ID   APC_RAT                 Reviewed;        2842 AA.
AC   P70478;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   22-NOV-2017, entry version 152.
DE   RecName: Full=Adenomatous polyposis coli protein;
DE            Short=Protein APC;
GN   Name=Apc;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Fischer 344/N; TISSUE=Brain;
RX   PubMed=8563176; DOI=10.1007/BF00354300;
RA   Toyota M., Ushijima T., Kakiuchi H., Watanabe M., Imai K., Yachi A.,
RA   Sugimura T., Nagao M.;
RT   "cDNA cloning of the rat APC gene and assignment to chromosome 18.";
RL   Mamm. Genome 6:746-748(1995).
RN   [2]
RP   MUTAGENESIS.
RC   STRAIN=Fischer 344/N, and Sprague-Dawley;
RX   PubMed=7846077; DOI=10.1073/pnas.92.3.910;
RA   Kakiuchi H., Watanabe M., Ushijima T., Toyota M., Imai K.,
RA   Weisburger J.H., Sugimura T., Nagao M.;
RT   "Specific 5'-GGGA-3'-->5'-GGA-3' mutation of the Apc gene in rat colon
RT   tumors induced by 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:910-914(1995).
RN   [3]
RP   IDENTIFICATION IN A COMPLEX WITH MACF1; CTNNB1; AXIN1 AND GSK3B.
RX   PubMed=16815997; DOI=10.1101/gad.1411206;
RA   Chen H.J., Lin C.M., Lin C.S., Perez-Olle R., Leung C.L., Liem R.K.;
RT   "The role of microtubule actin cross-linking factor 1 (MACF1) in the
RT   Wnt signaling pathway.";
RL   Genes Dev. 20:1933-1945(2006).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1714, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA   Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT   "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT   regulation of aquaporin-2 phosphorylation at two sites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-742; SER-778; SER-985;
RP   SER-1040; SER-1368; SER-1565; SER-1859; SER-2087; SER-2092; SER-2129;
RP   SER-2130; SER-2132 AND SER-2710, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
RA   Lundby C., Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14
RT   different rat organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Tumor suppressor. Promotes rapid degradation of CTNNB1
CC       and participates in Wnt signaling as a negative regulator. APC
CC       activity is correlated with its phosphorylation state. Activates
CC       the GEF activity of SPATA13 and ARHGEF4. Plays a role in
CC       hepatocyte growth factor (HGF)-induced cell migration. Required
CC       for MMP9 up-regulation via the JNK signaling pathway in colorectal
CC       tumor cells. Acts as a mediator of ERBB2-dependent stabilization
CC       of microtubules at the cell cortex. It is required for the
CC       localization of MACF1 to the cell membrane and this localization
CC       of MACF1 is critical for its function in microtubule stabilization
CC       (By similarity). {ECO:0000250|UniProtKB:P25054,
CC       ECO:0000250|UniProtKB:Q61315}.
CC   -!- SUBUNIT: Forms homooligomers and heterooligomers with APC2.
CC       Interacts with DIAPH1 and DIAPH2. Interacts with PDZ domains of
CC       DLG1 and DLG3. Associates with catenins. Binds axin. Interacts
CC       with ARHGEF4 (via N-terminus). Interacts with MAPRE1 (via C-
CC       terminus); probably required for APC targeting to the growing
CC       microtubule plus ends. Interacts with MAPRE2 and MAPRE3 (via C-
CC       terminus). Found in a complex consisting of ARHGEF4, APC and
CC       CTNNB1. Interacts with SCRIB; may mediate APC targeting to
CC       adherens junctions of epithelial cells. Interacts with SPATA13
CC       (via N-terminus and SH3 domain). Interacts with ASAP1 (via SH3
CC       domain). Interacts at the cell membrane with AMER1 and AMER2 (via
CC       ARM repeats) (By similarity). Found in a complex composed of
CC       MACF1, APC, AXIN1, CTNNB1 and GSK3B. Interacts with KHDRBS1 (By
CC       similarity). The complex composed, at least, of APC, CTNNB1 and
CC       GSK3B interacts with JPT1; the interaction requires the inactive
CC       form of GSK3B (phosphorylated at 'Ser-9') (By similarity).
