DIXC1_MOUSE
ID DIXC1_MOUSE Reviewed; 711 AA.
AC Q80Y83; Q3TPF4; Q3UQ90; Q5DPZ2; Q5DPZ3; Q5DPZ4; Q5DPZ6; Q6ZPJ2; Q8C467;
AC Q8R1C1;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Dixin;
DE AltName: Full=Coiled-coil protein DIX1;
DE Short=Coiled-coil-DIX1;
DE AltName: Full=DIX domain-containing protein 1;
GN Name=Dixdc1; Synonyms=Ccd1, Kiaa1735;
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] (ISOFORMS 1; 3; 9; 11 AND 13), ALTERNATIVE
RP SPLICING (ISOFORMS 2; 4; 5; 6; 7; 8; 10; 12 AND 14), FUNCTION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15857680; DOI=10.1016/j.molbrainres.2004.12.002;
RA Shiomi K., Kanemoto M., Keino-Masu K., Yoshida S., Soma K., Masu M.;
RT "Identification and differential expression of multiple isoforms of mouse
RT coiled-coil-DIX1 (Ccd1), a positive regulator of Wnt signaling.";
RL Brain Res. Mol. Brain Res. 135:169-180(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 15), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-316 (ISOFORM 5), AND NUCLEOTIDE SEQUENCE [LARGE
RP SCALE MRNA] OF 612-711 (ISOFORMS 1/2/3/4/5).
RC STRAIN=C57BL/6J;
RC TISSUE=Embryonic eye, Embryonic spinal cord, and Mammary gland;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 16).
RC STRAIN=C57BL/6J; TISSUE=Embryonic brain, and Eye;
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 228-711 (ISOFORMS 1/2).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
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. 10:167-180(2003).
RN [5]
RP FUNCTION, AND INTERACTION WITH AXIN1; DVL2; MAP3K4 AND RAC.
RX PubMed=15262978; DOI=10.1074/jbc.m404598200;
RA Wong C.K., Luo W., Deng Y., Zou H., Ye Z., Lin S.-C.;
RT "The DIX domain protein coiled-coil-DIX1 inhibits c-Jun N-terminal kinase
RT activation by Axin and dishevelled through distinct mechanisms.";
RL J. Biol. Chem. 279:39366-39373(2004).
RN [6]
RP DEVELOPMENTAL STAGE.
RX PubMed=16378754; DOI=10.1016/j.modgep.2005.06.013;
RA Soma K., Shiomi K., Keino-Masu K., Masu M.;
RT "Expression of mouse Coiled-coil-DIX1 (Ccd1), a positive regulator of Wnt
RT signaling, during embryonic development.";
RL Gene Expr. Patterns 6:325-330(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212 AND SER-257,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 (ISOFORMS 11 AND 12), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Kidney;
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).
CC -!- FUNCTION: Positive effector of the Wnt signaling pathway; activates
CC WNT3A signaling via DVL2. Regulates JNK activation by AXIN1 and DVL2.
CC {ECO:0000269|PubMed:15262978, ECO:0000269|PubMed:15857680}.
CC -!- SUBUNIT: May bind filamentous actin. Directly interacts (via DIX
CC domain) with DVL2 (via DIX domain). Interacts with gamma-tubulin (By
CC similarity). Interacts with the complex composed of DVL2 and Rac.
CC Interacts with AXIN1; competes with MAP3K1. Interacts with MAP3K4
CC preventing MAP3K4 interaction with AXIN1.
CC {ECO:0000250|UniProtKB:Q155Q3, ECO:0000269|PubMed:15262978}.
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC {ECO:0000250|UniProtKB:Q155Q3}. Cytoplasm, cytoskeleton, stress fiber
CC {ECO:0000250|UniProtKB:Q155Q3}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q155Q3}. Note=Colocalizes with gamma-tubulin at
CC the centrosome, both during interphase and mitosis. Associated with
CC actin stress fiber at the filament ends.
CC {ECO:0000250|UniProtKB:Q155Q3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=16;
CC Name=1; Synonyms=Abeta1L;
CC IsoId=Q80Y83-1; Sequence=Displayed;
CC Name=2; Synonyms=Abeta1S;
CC IsoId=Q80Y83-2; Sequence=VSP_025394;
CC Name=3; Synonyms=Aalpha1L;
CC IsoId=Q80Y83-3; Sequence=VSP_025387;
CC Name=4; Synonyms=Aalpha1S;
CC IsoId=Q80Y83-4; Sequence=VSP_025387, VSP_025394;
CC Name=5; Synonyms=Abeta2L;
CC IsoId=Q80Y83-5; Sequence=VSP_025388;
CC Name=6; Synonyms=Abeta2S;
CC IsoId=Q80Y83-6; Sequence=VSP_025388, VSP_025394;
CC Name=7; Synonyms=Aalpha2L;
CC IsoId=Q80Y83-7; Sequence=VSP_025387, VSP_025388;
CC Name=8; Synonyms=Aalpha2S;
CC IsoId=Q80Y83-8; Sequence=VSP_025387, VSP_025388, VSP_025394;
CC Name=9; Synonyms=BbetaL;
CC IsoId=Q80Y83-9; Sequence=VSP_025386, VSP_025391;
CC Name=10; Synonyms=BbetaS;
CC IsoId=Q80Y83-10; Sequence=VSP_025386, VSP_025391, VSP_025394;
CC Name=11; Synonyms=BalphaL;
CC IsoId=Q80Y83-11; Sequence=VSP_025385, VSP_025392;
CC Name=12; Synonyms=BalphaS;
CC IsoId=Q80Y83-12; Sequence=VSP_025385, VSP_025392, VSP_025394;
CC Name=13; Synonyms=CL;
CC IsoId=Q80Y83-13; Sequence=VSP_025383;
CC Name=14; Synonyms=CS;
CC IsoId=Q80Y83-14; Sequence=VSP_025383, VSP_025394;
CC Name=15;
CC IsoId=Q80Y83-15; Sequence=VSP_025384, VSP_025393, VSP_025395,
CC VSP_025396;
CC Name=16;
CC IsoId=Q80Y83-16; Sequence=VSP_025387, VSP_025389, VSP_025390;
CC -!- TISSUE SPECIFICITY: Abundantly expressed in brain and testis and to a
CC lower extent in lung, kidney, colon, ovary and urinary bladder.
CC Expressed in brain, liver, testis and spleen (at protein level).
CC Expressed throughout the brain with strong expression in main and
CC accessory olfactory bulbs, cerebral cortex, piriform cortex,
CC hippocampus, habenular nucleus, dorsal thalamus, superior and inferior
CC colliculi and cerebellum. {ECO:0000269|PubMed:15857680}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryonic brain, liver and spleen (at
CC protein level). First detected at 7.5 dpc in the node. Expressed in the
CC cephalic mesenchyme and tail bud at 8.5 dpc, and in the branchial arch
CC and forelimb bud at 9.5 dpc. In the central nervous system, expression
CC begins and persists in the regions where the neurons differentiate.
CC Expression is also strong in the peripheral nervous system, including
CC sensory cranial ganglia, dorsal root ganglia, and autonomic ganglia,
CC and in the sensory organs, such as the inner nuclear layer of the
CC neural retina, saccule and cochlea of the inner ear, and nasal
CC epithelium. Outside the nervous system, expression is detected in the
CC cartilage, tongue, lung bud, stomach, and gonad from 12.5 dpc to 14.5
CC dpc, and in the tooth bud, bronchial epithelium, and kidney at 17.5
CC dpc. {ECO:0000269|PubMed:15857680, ECO:0000269|PubMed:16378754}.
CC -!- DOMAIN: The coiled-coil domain mediates interaction with MAP3K4 and
CC inhibition of AXIN1-mediated JNK activation through MAP3K4.
CC {ECO:0000250|UniProtKB:Q155Q3}.
CC -!- DOMAIN: The DIX domain mediates interaction with AXIN1 and inhibition
CC of AXIN1-mediated JNK activation through MAP3K1. Mediates interaction
CC with DVL2; this interaction is required for activation of Wnt signaling
CC (By similarity). {ECO:0000250|UniProtKB:Q155Q3}.
CC -!- PTM: Phosphorylated on tyrosine and serine residues.
CC {ECO:0000250|UniProtKB:Q155Q3}.
CC -!- PTM: Polyubiquitinated, leading to its proteasomal degradation. WNT3A
CC signaling increases DIXDC1 protein levels by inhibiting its
CC ubiquitination and subsequent degradation.
CC {ECO:0000250|UniProtKB:Q155Q3}.
CC -!- MISCELLANEOUS: [Isoform 5]: Major isoform. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 7]: Major isoform. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 11]: Major isoform. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DIXDC1 family. {ECO:0000305}.
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DR EMBL; AY549883; AAT41660.1; -; mRNA.
