Reviewed, UniProtKB/Swiss-Prot P70478 (APC_RAT)

Names and origin

Protein names

Recommended name:
    Adenomatous polyposis coli protein
      Short name=Protein APC

Gene names

Name:

Apc

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	2842 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Tumor suppressor. Promotes rapid degradation of CTNNB1 and participates in Wnt signaling. APC activity is correlated with its phosphorylation state By similarity.
Subunit structure	Forms homooligomers and heterooligomers with APC2. Interacts with PDZ domains of DLG1 and DLG3. Associates with catenins. Binds axin. Interacts with the N-terminus of ARHGEF4, and the C-terminus of MAPRE1, MAPRE2 and MAPRE3. Found in a complex consisting of ARHGEF4, APC and CTNNB1. Interacts with DIAPH1 and DIAPH2. Interacts with APC2 By similarity.
Post-translational modification	Phosphorylated by GSK3B By similarity.
Sequence similarities	Belongs to the adenomatous polyposis coli (APC) family. Contains 7 ARM repeats.

Ontologies

Keywords
Biological process	Cell cycle Wnt signaling pathway
Domain	Coiled coil Repeat
Molecular function	Anti-oncogene
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	Wnt receptor signaling pathway Inferred from electronic annotation. Source: InterPro cell cycle arrest Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of cell proliferation Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of cyclin-dependent protein kinase activity Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of microtubule depolymerization Inferred from sequence or structural similarity. Source: UniProtKB protein complex assembly Inferred from sequence or structural similarity. Source: UniProtKB response to DNA damage stimulus Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	beta-catenin destruction complex Inferred from sequence or structural similarity. Source: UniProtKB centrosome Inferred from sequence or structural similarity. Source: UniProtKB kinetochore Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	beta-catenin binding Inferred from sequence or structural similarity. Source: UniProtKB microtubule binding Inferred from sequence or structural similarity. Source: UniProtKB protein kinase CK2 regulator activity Inferred from sequence or structural similarity. Source: UniProtKB protein kinase binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Dlg4	P31016	2	EBI-631663,EBI-375655

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2842	2842	Adenomatous polyposis coli protein		PRO_0000064629
Regions
	Repeat	451 – 493	43	ARM 1
	Repeat	503 – 545	43	ARM 2
	Repeat	546 – 589	44	ARM 3
	Repeat	590 – 636	47	ARM 4
	Repeat	637 – 681	45	ARM 5
	Repeat	682 – 723	42	ARM 6
	Repeat	724 – 765	42	ARM 7
	Region	1864 – 1891	28	Highly charged
	Coiled coil	1 – 62	62	Potential
	Coiled coil	125 – 260	136	Potential
	Motif	2840 – 2842	3	PDZ-binding By similarity
	Compositional bias	1 – 728	728	Leu-rich
	Compositional bias	739 – 2831	2093	Ser-rich
	Compositional bias	1130 – 1155	26	Asp/Glu-rich (acidic)
	Compositional bias	1556 – 1575	20	Asp/Glu-rich (acidic)
Amino acid modifications
	Modified residue	1036	1	Phosphoserine By similarity
	Modified residue	1178	1	Phosphoserine
	Modified residue	1368	1	Phosphoserine By similarity
	Modified residue	1695	1	Phosphothreonine
	Modified residue	1714	1	Phosphoserine
	Modified residue	1859	1	Phosphoserine By similarity
	Modified residue	1861	1	Phosphoserine By similarity
	Modified residue	1862	1	Phosphoserine By similarity
	Modified residue	2125	1	Phosphoserine By similarity
	Modified residue	2283	1	Phosphoserine By similarity
	Modified residue	2398	1	Phosphoserine By similarity
	Modified residue	2671	1	Phosphoserine By similarity
	Modified residue	2674	1	Phosphoserine By similarity
	Modified residue	2676	1	Phosphothreonine By similarity
	Modified residue	2710	1	Phosphoserine By similarity
	Modified residue	2788	1	Phosphoserine By similarity
	Modified residue	2834	1	Phosphoserine By similarity
	Modified residue	2836	1	Phosphoserine By similarity
	Modified residue	2837	1	Phosphotyrosine By similarity
Experimental info
	Mutagenesis	523	1	C → R in an IQ-induced colon tumor