CC       {ECO:0000250|UniProtKB:P25054, ECO:0000250|UniProtKB:Q61315,
CC       ECO:0000269|PubMed:16815997}.
CC   -!- INTERACTION:
CC       P31016:Dlg4; NbExp=2; IntAct=EBI-631663, EBI-375655;
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
CC       microtubule network at the growing distal tip of microtubules.
CC       Accumulates in the lamellipodium and ruffle membrane in response
CC       to hepatocyte growth factor (HGF) treatment. The MEMO1-RHOA-DIAPH1
CC       signaling pathway controls localization of the phosphorylated form
CC       to the cell membrane. {ECO:0000250|UniProtKB:P25054}.
CC   -!- DOMAIN: The microtubule tip localization signal (MtLS) motif;
CC       mediates interaction with MAPRE1 and targeting to the growing
CC       microtubule plus 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
CC       ZRANB1/TRABID (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the adenomatous polyposis coli (APC)
CC       family. {ECO:0000305}.
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DR   EMBL; D38629; BAA07609.1; -; mRNA.
DR   RefSeq; NP_036631.1; NM_012499.1.
DR   UniGene; Rn.156346; -.
DR   UniGene; Rn.88057; -.
DR   ProteinModelPortal; P70478; -.
DR   SMR; P70478; -.
DR   BioGrid; 246393; 6.
DR   CORUM; P70478; -.
DR   IntAct; P70478; 3.
DR   STRING; 10116.ENSRNOP00000027691; -.
DR   iPTMnet; P70478; -.
DR   PhosphoSitePlus; P70478; -.
DR   PaxDb; P70478; -.
DR   PRIDE; P70478; -.
DR   GeneID; 24205; -.
DR   KEGG; rno:24205; -.
DR   UCSC; RGD:2123; rat.
DR   CTD; 324; -.
DR   RGD; 2123; Apc.
DR   eggNOG; KOG2122; Eukaryota.
DR   eggNOG; ENOG410XR2V; LUCA.
DR   HOGENOM; HOG000033986; -.
DR   HOVERGEN; HBG004264; -.
DR   InParanoid; P70478; -.
DR   KO; K02085; -.
DR   PhylomeDB; P70478; -.
DR   PRO; PR:P70478; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0030424; C:axon; ISO:RGD.
DR   GO; GO:0044295; C:axonal growth cone; IDA:RGD.
DR   GO; GO:0030877; C:beta-catenin destruction complex; ISS:UniProtKB.
DR   GO; GO:0005923; C:bicellular tight junction; ISO:RGD.
DR   GO; GO:0016342; C:catenin complex; ISO:RGD.
DR   GO; GO:0070852; C:cell body fiber; IDA:RGD.
DR   GO; GO:0005938; C:cell cortex; IDA:RGD.
DR   GO; GO:0042995; C:cell projection; ISO:RGD.
DR   GO; GO:0031253; C:cell projection membrane; ISO:RGD.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR   GO; GO:0030425; C:dendrite; IDA:RGD.
DR   GO; GO:0030426; C:growth cone; IDA:RGD.
DR   GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR   GO; GO:0030027; C:lamellipodium; IDA:RGD.
DR   GO; GO:0016328; C:lateral plasma membrane; ISO:RGD.
DR   GO; GO:0005874; C:microtubule; IDA:RGD.
DR   GO; GO:0044306; C:neuron projection terminus; IDA:RGD.
DR   GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR   GO; GO:0031965; C:nuclear membrane; IDA:RGD.
DR   GO; GO:0005634; C:nucleus; IDA:RGD.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0043234; C:protein complex; IDA:RGD.
DR   GO; GO:0032587; C:ruffle membrane; ISS:UniProtKB.
DR   GO; GO:0034750; C:Scrib-APC-beta-catenin complex; ISO:RGD.