DR EMBL; AY549884; AAT41661.1; -; mRNA.
DR EMBL; AY549885; AAT41662.1; -; mRNA.
DR EMBL; AY549886; AAT41663.1; -; mRNA.
DR EMBL; AY549887; AAT41664.1; -; mRNA.
DR EMBL; AK082960; BAC38711.1; -; mRNA.
DR EMBL; AK142668; BAE25153.1; -; mRNA.
DR EMBL; AK164424; BAE37782.1; -; mRNA.
DR EMBL; BC024834; AAH24834.1; -; mRNA.
DR EMBL; BC048182; AAH48182.1; -; mRNA.
DR EMBL; BC063085; AAH63085.1; -; mRNA.
DR EMBL; AK129432; BAC98242.1; -; mRNA.
DR CCDS; CCDS23169.1; -. [Q80Y83-1]
DR CCDS; CCDS80995.1; -. [Q80Y83-3]
DR CCDS; CCDS90563.1; -. [Q80Y83-5]
DR RefSeq; NP_001297998.1; NM_001311069.1. [Q80Y83-3]
DR RefSeq; NP_835219.1; NM_178118.2. [Q80Y83-1]
DR RefSeq; XP_006510517.1; XM_006510454.3.
DR RefSeq; XP_006510518.1; XM_006510455.3. [Q80Y83-2]
DR RefSeq; XP_006510519.1; XM_006510456.3. [Q80Y83-11]
DR RefSeq; XP_006510520.1; XM_006510457.3. [Q80Y83-13]
DR RefSeq; XP_017168928.1; XM_017313439.1. [Q80Y83-3]
DR RefSeq; XP_017168929.1; XM_017313440.1. [Q80Y83-3]
DR RefSeq; XP_017168930.1; XM_017313441.1. [Q80Y83-12]
DR PDB; 5Y3B; X-ray; 3.00 A; A/B/C/D/E/F/G=625-707.
DR PDBsum; 5Y3B; -.
DR AlphaFoldDB; Q80Y83; -.
DR SMR; Q80Y83; -.
DR BioGRID; 237048; 2.
DR CORUM; Q80Y83; -.
DR IntAct; Q80Y83; 1.
DR STRING; 10090.ENSMUSP00000034566; -.
DR iPTMnet; Q80Y83; -.
DR PhosphoSitePlus; Q80Y83; -.
DR MaxQB; Q80Y83; -.
DR PaxDb; Q80Y83; -.
DR PeptideAtlas; Q80Y83; -.
DR PRIDE; Q80Y83; -.
DR ProteomicsDB; 279697; -. [Q80Y83-1]
DR ProteomicsDB; 279698; -. [Q80Y83-2]
DR ProteomicsDB; 279699; -. [Q80Y83-3]
DR ProteomicsDB; 279700; -. [Q80Y83-4]
DR ProteomicsDB; 279701; -. [Q80Y83-5]
DR ProteomicsDB; 279702; -. [Q80Y83-6]
DR ProteomicsDB; 279703; -. [Q80Y83-7]
DR ProteomicsDB; 279704; -. [Q80Y83-8]
DR ProteomicsDB; 279705; -. [Q80Y83-9]
DR ProteomicsDB; 279706; -. [Q80Y83-10]
DR ProteomicsDB; 279707; -. [Q80Y83-11]
DR ProteomicsDB; 279708; -. [Q80Y83-12]
DR ProteomicsDB; 279709; -. [Q80Y83-13]
DR ProteomicsDB; 279710; -. [Q80Y83-14]
DR ProteomicsDB; 279711; -. [Q80Y83-15]
DR Antibodypedia; 32094; 212 antibodies from 31 providers.
DR DNASU; 330938; -.
DR Ensembl; ENSMUST00000034566; ENSMUSP00000034566; ENSMUSG00000032064. [Q80Y83-1]
DR Ensembl; ENSMUST00000117093; ENSMUSP00000112654; ENSMUSG00000032064. [Q80Y83-16]
DR Ensembl; ENSMUST00000117646; ENSMUSP00000112431; ENSMUSG00000032064. [Q80Y83-5]
DR Ensembl; ENSMUST00000120622; ENSMUSP00000113934; ENSMUSG00000032064. [Q80Y83-15]
DR Ensembl; ENSMUST00000121634; ENSMUSP00000113089; ENSMUSG00000032064. [Q80Y83-3]
DR GeneID; 330938; -.
DR KEGG; mmu:330938; -.
