IED Industry Enzyme Database

Detail Information for IndEnz0002003645
IED ID IndEnz0002003645
Enzyme Type ID protease003645
Protein Name Adenomatous polyposis coli protein
Protein APC
mAPC
Gene Name Apc
Organism Mus musculus (Mouse)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse)
Enzyme Sequence MAAASYDQLLKQVEALKMENSNLRQELEDNSNHLTKLETEASNMKEVLKQLQGSIEDETMTSGQIDLLERLKEFNLDSNFPGVKLRSKMSLRSYGSREGSVSSRSGECSPVPMGSFPRRTFVNGSRESTGYLEELEKERSLLLADLDKEEKEKDWYYAQLQNLTKRIDSLPLTENFSLQTDMTRRQLEYEARQIRAAMEEQLGTCQDMEKRAQRRIARIQQIEKDILRVRQLLQSQAAEAERSSQSRHDAASHEAGRQHEGHGVAESNTAASSSGQSPATRVDHETASVLSSSGTHSAPRRLTSHLGTKVEMVYSLLSMLGTHDKDDMSRTLLAMSSSQDSCISMRQSGCLPLLIQLLHGNDKDSVLLGNSRGSKEARARASAALHNIIHSQPDDKRGRREIRVLHLLEQIRAYCETCWEWQEAHEQGMDQDKNPMPAPVEHQICPAVCVLMKLSFDEEHRHAMNELGGLQAIAELLQVDCEMYGLTNDHYSVTLRRYAGMALTNLTFGDVANKATLCSMKGCMRALVAQLKSESEDLQQVIASVLRNLSWRADVNSKKTLREVGSVKALMECALEVKKESTLKSVLSALWNLSAHCTENKADICAVDGALAFLVGTLTYRSQTNTLAIIESGGGILRNVSSLIATNEDHRQILRENNCLQTLLQHLKSHSLTIVSNACGTLWNLSARNPKDQEALWDMGAVSMLKNLIHSKHKMIAMGSAAALRNLMANRPAKYKDANIMSPGSSLPSLHVRKQKALEAELDAQHLSETFDNIDNLSPKASHRSKQRHKQNLYGDYAFDANRHDDSRSDNFNTGNMTVLSPYLNTTVLPSSSSSRGSLDSSRSEKDRSLERERGIGLSAYHPTTENAGTSSKRGLQITTTAAQIAKVMEEVSAIHTSQDDRSSASTTEFHCVADDRSAARRSSASHTHSNTYNFTKSENSNRTCSMPYAKVEYKRSSNDSLNSVTSSDGYGKRGQMKPSVESYSEDDESKFCSYGQYPADLAHKIHSANHMDDNDGELDTPINYSLKYSDEQLNSGRQSPSQNERWARPKHVIEDEIKQNEQRQARSQNTSYPVYSENTDDKHLKFQPHFGQQECVSPYRSRGTSGSETNRMGSSHAINQNVNQSLCQEDDYEDDKPTNYSERYSEEEQHEEEEERPTNYSIKYNEEKHHVDQPIDYSLKYATDISSSQKPSFSFSKNSSAQSTKPEHLSPSSENTAVPPSNAKRQNQLRPSSAQRNGQTQKGTTCKVPSINQETIQTYCVEDTPICFSRCSSLSSLSSADDEIGCDQTTQEADSANTLQTAEVKENDVTRSAEDPATEVPAVSQNARAKPSRLQASGLSSESTRHNKAVEFSSGAKSPSKSGAQTPKSPPEHYVQETPLVFSRCTSVSSLDSFESRSIASSVQSEPCSGMVSGIISPSDLPDSPGQTMPPSRSKTPPPPPQTVQAKREVPKSKVPAAEKRESGPKQTAVNAAVQRVQVLPDVDTLLHFATESTPDGFSCSSSLSALSLDEPFIQKDVELRIMPPVQENDNGNETESEQPEESNENQDKEVEKPDSEKDLLDDSDDDDIEILEECIISAMPTKSSRKAKKLAQTASKLPPPVARKPSQLPVYKLLPAQNRLQAQKHVSFTPGDDVPRVYCVEGTPINFSTATSLSDLTIESPPNELATGDGVRAGIQSGEFEKRDTIPTEGRSTDDAQRGKISSIVTPDLDDNKAEEGDILAECINSAMPKGKSHKPFRVKKIMDQVQQASSTSSGANKNQVDTKKKKPTSPVKPMPQNTEYRTRVRKNTDSKVNVNTEETFSDNKDSKKPSLQTNAKAFNEKLPNNEDRVRGTFALDSPHHYTPIEGTPYCFSRNDSLSSLDFDDDDVDLSREKAELRKGKESKDSEAKVTCRPEPNSSQQAASKSQASIKHPANRAQSKPVLQKQPTFPQSSKDGPDRGAATDEKLQNLAIENTPVCFSRNSSLSSLSDIDQENNNNKESEPIKEAEPANSQGEPSKPQASGYAPKSFHVEDTPVCFSRNSSLSSLSIDSEDDLLQECISSAMPKKKRPSRLKSESEKQSPRKVGGILAEDLTLDLKDLQRPDSEHAFSPGSENFDWKAIQEGANSIVSSLHQAAAAAACLSRQASSDSDSILSLKSGISLGSPFHLTPDQEEKPFTSNKGPRILKPGEKSTLEAKKIESENKGIKGGKKVYKSLITGKIRSNSEISSQMKQPLPTNMPSISRGRTMIHIPGLRNSSSSTSPVSKKGPPLKTPASKSPSEGPGATTSPRGTKPAGKSELSPITRQTSQISGSNKGSSRSGSRDSTPSRPTQQPLSRPMQSPGRNSISPGRNGISPPNKLSQLPRTSSPSTASTKSSGSGKMSYTSPGRQLSQQNLTKQASLSKNASSIPRSESASKGLNQMSNGNGSNKKVELSRMSSTKSSGSESDSSERPALVRQSTFIKEAPSPTLRRKLEESASFESLSPSSRPDSPTRSQAQTPVLSPSLPDMSLSTHPSVQAGGWRKLPPNLSPTIEYNDGRPTKRHDIARSHSESPSRLPINRAGTWKREHSKHSSSLPRVSTWRRTGSSSSILSASSESSEKAKSEDERHVSSMPAPRQMKENQVPTKGTWRKIKESDISPTGMASQSASSGAASGAESKPLIYQMAPPVSKTEDVWVRIEDCPINNPRSGRSPTGNTPPVIDSVSEKGSSSIKDSKDSKDTHGKQSVGSGSPVQTVGLETRLNSFVQVEAPEQKGTEAKPGQSNPVSIAETAETCIAERTPFSSSSSSKHSSPSGTVAARVTPFNYNPSPRKSSADSTSARPSQIPTPVSTNTKKRDSKTDITESSGAQSPKRHSGSYLVTSV
Enzyme Length 2845
Uniprot Accession Number Q61315
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Tumor suppressor. Promotes rapid degradation of CTNNB1 and participates in Wnt signaling as a negative regulator. APC activity is correlated with its phosphorylation state. Activates the GEF activity of SPATA13 and ARHGEF4. Plays a role in hepatocyte growth factor (HGF)-induced cell migration (By similarity). Required for MMP9 up-regulation via the JNK signaling pathway in colorectal tumor cells. Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. It is required for the localization of MACF1 to the cell membrane and this localization of MACF1 is critical for its function in microtubule stabilization (By similarity). {ECO:0000250|UniProtKB:P25054, ECO:0000269|PubMed:19893577}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Alternative sequence (2); Chain (1); Coiled coil (2); Compositional bias (31); Initiator methionine (1); Modified residue (42); Motif (2); Natural variant (9); Region (17); Repeat (7)
Keywords 3D-structure;Acetylation;Alternative splicing;Cell junction;Cell membrane;Cell projection;Coiled coil;Cytoplasm;Cytoskeleton;Direct protein sequencing;Membrane;Microtubule;Phosphoprotein;Reference proteome;Repeat;Tumor suppressor;Ubl conjugation;Wnt signaling pathway
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cell junction, adherens junction {ECO:0000250|UniProtKB:P25054}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P25054}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:P25054}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:P25054}. Cytoplasm {ECO:0000250|UniProtKB:P25054}. Cell membrane {ECO:0000250|UniProtKB:P25054}. Note=Associated with the microtubule network at the growing distal tip of microtubules. Accumulates in the lamellipodium and ruffle membrane in response to hepatocyte growth factor (HGF) treatment. The MEMO1-RHOA-DIAPH1 signaling pathway controls localization of the phosphorylated form to the cell membrane. {ECO:0000250|UniProtKB:P25054}.