DR   GO; GO:0008013; F:beta-catenin binding; ISS:UniProtKB.
DR   GO; GO:0070840; F:dynein complex binding; ISO:RGD.
DR   GO; GO:0045295; F:gamma-catenin binding; ISO:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0008017; F:microtubule binding; IDA:RGD.
DR   GO; GO:0051010; F:microtubule plus-end binding; ISS:UniProtKB.
DR   GO; GO:0002020; F:protease binding; ISO:RGD.
DR   GO; GO:0032403; F:protein complex binding; IDA:RGD.
DR   GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR   GO; GO:0019887; F:protein kinase regulator activity; ISS:UniProtKB.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR   GO; GO:0009952; P:anterior/posterior pattern specification; ISO:RGD.
DR   GO; GO:0009798; P:axis specification; ISO:RGD.
DR   GO; GO:0007409; P:axonogenesis; ISO:RGD.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; ISO:RGD.
DR   GO; GO:0044336; P:canonical Wnt signaling pathway involved in negative regulation of apoptotic process; ISO:RGD.
DR   GO; GO:0044337; P:canonical Wnt signaling pathway involved in positive regulation of apoptotic process; ISO:RGD.
DR   GO; GO:0007050; P:cell cycle arrest; ISS:UniProtKB.
DR   GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR   GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEP:RGD.
DR   GO; GO:0051276; P:chromosome organization; ISO:RGD.
DR   GO; GO:0031122; P:cytoplasmic microtubule organization; ISO:RGD.
DR   GO; GO:0009953; P:dorsal/ventral pattern formation; ISO:RGD.
DR   GO; GO:0007163; P:establishment or maintenance of cell polarity; IDA:RGD.
DR   GO; GO:0001942; P:hair follicle development; ISO:RGD.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; ISO:RGD.
DR   GO; GO:0001822; P:kidney development; ISO:RGD.
DR   GO; GO:0007091; P:metaphase/anaphase transition of mitotic cell cycle; ISO:RGD.
DR   GO; GO:0000281; P:mitotic cytokinesis; ISO:RGD.
DR   GO; GO:0007094; P:mitotic spindle assembly checkpoint; ISO:RGD.
DR   GO; GO:0046716; P:muscle cell cellular homeostasis; ISO:RGD.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:RGD.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
DR   GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; ISS:UniProtKB.
DR   GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISO:RGD.
DR   GO; GO:0060770; P:negative regulation of epithelial cell proliferation involved in prostate gland development; ISO:RGD.
DR   GO; GO:0043409; P:negative regulation of MAPK cascade; ISO:RGD.
DR   GO; GO:0007026; P:negative regulation of microtubule depolymerization; ISS:UniProtKB.
DR   GO; GO:0042483; P:negative regulation of odontogenesis; ISO:RGD.
DR   GO; GO:0030178; P:negative regulation of Wnt signaling pathway; ISO:RGD.
DR   GO; GO:0031175; P:neuron projection development; IMP:RGD.
DR   GO; GO:0031016; P:pancreas development; IEP:RGD.
DR   GO; GO:0007389; P:pattern specification process; ISO:RGD.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
DR   GO; GO:0045785; P:positive regulation of cell adhesion; ISO:RGD.
DR   GO; GO:0010942; P:positive regulation of cell death; ISO:RGD.
DR   GO; GO:0045597; P:positive regulation of cell differentiation; ISO:RGD.
DR   GO; GO:0051781; P:positive regulation of cell division; ISO:RGD.
DR   GO; GO:0030335; P:positive regulation of cell migration; ISO:RGD.
DR   GO; GO:0030858; P:positive regulation of epithelial cell differentiation; ISO:RGD.
DR   GO; GO:0031116; P:positive regulation of microtubule polymerization; ISO:RGD.
DR   GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:RGD.
DR   GO; GO:1904781; P:positive regulation of protein localization to centrosome; ISO:RGD.
DR   GO; GO:0031274; P:positive regulation of pseudopodium assembly; ISO:RGD.
DR   GO; GO:0006461; P:protein complex assembly; ISS:UniProtKB.
DR   GO; GO:0051260; P:protein homooligomerization; ISO:RGD.
DR   GO; GO:0009954; P:proximal/distal pattern formation; ISO:RGD.
DR   GO; GO:0051988; P:regulation of attachment of spindle microtubules to kinetochore; ISO:RGD.
DR   GO; GO:0051726; P:regulation of cell cycle; ISO:RGD.
DR   GO; GO:0045595; P:regulation of cell differentiation; ISO:RGD.
DR   GO; GO:0030334; P:regulation of cell migration; ISO:RGD.
DR   GO; GO:0030856; P:regulation of epithelial cell differentiation; ISO:RGD.
DR   GO; GO:2000211; P:regulation of glutamate metabolic process; IDA:RGD.
DR   GO; GO:0032886; P:regulation of microtubule-based process; ISS:UniProtKB.
DR   GO; GO:0051171; P:regulation of nitrogen compound metabolic process; ISO:RGD.
DR   GO; GO:0045667; P:regulation of osteoblast differentiation; ISO:RGD.
DR   GO; GO:0045670; P:regulation of osteoclast differentiation; ISO:RGD.
DR   GO; GO:0097305; P:response to alcohol; IEP:RGD.
DR   GO; GO:0042493; P:response to drug; IEP:RGD.
DR   GO; GO:0060041; P:retina development in camera-type eye; ISO:RGD.
DR   GO; GO:0043588; P:skin development; ISO:RGD.
DR   GO; GO:0035019; P:somatic stem cell population maintenance; ISO:RGD.
DR   GO; GO:0019827; P:stem cell population maintenance; ISO:RGD.
DR   GO; GO:0033077; P:T cell differentiation in thymus; ISO:RGD.
DR   GO; GO:0048538; P:thymus development; ISO:RGD.
DR   GO; GO:0016055; P:Wnt signaling pathway; ISO:RGD.
DR   Gene3D; 1.25.10.10; -; 3.
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; 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; 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   Acetylation; Cell junction; Cell membrane; Cell projection;
KW   Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Membrane;
KW   Microtubule; Phosphoprotein; Reference proteome; Repeat;
KW   Tumor suppressor; Ubl conjugation; Wnt signaling pathway.
FT   INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:P25054}.
FT   CHAIN         2   2842       Adenomatous polyposis coli protein.
FT                                /FTId=PRO_0000064629.
FT   REPEAT      451    493       ARM 1.
FT   REPEAT      503    545       ARM 2.
FT   REPEAT      546    589       ARM 3.
FT   REPEAT      590    636       ARM 4.
FT   REPEAT      637    681       ARM 5.
FT   REPEAT      682    723       ARM 6.
FT   REPEAT      724    765       ARM 7.
FT   REGION     1864   1891       Highly charged.
FT   COILED        2     62       {ECO:0000255}.
FT   COILED      125    260       {ECO:0000255}.
FT   MOTIF      2802   2805       Microtubule tip localization signal.
FT   MOTIF      2840   2842       PDZ-binding. {ECO:0000250}.
FT   COMPBIAS      1    728       Leu-rich.
FT   COMPBIAS    739   2831       Ser-rich.
FT   COMPBIAS   1130   1155       Asp/Glu-rich (acidic).
FT   COMPBIAS   1556   1575       Asp/Glu-rich (acidic).
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000250|UniProtKB:P25054}.
FT   MOD_RES     105    105       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q61315}.
FT   MOD_RES     109    109       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q61315}.
FT   MOD_RES     742    742       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     746    746       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P25054}.
FT   MOD_RES     778    778       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     906    906       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P25054}.
FT   MOD_RES     985    985       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES    1036   1036       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q61315}.
FT   MOD_RES    1040   1040       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES    1357   1357       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P25054}.
FT   MOD_RES    1368   1368       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES    1382   1382       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P25054}.
FT   MOD_RES    1389   1389       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q61315}.
