ANKR6_MOUSE
ID ANKR6_MOUSE Reviewed; 712 AA.
AC Q69ZU8; A2ANZ0; Q6P1A8; Q8VHD9;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Ankyrin repeat domain-containing protein 6;
DE AltName: Full=Diversin;
GN Name=Ankrd6; Synonyms=Kiaa0957;
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 [MRNA] (ISOFORM 1), FUNCTION, AND INTERACTION WITH
RP AXN1; AXN2 AND CSNK1E.
RX PubMed=12183362; DOI=10.1101/gad.230402;
RA Schwarz-Romond T., Asbrand C., Bakkers J., Kuehl M., Schaeffer H.J.,
RA Huelsken J., Behrens J., Hammerschmidt M., Birchmeier W.;
RT "The ankyrin repeat protein diversin recruits casein kinase Iepsilon to the
RT beta-catenin degradation complex and acts in both canonical Wnt and Wnt/JNK
RT signaling.";
RL Genes Dev. 16:2073-2084(2002).
RN [2]
RP SEQUENCE REVISION TO 264-271.
RA Schwarz-Romond T., Behrens J., Birchmeier W.;
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Recruits CKI-epsilon to the beta-catenin degradation complex
CC that consists of AXN1 or AXN2 and GSK3-beta and allows efficient
CC phosphorylation of beta-catenin, thereby inhibiting beta-catenin/Tcf
CC signals. {ECO:0000269|PubMed:12183362}.
CC -!- SUBUNIT: Interacts with AXN1, AXN2 and CSNK1E/CKI-epsilon.
CC {ECO:0000269|PubMed:12183362}.
CC -!- INTERACTION:
CC Q69ZU8-1; Q60838: Dvl2; NbExp=3; IntAct=EBI-15605686, EBI-641940;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q69ZU8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q69ZU8-2; Sequence=VSP_031592;
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DR EMBL; AY026320; AAK15806.2; -; mRNA.
DR EMBL; AK173070; BAD32348.1; -; mRNA.
DR EMBL; AL831774; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466538; EDL05499.1; -; Genomic_DNA.
DR EMBL; BC065177; AAH65177.1; -; mRNA.
DR CCDS; CCDS18018.1; -. [Q69ZU8-1]
DR RefSeq; NP_001012453.1; NM_001012450.1. [Q69ZU8-1]
DR RefSeq; NP_001012454.1; NM_001012451.1. [Q69ZU8-1]
DR RefSeq; NP_536719.2; NM_080471.3. [Q69ZU8-1]
DR RefSeq; XP_006537671.1; XM_006537608.3.
DR RefSeq; XP_011248221.1; XM_011249919.2. [Q69ZU8-1]
DR RefSeq; XP_011248222.1; XM_011249920.2. [Q69ZU8-1]
DR RefSeq; XP_011248223.1; XM_011249921.2. [Q69ZU8-1]
DR RefSeq; XP_011248224.1; XM_011249922.2. [Q69ZU8-1]
DR RefSeq; XP_011248225.1; XM_011249923.2. [Q69ZU8-1]
DR RefSeq; XP_011248226.1; XM_011249924.2. [Q69ZU8-1]
DR AlphaFoldDB; Q69ZU8; -.
DR SMR; Q69ZU8; -.
DR BioGRID; 228286; 2.
DR DIP; DIP-61292N; -.
DR IntAct; Q69ZU8; 4.
DR STRING; 10090.ENSMUSP00000041300; -.
DR iPTMnet; Q69ZU8; -.
DR PhosphoSitePlus; Q69ZU8; -.
DR PaxDb; Q69ZU8; -.
DR PRIDE; Q69ZU8; -.
DR ProteomicsDB; 296303; -. [Q69ZU8-1]
DR ProteomicsDB; 296304; -. [Q69ZU8-2]
DR Antibodypedia; 54806; 105 antibodies from 19 providers.
DR DNASU; 140577; -.
DR Ensembl; ENSMUST00000035719; ENSMUSP00000041300; ENSMUSG00000040183. [Q69ZU8-1]
DR Ensembl; ENSMUST00000084748; ENSMUSP00000081800; ENSMUSG00000040183. [Q69ZU8-2]
DR Ensembl; ENSMUST00000084749; ENSMUSP00000081801; ENSMUSG00000040183. [Q69ZU8-1]
DR Ensembl; ENSMUST00000084750; ENSMUSP00000081802; ENSMUSG00000040183. [Q69ZU8-1]
DR GeneID; 140577; -.
DR KEGG; mmu:140577; -.
DR UCSC; uc008sff.1; mouse. [Q69ZU8-1]
DR CTD; 22881; -.
DR MGI; MGI:2154278; Ankrd6.
DR VEuPathDB; HostDB:ENSMUSG00000040183; -.
DR eggNOG; KOG0504; Eukaryota.
DR GeneTree; ENSGT00940000155887; -.
DR HOGENOM; CLU_027072_0_0_1; -.
DR InParanoid; Q69ZU8; -.
DR OMA; MKTEIHA; -.
DR OrthoDB; 1008734at2759; -.
DR PhylomeDB; Q69ZU8; -.
DR TreeFam; TF332587; -.
DR BioGRID-ORCS; 140577; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Ankrd6; mouse.
DR PRO; PR:Q69ZU8; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q69ZU8; protein.
DR Bgee; ENSMUSG00000040183; Expressed in facial nucleus and 233 other tissues.
DR ExpressionAtlas; Q69ZU8; baseline and differential.
DR Genevisible; Q69ZU8; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:MGI.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IBA:GO_Central.
DR GO; GO:2000096; P:positive regulation of Wnt signaling pathway, planar cell polarity pathway; IDA:MGI.
DR Gene3D; 1.25.40.20; -; 3.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF13857; Ank_5; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 8.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 6.
PE 1: Evidence at protein level;
KW Alternative splicing; ANK repeat; Coiled coil; Reference proteome; Repeat.
FT CHAIN 1..712
FT /note="Ankyrin repeat domain-containing protein 6"
FT /id="PRO_0000320066"
FT REPEAT 9..38
FT /note="ANK 1"
FT REPEAT 41..70
FT /note="ANK 2"
FT REPEAT 74..103
FT /note="ANK 3"
FT REPEAT 107..136
FT /note="ANK 4"
FT REPEAT 140..169
FT /note="ANK 5"
FT REPEAT 173..202
FT /note="ANK 6"
FT REPEAT 206..235
FT /note="ANK 7"
FT REPEAT 239..268
FT /note="ANK 8"
FT REGION 277..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 416..445
FT /evidence="ECO:0000255"
FT COILED 669..712
FT /evidence="ECO:0000255"
FT COMPBIAS 277..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..344
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..379
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 265..299
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_031592"
SQ SEQUENCE 712 AA; 77982 MW; 88616A71DD632AD0 CRC64;
MSQQDAVAAL SERLLIAAYK GQTENVVQLI NKGAKVAVTK HGRTPLHLAA NKGHLSVVQI
LLKAGCDLDV QDDGDQTALH RATVVGNTEI LTALIREGCA LDRQDKDGNT ALHEAAWHGF
SQSAKLLVKA GANVLARNKA GNTALHLACQ NSHSQSTRIL LLGGSRADLK NNAGDTCLHV
AARYNHLSVV RLLLNAFCSV HEKNQAGDTA LHVAAALNHK KVVKVLLEAG ADTTIVNNAG
QTPLETARYH NNPEVALLLT KAPQILRFSR GRSLRKRRER LKEERRAQSV PRDEVAQSKG
SVSAGDTPSS EQAVPQKEEA RRDCPPASQE PRKDERRRKS RPEVSALSDP TPAADQQPGH
QKNLHSHHHP KKKSRHRCWS PPPPHGFRAY QLYTLYRGED GKVMQAPIKG CRCEPLINKL
ENQLEATVEE IRAELGSVQD KVNAKLGQME SKTQHQMCVL DKLMVERLSA ERTECMNRLQ
QHAAAEKQEG EKRQMSLVDE LKAWCMLKIQ SLELRLSGES RTFRAKSTPP PSDSTPAVDQ
PVVAAGPGAA SDSSSQVVRP KDKALNASAA HSHQQELPPS DCTGSGLRKI KAPGASRCDQ
QTGSCVNRGT QTKKSGRSGQ TKHRGQQPTA SSPSGQQPSA ASSDVRDASQ ALELTQYFFE
AVSAQMEKWY ERKIEEARSQ ASQKAQQDEA TLKEHIRSLE EELARLRTKV QK
