DIXC1_HUMAN
ID DIXC1_HUMAN Reviewed; 683 AA.
AC Q155Q3; A1A5D8; E9PRV4; Q6P2J8; Q6PIK4; Q86SR7; Q8IVY4; Q96N69; Q9C0C8;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING (ISOFORMS 1
RP AND 2), TISSUE SPECIFICITY, SUBCELLULAR LOCATION (ISOFORMS 1 AND 2), AND
RP INTERACTION WITH ACTIN.
RX PubMed=16814745; DOI=10.1016/j.bbrc.2006.06.050;
RA Wang X., Zheng L., Zeng Z., Zhou G., Chien J., Qian C., Vasmatzis G.,
RA Shridhar V., Chen L., Liu W.;
RT "DIXDC1 isoform, l-DIXDC1, is a novel filamentous actin-binding protein.";
RL Biochem. Biophys. Res. Commun. 347:22-30(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-293 (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 3-218 (ISOFORM 4), AND NUCLEOTIDE SEQUENCE [LARGE
RP SCALE MRNA] OF 327-683 (ISOFORMS 1/2).
RC TISSUE=Brain, and Uterus;
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 257-683 (ISOFORMS 1/2).
RC TISSUE=Mammary gland;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH GAMMA TUBULIN.
RX PubMed=19375513; DOI=10.1016/j.cellbi.2009.04.001;
RA Wu Y., Jing X., Ma X., Wu Y., Ding X., Fan W., Fan M.;
RT "DIXDC1 co-localizes and interacts with gamma-tubulin in HEK293 cells.";
RL Cell Biol. Int. 33:697-701(2009).
RN [10]
RP PHOSPHORYLATION, SUBCELLULAR LOCATION, AND UBIQUITINATION.
RX PubMed=20085589; DOI=10.1111/j.1349-7006.2009.01448.x;
RA Wang L., Li H., Chen Q., Zhu T., Zhu H., Zheng L.;
RT "Wnt signaling stabilizes the DIXDC1 protein through decreased ubiquitin-
RT dependent degradation.";
RL Cancer Sci. 101:700-706(2010).
RN [11]
RP MYRISTOYLATION AT GLY-2 (ISOFORM 2).
RX PubMed=20213681; DOI=10.1002/pmic.200900783;
RA Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E.,
RA Tsunasawa S., Utsumi T.;
RT "Strategy for comprehensive identification of human N-myristoylated
RT proteins using an insect cell-free protein synthesis system.";
RL Proteomics 10:1780-1793(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-590, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 597-683, FUNCTION, MUTAGENESIS OF
RP ASP-648; PHE-651 AND LYS-655, DOMAIN, AND INTERACTION WITH DVL2.
RX PubMed=21189423; DOI=10.1074/jbc.m110.186742;
RA Liu Y.T., Dan Q.J., Wang J., Feng Y., Chen L., Liang J., Li Q., Lin S.C.,
RA Wang Z.X., Wu J.W.;
RT "Molecular basis of Wnt activation via the DIX-domain protein Ccd1.";
RL J. Biol. Chem. 286:8597-8608(2011).
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:21189423}.
CC -!- SUBUNIT: Isoform 1 but not isoform 2 binds filamentous actin. Interacts
CC with the complex composed of DVL2 and Rac. Interacts with AXIN1;
CC competes with MAP3K1. Interacts with MAP3K4 preventing MAP3K4
CC interaction with AXIN1. Directly interacts (via DIX domain) with DVL2
CC (via DIX domain). Interacts with gamma-tubulin.
CC {ECO:0000269|PubMed:15262978, ECO:0000269|PubMed:16814745,
CC ECO:0000269|PubMed:19375513, ECO:0000269|PubMed:21189423}.
CC -!- INTERACTION:
CC Q155Q3; O14641: DVL2; NbExp=2; IntAct=EBI-1104700, EBI-740850;
CC Q155Q3; Q60838: Dvl2; Xeno; NbExp=4; IntAct=EBI-1104700, EBI-641940;
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC {ECO:0000269|PubMed:16814745}. Cytoplasm, cytoskeleton, stress fiber
CC {ECO:0000269|PubMed:16814745}. Cytoplasm {ECO:0000269|PubMed:20085589}.
CC Note=Colocalizes with gamma-tubulin at the centrosome, both during
CC interphase and mitosis (PubMed:19375513). Associated with actin stress
CC fiber at the filament ends (PubMed:16814745).
CC {ECO:0000269|PubMed:16814745, ECO:0000269|PubMed:19375513}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:16814745}. Note=Not associated with stress fibers.
CC {ECO:0000269|PubMed:16814745}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=l-DIXDC1;
CC IsoId=Q155Q3-1; Sequence=Displayed;
CC Name=2; Synonyms=s-DIXDC1;
CC IsoId=Q155Q3-2; Sequence=VSP_025378, VSP_025379;
CC Name=3;
CC IsoId=Q155Q3-4; Sequence=VSP_025380, VSP_025381;
CC Name=4;
CC IsoId=Q155Q3-5; Sequence=VSP_054565, VSP_025380, VSP_025381;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with higher expression in
CC cardiac and skeletal muscles. {ECO:0000269|PubMed:16814745}.
CC -!- DOMAIN: The coiled-coil domain mediates interaction with MAP3K4 and
CC inhibition of AXIN1-mediated JNK activation through MAP3K4.
CC {ECO:0000269|PubMed:21189423}.
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
CC signaling. {ECO:0000269|PubMed:21189423}.
CC -!- PTM: Phosphorylated on tyrosine and serine residues.
CC {ECO:0000269|PubMed:20085589}.
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:0000269|PubMed:20085589}.
CC -!- MISCELLANEOUS: [Isoform 1]: Major isoform. Ubiquitously expressed.
CC -!- MISCELLANEOUS: [Isoform 2]: Major isoform. Preferentially expressed in
CC cardiac and skeletal muscles. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DIXDC1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH35509.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH64479.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAB21826.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB71039.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; DQ642016; ABG25914.1; -; mRNA.
DR EMBL; AB051522; BAB21826.1; ALT_INIT; mRNA.
DR EMBL; AP000907; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471065; EAW67171.1; -; Genomic_DNA.
DR EMBL; BC033034; AAH33034.1; -; mRNA.
DR EMBL; BC035509; AAH35509.1; ALT_SEQ; mRNA.
DR EMBL; BC041626; AAH41626.2; -; mRNA.
DR EMBL; BC048294; AAH48294.1; -; mRNA.
DR EMBL; BC064479; AAH64479.1; ALT_SEQ; mRNA.
DR EMBL; BC128600; AAI28601.1; -; mRNA.
DR EMBL; AK055899; BAB71039.1; ALT_SEQ; mRNA.
DR CCDS; CCDS60957.1; -. [Q155Q3-5]
DR CCDS; CCDS73381.1; -. [Q155Q3-1]
DR CCDS; CCDS73382.1; -. [Q155Q3-2]
DR RefSeq; NP_001033043.1; NM_001037954.3. [Q155Q3-1]
DR RefSeq; NP_001265471.1; NM_001278542.1. [Q155Q3-5]
DR RefSeq; NP_219493.1; NM_033425.4. [Q155Q3-2]
DR PDB; 3PZ7; X-ray; 2.44 A; A=597-683.
DR PDBsum; 3PZ7; -.
DR AlphaFoldDB; Q155Q3; -.
DR SMR; Q155Q3; -.
DR BioGRID; 124542; 26.
DR CORUM; Q155Q3; -.
DR IntAct; Q155Q3; 24.
DR MINT; Q155Q3; -.
DR STRING; 9606.ENSP00000394352; -.
DR iPTMnet; Q155Q3; -.
DR PhosphoSitePlus; Q155Q3; -.
DR BioMuta; DIXDC1; -.
DR DMDM; 147641721; -.
DR EPD; Q155Q3; -.
DR jPOST; Q155Q3; -.