Modified Residue MOD_RES 2; /note=N-acetylalanine; /evidence=ECO:0000250|UniProtKB:P25054; MOD_RES 105; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 109; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 742; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P25054; MOD_RES 746; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P25054; MOD_RES 778; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 906; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P25054; MOD_RES 985; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P70478; MOD_RES 1036; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 1040; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P25054; MOD_RES 1359; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P25054; MOD_RES 1370; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 1384; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P25054; MOD_RES 1391; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 1394; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 1437; /note=Phosphothreonine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 1565; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P70478; MOD_RES 1772; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 1859; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 1861; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P25054; MOD_RES 1862; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 1969; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 1971; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 2087; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P70478; MOD_RES 2092; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P70478; MOD_RES 2125; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 2129; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P70478; MOD_RES 2130; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P70478; MOD_RES 2132; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P70478; MOD_RES 2151; /note=Phosphothreonine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 2260; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P25054; MOD_RES 2270; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P25054; MOD_RES 2283; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P25054; MOD_RES 2473; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P25054; MOD_RES 2535; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P25054; MOD_RES 2569; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P25054; MOD_RES 2671; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P25054; MOD_RES 2674; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 2679; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:P25054; MOD_RES 2713; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P70478; MOD_RES 2726; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 2791; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P25054
Post Translational Modification PTM: Phosphorylated by GSK3B. {ECO:0000250}.; PTM: Ubiquitinated, leading to its degradation by the proteasome. Ubiquitination is facilitated by Axin. Deubiquitinated by ZRANB1/TRABID (By similarity). {ECO:0000250}.
Signal Peptide
Structure 3D NMR spectroscopy (1)
Cross Reference PDB 1VJ6;
Mapped Pubmed ID 10025873; 10027409; 10036185; 10069468; 10096563; 10188882; 10204802; 10210642; 10213222; 10223192; 10330403; 10334197; 10341706; 10346819; 10357779; 10357794; 10362808; 10383901; 10451698; 10469614; 10489374; 10498885; 10506110; 10512984; 10535960; 10537280; 10545699; 10602475; 10626800; 10648462; 10667389; 10680582; 10703747; 10706126; 10708962; 10716720; 10725249; 10733430; 10753194; 10766173; 10783313; 10783317; 10786662; 10801912; 10837006; 10851078; 10853036; 10862047; 10866310; 10868458; 10870964; 10873591; 10913614; 10919675; 10953028; 10969066; 10969819; 10974033; 10974406; 10982921; 10987266; 10987272; 10987662; 10992298; 10996730; 11016626; 11016642; 11034085; 11039641; 11040191; 11101838; 11126362; 11130972; 11156379; 11161784; 11181458; 11196148; 11196181; 11197776; 11206275; 11209052; 11212243; 11212250; 11212260; 11215675; 11245490; 11256068; 11274413; 11289129; 11309311; 11313976; 11323404; 11323676; 11355956; 11381263; 11385109; 11420398; 11424022; 11431334; 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Motif MOTIF 2805..2808; /note=Microtubule tip localization signal; MOTIF 2843..2845; /note=PDZ-binding; /evidence=ECO:0000250
Gene Encoded By
Mass 311,089
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda