APCL_MOUSE
ID APCL_MOUSE Reviewed; 2274 AA.
AC Q9Z1K7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Adenomatous polyposis coli protein 2;
GN Name=Apc2;
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 [GENOMIC DNA].
RX PubMed=10021369; DOI=10.1016/s0960-9822(99)80024-4;
RA van Es J.H., Kirkpatrick C., van de Wetering M., Molenaar M., Miles A.,
RA Kuipers J., Destree O., Peifer M., Clevers H.;
RT "Identification of APC2, a homologue of the adenomatous polyposis coli
RT tumour suppressor.";
RL Curr. Biol. 9:105-108(1999).
RN [2]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15018807; DOI=10.1016/s1567-133x(01)00021-7;
RA Yamanaka H., Hashimoto N., Koyama K., Nakagawa H., Nakamura Y., Noguchi K.;
RT "Expression of Apc2 during mouse development.";
RL Gene Expr. Patterns 1:107-114(2002).
RN [3]
RP INTERACTION WITH PSRC1 AND MAPRE3.
RX PubMed=17310996; DOI=10.1038/sj.onc.1210304;
RA Hsieh P.-C., Chang J.-C., Sun W.-T., Hsieh S.-C., Wang M.-C., Wang F.-F.;
RT "p53 downstream target DDA3 is a novel microtubule-associated protein that
RT interacts with end-binding protein EB3 and activates beta-catenin
RT pathway.";
RL Oncogene 26:4928-4940(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1563; SER-1565 AND SER-1861,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=25753423; DOI=10.1016/j.celrep.2015.02.011;
RA Almuriekhi M., Shintani T., Fahiminiya S., Fujikawa A., Kuboyama K.,
RA Takeuchi Y., Nawaz Z., Nadaf J., Kamel H., Kitam A.K., Samiha Z.,
RA Mahmoud L., Ben-Omran T., Majewski J., Noda M.;
RT "Loss-of-function mutation in APC2 causes Sotos syndrome features.";
RL Cell Rep. 10:1585-1598(2015).
CC -!- FUNCTION: Stabilizes microtubules and may regulate actin fiber dynamics
CC through the activation of Rho family GTPases. May also function in Wnt
CC signaling by promoting the rapid degradation of CTNNB1.
CC {ECO:0000250|UniProtKB:O95996}.
CC -!- SUBUNIT: Interacts with APC, CTNNB1, TP53BP2 and possibly with AXIN2
CC (By similarity). Interacts with MAPRE3, PSRC1 and probably MAPRE1.
CC {ECO:0000250, ECO:0000269|PubMed:17310996}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:O95996}. Golgi apparatus
CC {ECO:0000250|UniProtKB:O95996}. Cytoplasm
CC {ECO:0000250|UniProtKB:O95996}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:O95996}. Note=Associated with actin filaments.
CC Associated with microtubule network. {ECO:0000250|UniProtKB:O95996}.
CC -!- TISSUE SPECIFICITY: Expressed in brain and other neural tissues.
CC {ECO:0000269|PubMed:15018807}.
CC -!- DEVELOPMENTAL STAGE: Strongly expressed in fetal brain but expression
CC decreases from P12 onward. Expressed in postmitotic neurons.
CC {ECO:0000269|PubMed:15018807}.
CC -!- DISRUPTION PHENOTYPE: Mice display abnormal head shape with shortened
CC skull length and no change in the skull height. Brain ventricles of
CC these mice are significantly larger and the thickness of the corpus
CC callosum is significantly reduced. They show increased exploratory
CC activity and have impaired learning memory function.
CC {ECO:0000269|PubMed:25753423}.
CC -!- SIMILARITY: Belongs to the adenomatous polyposis coli (APC) family.
CC {ECO:0000305}.
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DR EMBL; AJ130783; CAA10207.1; -; Genomic_DNA.
DR EMBL; AJ130784; CAA10207.1; JOINED; Genomic_DNA.
DR EMBL; AJ130785; CAA10207.1; JOINED; Genomic_DNA.
DR EMBL; AJ130786; CAA10207.1; JOINED; Genomic_DNA.
DR EMBL; AJ130787; CAA10207.1; JOINED; Genomic_DNA.
DR EMBL; AJ130788; CAA10207.1; JOINED; Genomic_DNA.
DR EMBL; AJ130789; CAA10207.1; JOINED; Genomic_DNA.
DR EMBL; AJ130790; CAA10207.1; JOINED; Genomic_DNA.
DR EMBL; AJ130791; CAA10207.1; JOINED; Genomic_DNA.
DR EMBL; AJ130792; CAA10207.1; JOINED; Genomic_DNA.
DR EMBL; AJ130793; CAA10207.1; JOINED; Genomic_DNA.
DR EMBL; AJ130794; CAA10207.1; JOINED; Genomic_DNA.
DR EMBL; AJ130795; CAA10207.1; JOINED; Genomic_DNA.
DR EMBL; AJ130796; CAA10207.1; JOINED; Genomic_DNA.
DR CCDS; CCDS24016.1; -.
DR PIR; T30258; T30258.
DR AlphaFoldDB; Q9Z1K7; -.