DR MassIVE; Q155Q3; -.
DR MaxQB; Q155Q3; -.
DR PaxDb; Q155Q3; -.
DR PeptideAtlas; Q155Q3; -.
DR PRIDE; Q155Q3; -.
DR ProteomicsDB; 23427; -.
DR ProteomicsDB; 60652; -. [Q155Q3-1]
DR ProteomicsDB; 60653; -. [Q155Q3-2]
DR ProteomicsDB; 60654; -. [Q155Q3-4]
DR Antibodypedia; 32094; 212 antibodies from 31 providers.
DR DNASU; 85458; -.
DR Ensembl; ENST00000440460.7; ENSP00000394352.3; ENSG00000150764.14. [Q155Q3-1]
DR Ensembl; ENST00000529225.5; ENSP00000434130.1; ENSG00000150764.14. [Q155Q3-5]
DR Ensembl; ENST00000615255.1; ENSP00000480808.1; ENSG00000150764.14. [Q155Q3-2]
DR GeneID; 85458; -.
DR KEGG; hsa:85458; -.
DR MANE-Select; ENST00000440460.7; ENSP00000394352.3; NM_001037954.4; NP_001033043.1.
DR UCSC; uc001pmj.4; human. [Q155Q3-1]
DR CTD; 85458; -.
DR DisGeNET; 85458; -.
DR GeneCards; DIXDC1; -.
DR HGNC; HGNC:23695; DIXDC1.
DR HPA; ENSG00000150764; Low tissue specificity.
DR MIM; 610493; gene.
DR neXtProt; NX_Q155Q3; -.
DR OpenTargets; ENSG00000150764; -.
DR PharmGKB; PA134988674; -.
DR VEuPathDB; HostDB:ENSG00000150764; -.
DR eggNOG; ENOG502RD5G; Eukaryota.
DR GeneTree; ENSGT00950000182903; -.
DR HOGENOM; CLU_111841_0_0_1; -.
DR InParanoid; Q155Q3; -.
DR OMA; AHFKPTA; -.
DR OrthoDB; 949210at2759; -.
DR PhylomeDB; Q155Q3; -.
DR PathwayCommons; Q155Q3; -.
DR SignaLink; Q155Q3; -.
DR BioGRID-ORCS; 85458; 13 hits in 1021 CRISPR screens.
DR ChiTaRS; DIXDC1; human.
DR GeneWiki; DIXDC1; -.
DR GenomeRNAi; 85458; -.
DR Pharos; Q155Q3; Tbio.
DR PRO; PR:Q155Q3; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q155Q3; protein.
DR Bgee; ENSG00000150764; Expressed in calcaneal tendon and 206 other tissues.
DR ExpressionAtlas; Q155Q3; baseline and differential.
DR Genevisible; Q155Q3; HS.
DR GO; GO:0043679; C:axon terminus; IEA:Ensembl.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0043015; F:gamma-tubulin binding; IDA:UniProtKB.
DR GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:UniProtKB.
DR GO; GO:0021695; P:cerebellar cortex development; IEA:Ensembl.
DR GO; GO:0021799; P:cerebral cortex radially oriented cell migration; IEA:Ensembl.
DR GO; GO:0021869; P:forebrain ventricular zone progenitor cell division; IEA:Ensembl.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IEA:Ensembl.
DR GO; GO:0050772; P:positive regulation of axonogenesis; IEA:Ensembl.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IEA:Ensembl.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IEA:Ensembl.
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; Lipoprotein;
KW Myristate; Phosphoprotein; Reference proteome; Ubl conjugation;
KW Wnt signaling pathway.