FT   MOD_RES    1392   1392       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q61315}.
FT   MOD_RES    1435   1435       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P25054}.
FT   MOD_RES    1565   1565       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES    1714   1714       Phosphoserine.
FT                                {ECO:0000244|PubMed:16641100}.
FT   MOD_RES    1772   1772       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P25054}.
FT   MOD_RES    1859   1859       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES    1861   1861       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P25054}.
FT   MOD_RES    1862   1862       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P25054}.
FT   MOD_RES    1969   1969       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q61315}.
FT   MOD_RES    1971   1971       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q61315}.
FT   MOD_RES    2087   2087       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES    2092   2092       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES    2125   2125       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q61315}.
FT   MOD_RES    2129   2129       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES    2130   2130       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES    2132   2132       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES    2151   2151       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P25054}.
FT   MOD_RES    2260   2260       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P25054}.
FT   MOD_RES    2270   2270       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P25054}.
FT   MOD_RES    2283   2283       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P25054}.
FT   MOD_RES    2473   2473       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P25054}.
FT   MOD_RES    2535   2535       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P25054}.
FT   MOD_RES    2569   2569       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P25054}.
FT   MOD_RES    2671   2671       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P25054}.
FT   MOD_RES    2674   2674       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P25054}.
FT   MOD_RES    2679   2679       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P25054}.
FT   MOD_RES    2710   2710       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES    2723   2723       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P25054}.
FT   MOD_RES    2788   2788       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P25054}.
FT   MUTAGEN     523    523       C->R: In an IQ-induced colon tumor.
FT                                {ECO:0000269|PubMed:7846077}.
SQ   SEQUENCE   2842 AA;  310533 MW;  3CBB2EA8A34E8F47 CRC64;
     MAAASYDQLL KQVEALKMEN SNLRQELEDN SNHLTELETE ASNMKEVLKQ LQGSIEDETM
     TSGQIDLLER LKEFNLDSNF PGVKLRSKMS LRSYGSREGS VSSRSGECSP VPMGSFPRRA