DR SMR; Q9Z1K7; -.
DR ComplexPortal; CPX-448; Beta-catenin destruction core complex, variant 2.
DR ComplexPortal; CPX-452; Beta-catenin destruction core complex, variant 4.
DR ComplexPortal; CPX-456; Beta-catenin destruction core complex, variant 6.
DR ComplexPortal; CPX-458; Beta-catenin destruction core complex, variant 8.
DR IntAct; Q9Z1K7; 1.
DR STRING; 10090.ENSMUSP00000100996; -.
DR iPTMnet; Q9Z1K7; -.
DR PhosphoSitePlus; Q9Z1K7; -.
DR MaxQB; Q9Z1K7; -.
DR PaxDb; Q9Z1K7; -.
DR PRIDE; Q9Z1K7; -.
DR ProteomicsDB; 296370; -.
DR MGI; MGI:1346052; Apc2.
DR eggNOG; KOG2122; Eukaryota.
DR InParanoid; Q9Z1K7; -.
DR PhylomeDB; Q9Z1K7; -.
DR ChiTaRS; Apc2; mouse.
DR PRO; PR:Q9Z1K7; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9Z1K7; protein.
DR GO; GO:0005884; C:actin filament; ISO:MGI.
DR GO; GO:0030877; C:beta-catenin destruction complex; IBA:GO_Central.
DR GO; GO:0016342; C:catenin complex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005881; C:cytoplasmic microtubule; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0031941; C:filamentous actin; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR GO; GO:0031258; C:lamellipodium membrane; ISO:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0030496; C:midbody; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0098794; C:postsynapse; ISO:MGI.
DR GO; GO:0008013; F:beta-catenin binding; ISO:MGI.
DR GO; GO:0045295; F:gamma-catenin binding; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0090630; P:activation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0001708; P:cell fate specification; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IBA:GO_Central.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0007389; P:pattern specification process; IBA:GO_Central.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IC:ComplexPortal.
DR GO; GO:0045595; P:regulation of cell differentiation; IBA:GO_Central.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR026837; APC2.
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; IPR009224; SAMP.
DR PANTHER; PTHR12607; PTHR12607; 1.
DR PANTHER; PTHR12607:SF3; PTHR12607:SF3; 1.
DR Pfam; PF05956; APC_basic; 1.
DR Pfam; PF16689; APC_N_CC; 1.
DR Pfam; PF05923; APC_r; 3.
DR Pfam; PF18797; APC_rep; 1.
DR Pfam; PF00514; Arm; 1.
DR Pfam; PF05924; SAMP; 1.
DR SMART; SM00185; ARM; 7.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF58050; SSF58050; 1.
DR SUPFAM; SSF82931; SSF82931; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Golgi apparatus; Microtubule;
KW Phosphoprotein; Reference proteome; Repeat; Wnt signaling pathway.
FT CHAIN 1..2274
FT /note="Adenomatous polyposis coli protein 2"
FT /id="PRO_0000313687"
FT REPEAT 301..341
FT /note="ARM 1"
FT REPEAT 472..511
FT /note="ARM 2"
FT REPEAT 515..555
FT /note="ARM 3"
FT REPEAT 557..602
FT /note="ARM 4"
FT REPEAT 608..647
FT /note="ARM 5"
FT REPEAT 650..689
FT /note="ARM 6"
FT REPEAT 1049..1068
FT /note="1"
FT REPEAT 1140..1159
FT /note="2"
FT REPEAT 1250..1269
FT /note="3"
FT REPEAT 1375..1394
FT /note="4"
FT REPEAT 1546..1565
FT /note="5"
FT REGION 97..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 859..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1049..1565
FT /note="5 X 20 AA approximate repeat of F-X-V-E-X-T-P-X-C-F-
FT S-R-X-S-S-L-S-S-L-S"
FT REGION 1049..1565
FT /note="Interaction with CTNNB1"
FT /evidence="ECO:0000250"
FT REGION 1061..1143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1165..1216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1290..1323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1368..1480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1493..1631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1699..2003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1792..1871
FT /note="Required for localization to microtubules and