Sequences

	Sequence		Length	Mass (Da)
	P70478-1 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 3CBB2EA8A34E8F47	FASTA	2,842	310,533
	10 20 30 40 50 60 MAAASYDQLL KQVEALKMEN SNLRQELEDN SNHLTELETE ASNMKEVLKQ LQGSIEDETM 70 80 90 100 110 120 TSGQIDLLER LKEFNLDSNF PGVKLRSKMS LRSYGSREGS VSSRSGECSP VPMGSFPRRA 130 140 150 160 170 180 FVNGSRESTG YLEELEKERS LLLADLDKEE KEKDWYYAQL QNLTKRIDSL PLTENFSLQT 190 200 210 220 230 240 DMTRRQLEYE ARQIRAAMEE QLGTCQDMEK RAQRRIARIQ QIEKDILRVR QLLQSQAAEA 250 260 270 280 290 300 ERSSQSKHET ASHEAERQLE GQGVAESNLA TSGSGQSSAA RVDHETAGVL SSSGTHSAPR 310 320 330 340 350 360 RLTSHLGTKV EMVYSLLSML GTHDKDDMSR TLLAMSSSQD SCISMRQSGC LPLLIQLLHG 370 380 390 400 410 420 NDKDSVLLGN SRGSKEARAR ASAALHNIIH SQPDDKRGRR EIRVLHLLEQ IRAYCETCWE 430 440 450 460 470 480 WQEAHEQGMD QDKNPMPAPV EHQICPAVCV LMKLSFDEEH RHAMNELGGL QAIAELLQVD 490 500 510 520 530 540 CEMHGLTDDH YSVTLRRYAG MALTNLTFGD VANKATLCSM KGCMRALVAQ LKSESEDLQQ 550 560 570 580 590 600 VIASVLRNLS WRADVNSKKT LREVGSVKAL MECALEVKKE STLKSVLSAL WNLSAHCTEN 610 620 630 640 650 660 KADICAVDGA LAFLVGTLTY RSQTNTLAII ESGGGILRNV SSLIATNEDH RQILRENNCL 670 680 690 700 710 720 QTLLQHLKSH SLTIVSNACG TLWNLSARNP KDQEALWDMG AVSMLKNLIH SKHKMIAMGS 730 740 750 760 770 780 AAALRNLMAN RPAKYKDANI MSPGSSLPSL HVRKQKALEA ELDAQHLSET FDNIDNLSPK 790 800 810 820 830 840 ASHRSKQRHK QNLYGDYVFD ASRHDDNRSD NFNTGNMTVL SPYLNTTVLP SSSSSRGSLD 850 860 870 880 890 900 SSRSEKDRSL ERERGIGLST YHSATENPGT SSKRGLQLSA TAAQIAKVME EVSALHTSQD 910 920 930 940 950 960 DRSPASAAEL HCVAEERTAA RRSSASHTHP NTHNFAKSES SNRTCSMPYA KVEYKRSSND 970 980 990 1000 1010 1020 SLNSVTSSDG YGKRGQMKPS VESYSEDDEG KFCSYGQYPA DLAHKIHSAN HMDDNGGELD 1030 1040 1050 1060 1070 1080 TPINYSLKYS DEQLNSGRQS PSQNERWARP KHVIEDEIKQ NEQRQSRSQN TNFPVYSENT 1090 1100 1110 1120 1130 1140 DDKHLKFQQH FGQQECVSPY RSRGTNGSET NRMGSSHAVN QNVNQSLCQE DDYEDDKPTN 1150 1160 1170 1180 1190 1200 YSERYSEEEQ HEEEERPTNY SIKYNEEKHH VDQPIDYSLK YATDISSSQK PSFSFSKTPS 1210 1220 1230 1240 1250 1260 VQGTKTEHNS PSSEAASAPS SNAKRQSQLH PSSAQRNGQT PKGTACKVPS INQETMQTYC 1270 1280 1290 1300 1310 1320 VEDTPICFSR CSSLSSLSSA EDEIGCDQTT QEADSANTLQ IAEIKENDVT RSAQDPASDV 1330 1340 1350 1360 1370 1380 PAVSQSTRTK PSRLQASGLA SESARHKAVE FSSGAKSPSK SGAQTPKSPP EHYVQETPLV 1390 1400 1410 1420 1430 1440 FSRCTSVSSL DSFESRSIAS SVQSEPCSGM VSGIVSPSDL PDSPGQTMPP SRSKTPPPPP 1450 1460 1470 1480 1490 1500 PPQPVQTKRE VPKTKVPAAE QREGGPKQTA VSAAVQRVQV LPDADTLLHF ATESTPDGFS 1510 1520 1530 1540 1550 1560 CSSSLSALSL DEPFIQKDVE LRIMPPVQEN DNGNETEPEQ PEESNENQDK EVEKPDSEKD 1570 1580 1590 1600 1610 1620 LLDDSDDDDI EILEECIISA MPTKSSRKAK KLAQTASKLP PPVARKPSQL PVYKLLPSQS 1630 1640 1650 1660 1670 1680 RLQAQKHVSF TPGDDVPRVY CVEGTPINFS TATSLSDLTI ESPPNELAAG DGVRASVQSG 1690 1700 1710 1720 1730 1740 EFEKRDTIPT EGRSTDEAQR GKVSSIAIPD LDGSKAEEGD ILAECINSAL PKGRSHKPFR 1750 1760 1770 1780 1790 1800 VKKIMDQVQQ ASMTSSGTNK NQIDTKKKKP TSPVKPMPQN TEYRTRVRKN TDSKVNVNTE 1810 1820 1830 1840 1850 1860 ETFSDNKDSK KQSLKNNPKD LNDKLPDNED RVRGGFTFDS PHHYAPIEGT PYCFSRNDSL 1870 1880 1890 1900 1910 1920 SSLDFDDDDV DLSREKAELR KGKESKDSEA KVTCHTEPSS SQQSARKAQA STKHPVNRGP 1930 1940 1950 1960 1970 1980 SKPLLQEQPT FPQSSKDVPD RGAATDEKLQ NFAIENTPVC FSRNSSLSSL SDVDQENNNN 1990 2000 2010 2020 2030 2040 EETGPVRDAE PANAQGQPGK PQASGYAPKS FHVEDTPVCF SRNSSLSSLS IDSEDDLLRE 2050 2060 2070 2080 2090 2100 CISSAMPKKR RPSRLKGEGE WQSPRKVGSV LAEDLTLDLK DIQRPESEHG LSPDSENFDW 2110 2120 2130 2140 2150 2160 KAIQEGANSI VSSLHQAAAA AACLSRQASS DSDSILSLKS GVSLGSPFHL TPDQEEKPFT 2170 2180 2190 2200 2210 2220 SHKGPRILKP GEKSTLEAKK IESENKGIKG GKKVYKSLIT GKIRSNSEIS SQMKQPLQTN 2230 2240 2250 2260 2270 2280 MPSISRGRTM IHIPGVRNSS SSTSPVSKKG PPLKTPASKS PSEGPVATTS PRGTKPAVKS 2290 2300 2310 2320 2330 2340 ELSPITRQTS HISGSNKGPS RSGSRDSTPS RPTQQPLSRP MQSPGRNSIS PGRNGISTPN 2350 2360 2370 2380 2390 2400 KLSQLPRTSS PSTASTKSSG SGKMSYTSPG RQLSQQNLSK QTGLSKNASS IPRSESASKG 2410 2420 2430 2440 2450 2460 LNQMNNSNGS NKKVELSRMS STKSSGSESD RSERPALVRQ STFIKEAPSP TLRRKLEESA 2470 2480 2490 2500 2510 2520 SFESLSPSSR PDSPTRSQAQ TPVLSPSLPD MSLSTHPSVQ AGGWRKLPPN LSPTIEYSDG 2530 2540 2550 2560 2570 2580 RPSKRHDIAR SHSESPSRLP VNRAGTWKRE HSKHSSSLPR VSTWRRTGSS SSILSASSES 2590 2600 2610 2620 2630 2640 SEKAKSEDEK HVNSVPGPRQ MKENQVPTKG TWRKIKESEI SPTNTVSQTT SSGAASGAES 2650 2660 2670 2680 2690 2700 KTLIYQMAPA VSRTEDVWVR IEDCPINNPR SGRSPTGNTP PVIDSISEKG NPSIKDSKDT 2710 2720 2730 2740 2750 2760 QGKQSVGSGS PVQTVGLENR LNSFIQVEAP EQKGTETKAG QGSPAPVAET GETCMAERTP 2770 2780 2790 2800 2810 2820 FSSSSSSKHS SPSGTVAARV TPFNYNPSPR KSSADSTSAR PSQIPTPVGS STKKRDSKTD 2830 2840 STESSGAQSP KRHSGSYLVT SV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA cloning of the rat APC gene and assignment to chromosome 18." Toyota M., Ushijima T., Kakiuchi H., Watanabe M., Imai K., Yachi A., Sugimura T., Nagao M. Mamm. Genome 6:746-748(1995) [PubMed: 8563176] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Fischer 344/N. Tissue: Brain.
