPAGKS
ELSPITRQTS QISGSNKGSS RSGSRDSTPS RPTQQPLSRP MQSPGRNSIS PGRNGISPPN
KLSQLPRTSS PSTASTKSSG SGKMSYTSPG RQLSQQNLTK QASLSKNASS IPRSESASKG
LNQMSNGNGS NKKVELSRMS STKSSGSESD SSERPALVRQ STFIKEAPSP TLRRKLEESA
SFESLSPSSR PDSPTRSQAQ TPVLSPSLPD MSLSTHPSVQ AGGWRKLPPN LSPTIEYNDG
RPTKRHDIAR SHSESPSRLP INRAGTWKRE HSKHSSSLPR VSTWRRTGSS SSILSASSES
SEKAKSEDER HVSSMPAPRQ MKENQVPTKG TWRKIKESDI SPTGMASQSA SSGAASGAES
KPLIYQMAPP VSKTEDVWVR IEDCPINNPR SGRSPTGNTP PVIDSVSEKG SSSIKDSKDS
KDTHGKQSVG SGSPVQTVGL ETRLNSFVQV EAPEQKGTEA KPGQSNPVSI AETAETCIAE
RTPFSSSSSS KHSSPSGTVA ARVTPFNYNP SPRKSSADST SARPSQIPTP VSTNTKKRDS
KTDITESSGA QSPKRHSGSY LVTSV