FT function in microtubule stabilization"
FT /evidence="ECO:0000250|UniProtKB:O95996"
FT REGION 2022..2122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2037..2114
FT /note="Interaction with MAPRE1 and MAPRE3"
FT /evidence="ECO:0000250"
FT REGION 2135..2274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 5..59
FT /evidence="ECO:0000255"
FT COILED 832..856
FT /evidence="ECO:0000255"
FT COMPBIAS 1061..1084
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1165..1197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1376..1396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1455..1480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1513..1527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1553..1569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1768..1811
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1838..1861
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1949..1963
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2076..2097
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2146..2183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1563
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1565
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1861
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 2274 AA; 243139 MW; 75ABDA15D0F707F5 CRC64;
MTSSMASYEQ LVRQVEALKA ENTHLRQELR DNSSHLSKLE TETSGMKEVL KHLQGKLEQE
ARVLVSSGQT EVLEQLKALQ TDISSLYNLK FHAPALGPEP AARTPEGSPV HGSGPSKDSF
GELSRATIRL LEELDQERCF LLSEIEKEEK EKLWYYSQLQ GLSKRLDELP HVDTFSMQMD
LIRQQLEFEA QHIRSLMEER FGTSDEMVQR AQIRASRLEQ IDKELLEAQD RVQQTEPQAL
LAVKPVAVEE EQEAEVPTHP EDGTPQPGNS KVEVVFWLLS MLATRDQEDT ARTLLAMSSS
PESCVAMRRS GCLPLLLQIL HGTEAGSVGR AGIPGAPGAK DARMRANAAL HNIVFSQPDQ
GLARKEMRVL HVLEQIRAYC ETCWDWLQAR DSGTETPVPI EPQICQATCA VMKLSFDEEY
RRAMNELGGL QAVAELLQVD YEMHKMTRDP LNLALRRYAG MTLTNLTFGD VANKATLCAR
RGCMEAIVAQ LGSESEELHQ VVSSILRNLS WRADINSKKV LREVGSMTAL MECVLRASKE
STLKSVLSAL WNLSAHSTEN KAAICQVDGA LGFLVSTLTY RCQGNSLAVI ESGGGILRNV
SSLIATREDY RQVLRDHNCL QTLLQHLTSH SLTIVSNACG TLWNLSARSP RDQELLWDLG
AVGMLRNLVH SKHKMIAMGS AAALRNLLAH RPAKYQAAAM AVSPGTCVPS LYVRKQRALE
AELDTRHLVH ALGHLEKQSL PEAETTSKKP LPPLRHLDGL VQDYASDSGC FDDDDAPSLA
AAATTAEPAS PAVMSMFLGG PFLQGQALAR TPPARQGGLE AEKEAGGEAA VAAKAKAKLA
LAVARIDRLV EDISALHTSS DDSFSLSSGD PGQEAPREGR AQSCSPCRGT EGGRREAGSR
AHPLLRLKAA HTSLSNDSLN SGSTSDGYCT REHMTPCPLA ALAEHRDDPV RGQTRPRRLD
LDLPSRAELP ARDTAATDAR VRTIKLSPTY QHVPLLDGAA GAGVRPLVGP GTSPGARKQA
WIPADSLSKV PEKLVASPLP IASKVLQKLV AQDGPMSLSR CSSLSSLSST GHAVPSQAEN
LDSDSSLEGL EEAGPGEAEL GRAWRASGST SLPVSIPAPQ RGRSRGLGVE DATPSSSSEN
CVQETPLVLS RCSSVSSLGS FESRSIASSI PSDPCSGLGS GTVSPSELPD SPGQTMPPSR
SKTPPAPPGQ PETSQFSLQW ESYVKRFLDI ADCRERCQPP SELDAGSVRF TVEKPDENFS
CASSLSALAL HELYVQQDVE LRLRPPACPE RAVGGGGHRR RDEAASRLDG PAPAGSRARS
ATDKELEALR ECLGAAMPAR LRKVASALVP GRRSLPVPVY MLVPAPARGD DSGTDSAEGT
PVNFSSAASL SDETLQGPSR DKPAGPGDRQ KPTGRAAPAR QTRSHRPKAA GAGKSTEHTR
GPCRNRAGLE LPLSRPQSAR SNRDSSCQTR TRGDGALQSL CLTTPTEEAV YCFYDSDEEP
PATAPPPRRA SAIPRALKRE KPAGRKETPS RAAQPATLPV RAQPRLIVDE TPPCYSLTSS
ASSLSEPEAP EQPANHARGP EQGSKQDSSP SPRAEEELLQ RCISLAMPRR RTQVPGSRRR
KPRALRSDIR PTEITQKCQE EVAGSDPASD LDSVEWQAIQ EGANSIVTWL HQAAAKASLE
ASSESDSLLS LVSGVSAGST LQPSKLRKGR KPAAEAGGAW RPEKRGTTST KINGSPRLPN
GPEKAKGTQK MMAGESTMLR GRTVIYSAGP ASRTQSKGIS GPCTTPKKTG TSGTTQPETV
TKAPSPEQQR SRSLHRPGKI SELAALRHPP RSATPPARLA KTPSSSSSQT SPASQPLPRR
SPLATPTGGP LPGPGGSLVP KSPARALLAK QHKTQKSPVR IPFMQRPARR VPPPLARPSP
EPGSRGRAGA EGTPGARGSR LGLVRMASAR SSGSESSDRS GFRRQLTFIK ESPGLLRRRR
SELSSADSTA STSQAASPRR GRPALPAVFL CSSRCDELRV SPRQPLAAQR SPQAKPGLAP
LAPRRTSSES PSRLPVRASP GRPETVKRYA SLPHISVSRR SDSAVSVPTT QANATRRGSD
GEARPLPRVA PPGTTWRRIK DEDVPHILRS TLPATALPLR VSSPEDSPAG TPQRKTSDAV
VQTEDVATSK TNSSTSPSLE SRDPPQAPAS GPVAPQGSDV DGPVLTKPPA SAPFPHEGLS
AVIAGFPTSR HGSPSRAARV PPFNYVPSPM AAATMASDSA VEKAPVSSPA SLLE