[2]	"Specific 5'-GGGA-3'-->5'-GGA-3' mutation of the Apc gene in rat colon tumors induced by 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine." Kakiuchi H., Watanabe M., Ushijima T., Toyota M., Imai K., Weisburger J.H., Sugimura T., Nagao M. Proc. Natl. Acad. Sci. U.S.A. 92:910-914(1995) [PubMed: 7846077] [Abstract] Cited for: MUTAGENESIS. Strain: Fischer 344/N and Sprague-Dawley.
[3]	"Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites." Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A. Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed: 16641100] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1178; THR-1695 AND SER-1714, MASS SPECTROMETRY. Tissue: Kidney.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D38629 mRNA. Translation: BAA07609.1.
RefSeq	NP_036631.1.
UniGene	Rn.88057
3D structure databases
HSSP	HSSP built from PDB template 1M5I based on UniProtKB P25054.
SMR	P70478. Positions 2-55, 128-237.
ModBase	Search...
Protein-protein interaction databases
IntAct	P70478.
PTM databases
PhosphoSite	P70478.
Genome annotation databases
Ensembl	ENSRNOG00000020423. Rattus norvegicus. [Contig view]
GeneID	24205.
KEGG	rno:24205.
Organism-specific databases
RGD	2123. Apc.
Phylogenomic databases
HOVERGEN	P70478.
Gene expression databases
ArrayExpress	P70478.
GermOnline	ENSRNOG00000020423. Rattus norvegicus.
Family and domain databases
InterPro	IPR009240. APC_15aa. IPR009234. APC_basic. IPR009223. APC_crr. IPR011989. ARM-like. IPR000225. Armadillo. IPR009232. EB1_bd. IPR009224. SAMP. [Graphical view]
Gene3D	G3DSA:1.25.10.10. ARM-like. 1 hit.
Pfam	PF05972. APC_15aa. 4 hits. PF05956. APC_basic. 1 hit. PF05923. APC_crr. 7 hits. PF00514. Arm. 4 hits. PF05937. EB1_binding. 1 hit. PF05924. SAMP. 3 hits. [Graphical view]
SMART	SM00185. ARM. 6 hits. [Graphical view]
PROSITE	PS50176. ARM_REPEAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	602593.

Entry information

Entry name

APC_RAT

Accession

Primary (citable) accession number: P70478

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	February 1, 1997
Last modified:	November 25, 2008
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)