     FVNGSRESTG YLEELEKERS LLLADLDKEE KEKDWYYAQL QNLTKRIDSL PLTENFSLQT
     DMTRRQLEYE ARQIRAAMEE QLGTCQDMEK RAQRRIARIQ QIEKDILRVR QLLQSQAAEA
     ERSSQSKHET ASHEAERQLE GQGVAESNLA TSGSGQSSAA RVDHETAGVL SSSGTHSAPR
     RLTSHLGTKV EMVYSLLSML GTHDKDDMSR TLLAMSSSQD SCISMRQSGC LPLLIQLLHG
     NDKDSVLLGN SRGSKEARAR ASAALHNIIH SQPDDKRGRR EIRVLHLLEQ IRAYCETCWE
     WQEAHEQGMD QDKNPMPAPV EHQICPAVCV LMKLSFDEEH RHAMNELGGL QAIAELLQVD
     CEMHGLTDDH 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 QNLYGDYVFD ASRHDDNRSD NFNTGNMTVL SPYLNTTVLP SSSSSRGSLD
     SSRSEKDRSL ERERGIGLST YHSATENPGT SSKRGLQLSA TAAQIAKVME EVSALHTSQD
     DRSPASAAEL HCVAEERTAA RRSSASHTHP NTHNFAKSES SNRTCSMPYA KVEYKRSSND
     SLNSVTSSDG YGKRGQMKPS VESYSEDDEG KFCSYGQYPA DLAHKIHSAN HMDDNGGELD
     TPINYSLKYS DEQLNSGRQS PSQNERWARP KHVIEDEIKQ NEQRQSRSQN TNFPVYSENT
     DDKHLKFQQH FGQQECVSPY RSRGTNGSET NRMGSSHAVN QNVNQSLCQE DDYEDDKPTN
     YSERYSEEEQ HEEEERPTNY SIKYNEEKHH VDQPIDYSLK YATDISSSQK PSFSFSKTPS
     VQGTKTEHNS PSSEAASAPS SNAKRQSQLH PSSAQRNGQT PKGTACKVPS INQETMQTYC
     VEDTPICFSR CSSLSSLSSA EDEIGCDQTT QEADSANTLQ IAEIKENDVT RSAQDPASDV
     PAVSQSTRTK PSRLQASGLA SESARHKAVE FSSGAKSPSK SGAQTPKSPP EHYVQETPLV
     FSRCTSVSSL DSFESRSIAS SVQSEPCSGM VSGIVSPSDL PDSPGQTMPP SRSKTPPPPP
     PPQPVQTKRE VPKTKVPAAE QREGGPKQTA VSAAVQRVQV LPDADTLLHF ATESTPDGFS
     CSSSLSALSL DEPFIQKDVE LRIMPPVQEN DNGNETEPEQ PEESNENQDK EVEKPDSEKD
     LLDDSDDDDI EILEECIISA MPTKSSRKAK KLAQTASKLP PPVARKPSQL PVYKLLPSQS
     RLQAQKHVSF TPGDDVPRVY CVEGTPINFS TATSLSDLTI ESPPNELAAG DGVRASVQSG
     EFEKRDTIPT EGRSTDEAQR GKVSSIAIPD LDGSKAEEGD ILAECINSAL PKGRSHKPFR
     VKKIMDQVQQ ASMTSSGTNK NQIDTKKKKP TSPVKPMPQN TEYRTRVRKN TDSKVNVNTE
     ETFSDNKDSK KQSLKNNPKD LNDKLPDNED RVRGGFTFDS PHHYAPIEGT PYCFSRNDSL
     SSLDFDDDDV DLSREKAELR KGKESKDSEA KVTCHTEPSS SQQSARKAQA STKHPVNRGP
     SKPLLQEQPT FPQSSKDVPD RGAATDEKLQ NFAIENTPVC FSRNSSLSSL SDVDQENNNN
     EETGPVRDAE PANAQGQPGK PQASGYAPKS FHVEDTPVCF SRNSSLSSLS IDSEDDLLRE
     CISSAMPKKR RPSRLKGEGE WQSPRKVGSV LAEDLTLDLK DIQRPESEHG LSPDSENFDW
     KAIQEGANSI VSSLHQAAAA AACLSRQASS DSDSILSLKS GVSLGSPFHL TPDQEEKPFT
     SHKGPRILKP GEKSTLEAKK IESENKGIKG GKKVYKSLIT GKIRSNSEIS SQMKQPLQTN
     MPSISRGRTM IHIPGVRNSS SSTSPVSKKG PPLKTPASKS PSEGPVATTS PRGTKPAVKS
     ELSPITRQTS HISGSNKGPS RSGSRDSTPS RPTQQPLSRP MQSPGRNSIS PGRNGISTPN
     KLSQLPRTSS PSTASTKSSG SGKMSYTSPG RQLSQQNLSK QTGLSKNASS IPRSESASKG
     LNQMNNSNGS NKKVELSRMS STKSSGSESD RSERPALVRQ STFIKEAPSP TLRRKLEESA
     SFESLSPSSR PDSPTRSQAQ TPVLSPSLPD MSLSTHPSVQ AGGWRKLPPN LSPTIEYSDG
     RPSKRHDIAR SHSESPSRLP VNRAGTWKRE HSKHSSSLPR VSTWRRTGSS SSILSASSES
     SEKAKSEDEK HVNSVPGPRQ MKENQVPTKG TWRKIKESEI SPTNTVSQTT SSGAASGAES
     KTLIYQMAPA VSRTEDVWVR IEDCPINNPR SGRSPTGNTP PVIDSISEKG NPSIKDSKDT
     QGKQSVGSGS PVQTVGLENR LNSFIQVEAP EQKGTETKAG QGSPAPVAET GETCMAERTP
     FSSSSSSKHS SPSGTVAARV TPFNYNPSPR KSSADSTSAR PSQIPTPVGS STKKRDSKTD
     STESSGAQSP KRHSGSYLVT SV
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