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UniProtKB - P70478 (APC_RAT)

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Protein

Adenomatous polyposis coli protein

Gene

Apc

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. 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).By similarity

GO - Molecular functioni

  • beta-catenin binding Source: UniProtKB
  • microtubule binding Source: RGD
  • microtubule plus-end binding Source: UniProtKB
  • protein complex binding Source: RGD
  • protein kinase regulator activity Source: UniProtKB
Complete GO annotation...

GO - Biological processi

Complete GO annotation...

Keywordsi

Biological processWnt signaling pathway

Names & Taxonomyi

Protein namesi
Recommended name:
Adenomatous polyposis coli protein
Short name:
Protein APC
Gene namesi
Name:Apc
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2123. Apc.

Subcellular locationi

  • Cell junction › adherens junction By similarity
  • Cytoplasm › cytoskeleton By similarity
  • Cell projection › lamellipodium By similarity
  • Cell projection › ruffle membrane By similarity
  • Cytoplasm By similarity
  • Cell membrane By similarity

    • 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.By similarity

GO - Cellular componenti

  • adherens junction Source: UniProtKB-SubCell
  • axonal growth cone Source: RGD
  • beta-catenin destruction complex Source: UniProtKB
  • cell body fiber Source: RGD
  • cell cortex Source: RGD
  • centrosome Source: UniProtKB
  • cytoplasm Source: RGD
  • dendrite Source: RGD
  • growth cone Source: RGD
  • kinetochore Source: UniProtKB
  • lamellipodium Source: RGD
  • microtubule Source: RGD
  • neuronal cell body Source: RGD
  • neuron projection terminus Source: RGD
  • nuclear membrane Source: RGD
  • nucleus Source: RGD
  • plasma membrane Source: UniProtKB
  • protein complex Source: RGD
  • ruffle membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Microtubule

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi523C → R in an IQ-induced colon tumor. 1 Publication1

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000646292 – 2842Adenomatous polyposis coli proteinAdd BLAST2841

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei105PhosphoserineBy similarity1
Modified residuei109PhosphoserineBy similarity1
Modified residuei742PhosphoserineCombined sources1
Modified residuei746PhosphoserineBy similarity1
Modified residuei778PhosphoserineCombined sources1
Modified residuei906PhosphoserineBy similarity1
Modified residuei985PhosphoserineCombined sources1
Modified residuei1036PhosphoserineBy similarity1
Modified residuei1040PhosphoserineCombined sources1
Modified residuei1357PhosphoserineBy similarity1
Modified residuei1368PhosphoserineCombined sources1
Modified residuei1382PhosphoserineBy similarity1
Modified residuei1389PhosphoserineBy similarity1
Modified residuei1392PhosphoserineBy similarity1
Modified residuei1435PhosphothreonineBy similarity1
Modified residuei1565PhosphoserineCombined sources1
Modified residuei1714PhosphoserineCombined sources1
Modified residuei1772PhosphoserineBy similarity1
Modified residuei1859PhosphoserineCombined sources1
Modified residuei1861PhosphoserineBy similarity1
Modified residuei1862PhosphoserineBy similarity1
Modified residuei1969PhosphoserineBy similarity1
Modified residuei1971PhosphoserineBy similarity1
Modified residuei2087PhosphoserineCombined sources1
Modified residuei2092PhosphoserineCombined sources1
Modified residuei2125PhosphoserineBy similarity1
Modified residuei2129PhosphoserineCombined sources1
Modified residuei2130PhosphoserineCombined sources1
Modified residuei2132PhosphoserineCombined sources1
Modified residuei2151PhosphothreonineBy similarity1
Modified residuei2260PhosphoserineBy similarity1
Modified residuei2270PhosphoserineBy similarity1
Modified residuei2283PhosphoserineBy similarity1
Modified residuei2473PhosphoserineBy similarity1
Modified residuei2535PhosphoserineBy similarity1
Modified residuei2569PhosphoserineBy similarity1
Modified residuei2671PhosphoserineBy similarity1
Modified residuei2674PhosphoserineBy similarity1
Modified residuei2679PhosphothreonineBy similarity1
Modified residuei2710PhosphoserineCombined sources1
Modified residuei2723PhosphoserineBy similarity1
Modified residuei2788PhosphoserineBy similarity1

Post-translational modificationi

Phosphorylated by GSK3B.By similarity
Ubiquitinated, leading to its degradation by the proteasome. Ubiquitination is facilitated by Axin. Deubiquitinated by ZRANB1/TRABID (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP70478.
PRIDEiP70478.

PTM databases

iPTMnetiP70478.
PhosphoSitePlusiP70478.

Interactioni

Subunit structurei

Forms homooligomers and heterooligomers with APC2. Interacts with DIAPH1 and DIAPH2. Interacts with PDZ domains of DLG1 and DLG3. Associates with catenins. Binds axin. Interacts with ARHGEF4 (via N-terminus). Interacts with MAPRE1 (via C-terminus); probably required for APC targeting to the growing microtubule plus ends. Interacts with MAPRE2 and MAPRE3 (via C-terminus). Found in a complex consisting of ARHGEF4, APC and CTNNB1. Interacts with SCRIB; may mediate APC targeting to adherens junctions of epithelial cells. Interacts with SPATA13 (via N-terminus and SH3 domain). Interacts with ASAP1 (via SH3 domain). Interacts at the cell membrane with AMER1 and AMER2 (via ARM repeats) (By similarity). Found in a complex composed of MACF1, APC, AXIN1, CTNNB1 and GSK3B. Interacts with KHDRBS1 (By similarity). The complex composed, at least, of APC, CTNNB1 and GSK3B interacts with JPT1; the interaction requires the inactive form of GSK3B (phosphorylated at 'Ser-9') (By similarity).By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Dlg4P310162EBI-631663,EBI-375655

GO - Molecular functioni

  • beta-catenin binding Source: UniProtKB
  • microtubule binding Source: RGD
  • microtubule plus-end binding Source: UniProtKB
  • protein complex binding Source: RGD
Complete GO annotation...

Protein-protein interaction databases

BioGridi246393. 6 interactors.
IntActiP70478. 3 interactors.
STRINGi10116.ENSRNOP00000027691.

Structurei

3D structure databases

ProteinModelPortaliP70478.
SMRiP70478.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati451 – 493ARM 1Add BLAST43
Repeati503 – 545ARM 2Add BLAST43
Repeati546 – 589ARM 3Add BLAST44
Repeati590 – 636ARM 4Add BLAST47
Repeati637 – 681ARM 5Add BLAST45
Repeati682 – 723ARM 6Add BLAST42
Repeati724 – 765ARM 7Add BLAST42

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1864 – 1891Highly chargedAdd BLAST28

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili2 – 62Sequence analysisAdd BLAST61
Coiled coili125 – 260Sequence analysisAdd BLAST136

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi2802 – 2805Microtubule tip localization signal4
Motifi2840 – 2842PDZ-bindingBy similarity3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1 – 728Leu-richAdd BLAST728
Compositional biasi739 – 2831Ser-richAdd BLAST2093
Compositional biasi1130 – 1155Asp/Glu-rich (acidic)Add BLAST26
Compositional biasi1556 – 1575Asp/Glu-rich (acidic)Add BLAST20

Domaini

The microtubule tip localization signal (MtLS) motif; mediates interaction with MAPRE1 and targeting to the growing microtubule plus ends.By similarity

Sequence similaritiesi

Belongs to the adenomatous polyposis coli (APC) family.Curated

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiKOG2122. Eukaryota.
ENOG410XR2V. LUCA.
HOGENOMiHOG000033986.
HOVERGENiHBG004264.
InParanoidiP70478.
KOiK02085.
PhylomeDBiP70478.

Family and domain databases

Gene3Di1.25.10.10. 3 hits.
InterProiView protein in InterPro
IPR026836. APC.
IPR009240. APC_15aa_rpt.
IPR009234. APC_basic_dom.
IPR026831. APC_dom.
IPR026818. Apc_fam.
IPR032038. APC_N.
IPR009223. APC_rpt.
IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR009232. EB1-bd.
IPR009224. SAMP.
PANTHERiPTHR12607. PTHR12607. 1 hit.
PTHR12607:SF13. PTHR12607:SF13. 1 hit.
PfamiView protein in Pfam
PF05972. APC_15aa. 3 hits.
PF05956. APC_basic. 1 hit.
PF16689. APC_N_CC. 1 hit.
PF05923. APC_r. 7 hits.
PF00514. Arm. 2 hits.
PF05937. EB1_binding. 1 hit.
PF05924. SAMP. 3 hits.
SMARTiView protein in SMART
SM00185. ARM. 7 hits.
SUPFAMiSSF48371. SSF48371. 1 hit.
SSF58050. SSF58050. 1 hit.
SSF82931. SSF82931. 1 hit.
PROSITEiView protein in PROSITE
PS50176. ARM_REPEAT. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P70478-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAASYDQLL KQVEALKMEN SNLRQELEDN SNHLTELETE ASNMKEVLKQ 
        60         70         80         90        100
LQGSIEDETM TSGQIDLLER LKEFNLDSNF PGVKLRSKMS LRSYGSREGS 
       110        120        130        140        150
VSSRSGECSP VPMGSFPRRA FVNGSRESTG YLEELEKERS LLLADLDKEE 
       160        170        180        190        200
KEKDWYYAQL QNLTKRIDSL PLTENFSLQT DMTRRQLEYE ARQIRAAMEE 
       210        220        230        240        250
QLGTCQDMEK RAQRRIARIQ QIEKDILRVR QLLQSQAAEA ERSSQSKHET 
       260        270        280        290        300
ASHEAERQLE GQGVAESNLA TSGSGQSSAA RVDHETAGVL SSSGTHSAPR 
       310        320        330        340        350
RLTSHLGTKV EMVYSLLSML GTHDKDDMSR TLLAMSSSQD SCISMRQSGC 
       360        370        380        390        400
LPLLIQLLHG NDKDSVLLGN SRGSKEARAR ASAALHNIIH SQPDDKRGRR 
       410        420        430        440        450
EIRVLHLLEQ IRAYCETCWE WQEAHEQGMD QDKNPMPAPV EHQICPAVCV 
       460        470        480        490        500
LMKLSFDEEH RHAMNELGGL QAIAELLQVD CEMHGLTDDH YSVTLRRYAG 
       510        520        530        540        550
MALTNLTFGD VANKATLCSM KGCMRALVAQ LKSESEDLQQ VIASVLRNLS 
       560        570        580        590        600
WRADVNSKKT LREVGSVKAL MECALEVKKE STLKSVLSAL WNLSAHCTEN 
       610        620        630        640        650
KADICAVDGA LAFLVGTLTY RSQTNTLAII ESGGGILRNV SSLIATNEDH 
       660        670        680        690        700
RQILRENNCL QTLLQHLKSH SLTIVSNACG TLWNLSARNP KDQEALWDMG 
       710        720        730        740        750
AVSMLKNLIH SKHKMIAMGS AAALRNLMAN RPAKYKDANI MSPGSSLPSL 
       760        770        780        790        800
HVRKQKALEA ELDAQHLSET FDNIDNLSPK ASHRSKQRHK QNLYGDYVFD 
       810        820        830        840        850
ASRHDDNRSD NFNTGNMTVL SPYLNTTVLP SSSSSRGSLD SSRSEKDRSL 
       860        870        880        890        900
ERERGIGLST YHSATENPGT SSKRGLQLSA TAAQIAKVME EVSALHTSQD 
       910        920        930        940        950
DRSPASAAEL HCVAEERTAA RRSSASHTHP NTHNFAKSES SNRTCSMPYA 
       960        970        980        990       1000
KVEYKRSSND SLNSVTSSDG YGKRGQMKPS VESYSEDDEG KFCSYGQYPA 
      1010       1020       1030       1040       1050
DLAHKIHSAN HMDDNGGELD TPINYSLKYS DEQLNSGRQS PSQNERWARP 
      1060       1070       1080       1090       1100
KHVIEDEIKQ NEQRQSRSQN TNFPVYSENT DDKHLKFQQH FGQQECVSPY 
      1110       1120       1130       1140       1150
RSRGTNGSET NRMGSSHAVN QNVNQSLCQE DDYEDDKPTN YSERYSEEEQ 
      1160       1170       1180       1190       1200
HEEEERPTNY SIKYNEEKHH VDQPIDYSLK YATDISSSQK PSFSFSKTPS 
      1210       1220       1230       1240       1250
VQGTKTEHNS PSSEAASAPS SNAKRQSQLH PSSAQRNGQT PKGTACKVPS 
      1260       1270       1280       1290       1300
INQETMQTYC VEDTPICFSR CSSLSSLSSA EDEIGCDQTT QEADSANTLQ 
      1310       1320       1330       1340       1350
IAEIKENDVT RSAQDPASDV PAVSQSTRTK PSRLQASGLA SESARHKAVE 
      1360       1370       1380       1390       1400
FSSGAKSPSK SGAQTPKSPP EHYVQETPLV FSRCTSVSSL DSFESRSIAS 
      1410       1420       1430       1440       1450
SVQSEPCSGM VSGIVSPSDL PDSPGQTMPP SRSKTPPPPP PPQPVQTKRE 
      1460       1470       1480       1490       1500
VPKTKVPAAE QREGGPKQTA VSAAVQRVQV LPDADTLLHF ATESTPDGFS 
      1510       1520       1530       1540       1550
CSSSLSALSL DEPFIQKDVE LRIMPPVQEN DNGNETEPEQ PEESNENQDK 
      1560       1570       1580       1590       1600
EVEKPDSEKD LLDDSDDDDI EILEECIISA MPTKSSRKAK KLAQTASKLP 
      1610       1620       1630       1640       1650
PPVARKPSQL PVYKLLPSQS RLQAQKHVSF TPGDDVPRVY CVEGTPINFS 
      1660       1670       1680       1690       1700
TATSLSDLTI ESPPNELAAG DGVRASVQSG EFEKRDTIPT EGRSTDEAQR 
      1710       1720       1730       1740       1750
GKVSSIAIPD LDGSKAEEGD ILAECINSAL PKGRSHKPFR VKKIMDQVQQ 
      1760       1770       1780       1790       1800
ASMTSSGTNK NQIDTKKKKP TSPVKPMPQN TEYRTRVRKN TDSKVNVNTE 
      1810       1820       1830       1840       1850
ETFSDNKDSK KQSLKNNPKD LNDKLPDNED RVRGGFTFDS PHHYAPIEGT 
      1860       1870       1880       1890       1900
PYCFSRNDSL SSLDFDDDDV DLSREKAELR KGKESKDSEA KVTCHTEPSS 
      1910       1920       1930       1940       1950
SQQSARKAQA STKHPVNRGP SKPLLQEQPT FPQSSKDVPD RGAATDEKLQ 
      1960       1970       1980       1990       2000
NFAIENTPVC FSRNSSLSSL SDVDQENNNN EETGPVRDAE PANAQGQPGK 
      2010       2020       2030       2040       2050
PQASGYAPKS FHVEDTPVCF SRNSSLSSLS IDSEDDLLRE CISSAMPKKR 
      2060       2070       2080       2090       2100
RPSRLKGEGE WQSPRKVGSV LAEDLTLDLK DIQRPESEHG LSPDSENFDW 
      2110       2120       2130       2140       2150
KAIQEGANSI VSSLHQAAAA AACLSRQASS DSDSILSLKS GVSLGSPFHL 
      2160       2170       2180       2190       2200
TPDQEEKPFT SHKGPRILKP GEKSTLEAKK IESENKGIKG GKKVYKSLIT 
      2210       2220       2230       2240       2250
GKIRSNSEIS SQMKQPLQTN MPSISRGRTM IHIPGVRNSS SSTSPVSKKG 
      2260       2270       2280       2290       2300
PPLKTPASKS PSEGPVATTS PRGTKPAVKS ELSPITRQTS HISGSNKGPS 
      2310       2320       2330       2340       2350
RSGSRDSTPS RPTQQPLSRP MQSPGRNSIS PGRNGISTPN KLSQLPRTSS 
      2360       2370       2380       2390       2400
PSTASTKSSG SGKMSYTSPG RQLSQQNLSK QTGLSKNASS IPRSESASKG 
      2410       2420       2430       2440       2450
LNQMNNSNGS NKKVELSRMS STKSSGSESD RSERPALVRQ STFIKEAPSP 
      2460       2470       2480       2490       2500
TLRRKLEESA SFESLSPSSR PDSPTRSQAQ TPVLSPSLPD MSLSTHPSVQ 
      2510       2520       2530       2540       2550
AGGWRKLPPN LSPTIEYSDG RPSKRHDIAR SHSESPSRLP VNRAGTWKRE 
      2560       2570       2580       2590       2600
HSKHSSSLPR VSTWRRTGSS SSILSASSES SEKAKSEDEK HVNSVPGPRQ 
      2610       2620       2630       2640       2650
MKENQVPTKG TWRKIKESEI SPTNTVSQTT SSGAASGAES KTLIYQMAPA 
      2660       2670       2680       2690       2700
VSRTEDVWVR IEDCPINNPR SGRSPTGNTP PVIDSISEKG NPSIKDSKDT 
      2710       2720       2730       2740       2750
QGKQSVGSGS PVQTVGLENR LNSFIQVEAP EQKGTETKAG QGSPAPVAET 
      2760       2770       2780       2790       2800
GETCMAERTP FSSSSSSKHS SPSGTVAARV TPFNYNPSPR KSSADSTSAR 
      2810       2820       2830       2840 
PSQIPTPVGS STKKRDSKTD STESSGAQSP KRHSGSYLVT SV
Length:2,842
Mass (Da):310,533
Last modified:February 1, 1997 - v1
Checksum:i3CBB2EA8A34E8F47
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D38629 mRNA. Translation: BAA07609.1.
RefSeqiNP_036631.1. NM_012499.1.
UniGeneiRn.156346.
Rn.88057.

Genome annotation databases

GeneIDi24205.
KEGGirno:24205.
UCSCiRGD:2123. rat.

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiAPC_RAT
AccessioniPrimary (citable) accession number: P70478
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: February 1, 1997
Last modified: June 7, 2017
This is version 149 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families