DR UCSC; uc009pkb.1; mouse. [Q80Y83-11]
DR UCSC; uc009pkc.2; mouse. [Q80Y83-1]
DR UCSC; uc009pkd.1; mouse. [Q80Y83-3]
DR UCSC; uc009pke.1; mouse. [Q80Y83-15]
DR UCSC; uc009pkh.1; mouse. [Q80Y83-16]
DR CTD; 85458; -.
DR MGI; MGI:2679721; Dixdc1.
DR VEuPathDB; HostDB:ENSMUSG00000032064; -.
DR eggNOG; ENOG502RD5G; Eukaryota.
DR GeneTree; ENSGT00950000182903; -.
DR HOGENOM; CLU_025678_0_0_1; -.
DR InParanoid; Q80Y83; -.
DR OMA; AHFKPTA; -.
DR OrthoDB; 949210at2759; -.
DR PhylomeDB; Q80Y83; -.
DR TreeFam; TF318198; -.
DR BioGRID-ORCS; 330938; 0 hits in 57 CRISPR screens.
DR PRO; PR:Q80Y83; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q80Y83; protein.
DR Bgee; ENSMUSG00000032064; Expressed in cerebellum lobe and 267 other tissues.
DR ExpressionAtlas; Q80Y83; baseline and differential.
DR Genevisible; Q80Y83; MM.
DR GO; GO:0043679; C:axon terminus; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0043015; F:gamma-tubulin binding; ISS:UniProtKB.
DR GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; IPI:MGI.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IMP:DFLAT.
DR GO; GO:0021846; P:cell proliferation in forebrain; IMP:DFLAT.
DR GO; GO:0021695; P:cerebellar cortex development; ISO:MGI.
DR GO; GO:0021795; P:cerebral cortex cell migration; IMP:DFLAT.
DR GO; GO:0021799; P:cerebral cortex radially oriented cell migration; IMP:DFLAT.
DR GO; GO:0021869; P:forebrain ventricular zone progenitor cell division; IMP:DFLAT.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IMP:DFLAT.
DR GO; GO:0050772; P:positive regulation of axonogenesis; ISO:MGI.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISO:MGI.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IMP:DFLAT.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:DFLAT.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IMP:DFLAT.
DR CDD; cd00014; CH; 1.
DR Gene3D; 1.10.418.10; -; 1.
DR Gene3D; 2.40.240.130; -; 1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR001158; DIX.
DR InterPro; IPR038207; DIX_dom_sf.
DR InterPro; IPR029800; Dixin.
DR InterPro; IPR015506; Dsh/Dvl-rel.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10878; PTHR10878; 1.
DR PANTHER; PTHR10878:SF22; PTHR10878:SF22; 1.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF00778; DIX; 1.
DR SMART; SM00033; CH; 1.
DR SMART; SM00021; DAX; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS50841; DIX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Alternative splicing; Cell junction;
KW Coiled coil; Cytoplasm; Cytoskeleton; Developmental protein;
KW Phosphoprotein; Reference proteome; Ubl conjugation; Wnt signaling pathway.
FT CHAIN 1..711
FT /note="Dixin"
FT /id="PRO_0000287224"
FT DOMAIN 20..153
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 600..680
FT /note="DIX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00069"
FT REGION 153..326
FT /note="Actin-binding"
FT /evidence="ECO:0000250|UniProtKB:Q155Q3"
FT REGION 233..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 279..452
FT /evidence="ECO:0000255"
FT COMPBIAS 595..623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 618
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q155Q3"
FT VAR_SEQ 1..320
FT /note="Missing (in isoform 13 and isoform 14)"
FT /evidence="ECO:0000303|PubMed:15857680"
FT /id="VSP_025383"
FT VAR_SEQ 1..272
FT /note="Missing (in isoform 15)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025384"