FT CHAIN 1..683
FT /note="Dixin"
FT /id="PRO_0000287223"
FT DOMAIN 20..127
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 127..300
FT /note="Actin-binding"
FT /evidence="ECO:0000269|PubMed:16814745"
FT REGION 207..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 279..452
FT /evidence="ECO:0000255"
FT COMPBIAS 573..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80Y83"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80Y83"
FT MOD_RES 590
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..211
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11214970,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_025378"
FT VAR_SEQ 1..20
FT /note="MLACLTRGNLLDVLQEGFNE -> MGTQVVMRFNNSLLPTEPS (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054565"
FT VAR_SEQ 212..219
FT /note="PSESSCSS -> MGGTQVKC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11214970,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_025379"
FT VAR_SEQ 219
FT /note="S -> R (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025380"
FT VAR_SEQ 220..683
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025381"
FT VARIANT 300
FT /note="K -> R (in dbSNP:rs34575249)"
FT /id="VAR_032294"
FT MUTAGEN 648
FT /note="D->A: Loss of interaction with DVL2. Abolishes
FT activation of Wnt signaling."
FT /evidence="ECO:0000269|PubMed:21189423"
FT MUTAGEN 651
FT /note="F->A: Loss of interaction with DVL2. Abolishes
FT activation of Wnt signaling."
FT /evidence="ECO:0000269|PubMed:21189423"
FT MUTAGEN 655
FT /note="K->A: Loss of interaction with DVL2. Abolishes
FT activation of Wnt signaling."
FT /evidence="ECO:0000269|PubMed:21189423"
FT CONFLICT 140
FT /note="S -> P (in Ref. 1; ABG25914)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="L -> R (in Ref. 1; ABG25914)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="H -> Q (in Ref. 1; ABG25914)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="L -> S (in Ref. 3; BAB71039)"
FT /evidence="ECO:0000305"
FT STRAND 601..606
FT /evidence="ECO:0007829|PDB:3PZ7"
FT STRAND 614..620
FT /evidence="ECO:0007829|PDB:3PZ7"
FT HELIX 627..634
FT /evidence="ECO:0007829|PDB:3PZ7"
FT STRAND 640..648
FT /evidence="ECO:0007829|PDB:3PZ7"
FT TURN 649..651
FT /evidence="ECO:0007829|PDB:3PZ7"
FT STRAND 652..658
FT /evidence="ECO:0007829|PDB:3PZ7"
FT STRAND 671..678
FT /evidence="ECO:0007829|PDB:3PZ7"
FT INIT_MET Q155Q3-2:1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT LIPID Q155Q3-2:2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:20213681"
SQ SEQUENCE 683 AA; 77478 MW; E643D1A69B00238C CRC64;
MLACLTRGNL LDVLQEGFNE QQLQAYVAWV NAQLKKRPAV KPVQDLRQDL RDGVILAYLI
EIVAGEKLSG VQLSPGNQQE MKNNVEKVLQ FVASKKIRMH QTSAKDIVDG NLKSIMRLVL
ALAAHFKPGS SRTVNQGRDS RAPLQSHRPH CATAVAQGAA AALADVCHDM SRSGRDVFRY
RQRNSSMDEE IENPYWSVRA LVQQYEGQQR SPSESSCSSL TSPSPIHSAK SESIITQSEE
KADFVIIPAE GIENRTEGTD SPLSRDWRPG SPGTYLETSW EEQLLEQQEY LEKEMEEAKK
MISGLQALLL NGSLPEDEQE RPLALCEPGV NPEEQLIIIQ SRLDQSMEEN QDLKKELLKC
KQEARNLQGI KDALQQRLTQ QDTSVLQLKQ ELLRANMDKD ELHNQNVDLQ RKLDERNRLL
GEYKKELGQK DRLLQQHQAK LEEALRKLSD VSYHQVDLER ELEHKDVLLA HCMKREADEA
TNYNSHNSQS NGFLLPTAGK GATSVSNRGT SDLQLVRDAL RSLRNSFSGH DPQHHTIDSL
EQGISSLMER LHVMETQKKQ ERKVRVKSPR TQVGSEYRES WPPNSKLPHS QSSPTVSSTC
TKVLYFTDRS LTPFMVNIPK RLEEVTLKDF KAAIDREGNH RYHFKALDPE FGTVKEEIFH
DDDAIPGWEG KIVAWVEEDH GEN