FT VAR_SEQ 1..237
FT /note="Missing (in isoform 11 and isoform 12)"
FT /evidence="ECO:0000303|PubMed:15857680"
FT /id="VSP_025385"
FT VAR_SEQ 1..234
FT /note="Missing (in isoform 9 and isoform 10)"
FT /evidence="ECO:0000303|PubMed:15857680"
FT /id="VSP_025386"
FT VAR_SEQ 1..20
FT /note="MLACLTRGNLLDVLQEGFNE -> MGTQVVMRVCNSSMPGAPS (in
FT isoform 3, isoform 4, isoform 7, isoform 8 and isoform 16)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:15857680"
FT /id="VSP_025387"
FT VAR_SEQ 64..89
FT /note="Missing (in isoform 5, isoform 6, isoform 7 and
FT isoform 8)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025388"
FT VAR_SEQ 90..117
FT /note="AGEKLTGVQLSPSNQQEMKSNVERVLQF -> GCSFFRMHGNSVGKYLKVLA
FT LVNLRVGQ (in isoform 16)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025389"
FT VAR_SEQ 118..711
FT /note="Missing (in isoform 16)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025390"
FT VAR_SEQ 235..245
FT /note="QKSPSESSCSS -> MMIILQSKLIT (in isoform 9 and isoform
FT 10)"
FT /evidence="ECO:0000303|PubMed:15857680"
FT /id="VSP_025391"
FT VAR_SEQ 238..245
FT /note="PSESSCSS -> MGGTQVKC (in isoform 11 and isoform 12)"
FT /evidence="ECO:0000303|PubMed:15857680"
FT /id="VSP_025392"
FT VAR_SEQ 273..282
FT /note="IPSEGIENRT -> MNYGSTFHLA (in isoform 15)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025393"
FT VAR_SEQ 506..535
FT /note="Missing (in isoform 2, isoform 4, isoform 6, isoform
FT 8, isoform 10, isoform 12 and isoform 14)"
FT /evidence="ECO:0000305"
FT /id="VSP_025394"
FT VAR_SEQ 614..615
FT /note="TL -> KA (in isoform 15)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025395"
FT VAR_SEQ 616..711
FT /note="Missing (in isoform 15)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025396"
FT CONFLICT 278
FT /note="I -> T (in Ref. 4; BAC98242)"
FT /evidence="ECO:0000305"
FT CONFLICT 474
FT /note="L -> F (in Ref. 4; BAC98242)"
FT /evidence="ECO:0000305"
FT STRAND 628..635
FT /evidence="ECO:0007829|PDB:5Y3B"
FT STRAND 638..648
FT /evidence="ECO:0007829|PDB:5Y3B"
FT TURN 650..652
FT /evidence="ECO:0007829|PDB:5Y3B"
FT HELIX 655..662
FT /evidence="ECO:0007829|PDB:5Y3B"
FT STRAND 668..676
FT /evidence="ECO:0007829|PDB:5Y3B"
FT TURN 677..679
FT /evidence="ECO:0007829|PDB:5Y3B"
FT STRAND 680..685
FT /evidence="ECO:0007829|PDB:5Y3B"
FT STRAND 696..706
FT /evidence="ECO:0007829|PDB:5Y3B"
FT LIPID Q80Y83-4:2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
FT MOD_RES Q80Y83-11:13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q80Y83-12:13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 711 AA; 80215 MW; 153063F1B995EB8C CRC64;
MLACLTRGNL LDVLQEGFNE QQLQAYVAWV NAQLKKRPSV KPVQDLRQDL RDGVILAYLI
EIVGQLALDS DASVDERTDF FLLHSPFKAA GEKLTGVQLS PSNQQEMKSN VERVLQFVAS
KKIRMHQTSA KDIVEGNLKS IMRLVLALAA HFKPGSSRTV SQGRDSKAPV QSHQPHCATA
VAQGAAAALA DVCHDVSRSG RDVFRYRQRN ASVDGEIENP YWSVRALVQQ YEGQQKSPSE
SSCSSLTSPS PIHSAKSESI ITQAEEKADF VIIPSEGIEN RTDEPDSPSS RDWRPGSRGT
YLEATWEEQL LEQQEHLEKE MEEAKKMISG LQALLLNGSL PEDEQERPVA LCEPGVNPEE
QLIIIRSRLD QSVEENQDLK KELLKCKQEA RNLQGIKDAL QQRLTQQDTS VLQLKQELLR
ANMDKDELHN QNVDLQRKLE ERNRLLGEYK KELGQKDRLF QQQQAKLEEA LRKLSDASYQ
QVDLERELEQ KDVLLAHCMK GETDEVTNYN SHSSQRNGFV LPVAGRGATT VTHRGPQTSD
LQLVRDALRS LRNSFSGHDP QHHTIDSLEQ GISSLMERLH VVETQKKQER KVGGRSPRNQ
ASSEYRASWP PNSTLPHSQS SPAVSSTCTK VLYFTDRSLT PFMVNIPKRL GEVTLKDFKA
AIDREGNHRY HFKALDPEFG TVKEEVFHDD DAIPGWEGKI VAWVEEDHRE N
