DIXC1_RAT
ID DIXC1_RAT Reviewed; 684 AA.
AC Q2VUH7;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 2.
DT 03-AUG-2022, entry version 108.
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;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Brown Norway;
RA Zhou G., Wang X., Qian C., Liu W.;
RT "Cloning of wnt pathway protein dixin.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
CC -!- FUNCTION: Positive effector of the Wnt signaling pathway; activates
CC WNT3A signaling via DVL2. Regulates JNK activation by AXIN1 and DVL2.
CC {ECO:0000250|UniProtKB:Q155Q3}.
CC -!- SUBUNIT: May bind filamentous actin. Interacts with the complex
CC composed of DVL2 and Rac. Interacts with AXIN1; competes with MAP3K1.
CC Interacts with MAP3K4 preventing MAP3K4 interaction with AXIN1.
CC Directly interacts (via DIX domain) with DVL2 (via DIX domain).
CC Interacts with gamma-tubulin. {ECO:0000250|UniProtKB:Q155Q3}.
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 -!- 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 (By similarity).
CC {ECO:0000250|UniProtKB:Q155Q3}.
CC -!- SIMILARITY: Belongs to the DIXDC1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAX76925.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; AY770507; AAX76925.1; ALT_SEQ; mRNA.
DR EMBL; AC094189; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC132668; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001032743.1; NM_001037654.1.
DR RefSeq; XP_006243104.1; XM_006243042.3.
DR AlphaFoldDB; Q2VUH7; -.
DR SMR; Q2VUH7; -.
DR STRING; 10116.ENSRNOP00000037500; -.
DR iPTMnet; Q2VUH7; -.
DR PhosphoSitePlus; Q2VUH7; -.
DR PaxDb; Q2VUH7; -.
DR PRIDE; Q2VUH7; -.
DR GeneID; 363062; -.
DR KEGG; rno:363062; -.
DR UCSC; RGD:1309902; rat.
DR CTD; 85458; -.
DR RGD; 1309902; Dixdc1.
DR eggNOG; ENOG502RD5G; Eukaryota.
DR HOGENOM; CLU_025678_0_0_1; -.
DR InParanoid; Q2VUH7; -.
DR OrthoDB; 949210at2759; -.
DR PhylomeDB; Q2VUH7; -.
DR PRO; PR:Q2VUH7; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000010260; Expressed in cerebellum and 20 other tissues.
DR ExpressionAtlas; Q2VUH7; baseline and differential.
DR Genevisible; Q2VUH7; RN.
DR GO; GO:0043679; C:axon terminus; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
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; IDA:RGD.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0021846; P:cell proliferation in forebrain; ISO:RGD.
DR GO; GO:0021695; P:cerebellar cortex development; IMP:RGD.
DR GO; GO:0021795; P:cerebral cortex cell migration; ISO:RGD.
DR GO; GO:0021799; P:cerebral cortex radially oriented cell migration; ISO:RGD.
DR GO; GO:0021869; P:forebrain ventricular zone progenitor cell division; ISO:RGD.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; ISO:RGD.
DR GO; GO:0050772; P:positive regulation of axonogenesis; IMP:RGD.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IMP:RGD.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; ISO:RGD.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISO:RGD.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; ISO:RGD.
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 2: Evidence at transcript level;
KW Actin-binding; Cell junction; Coiled coil; Cytoplasm; Cytoskeleton;
KW Developmental protein; Phosphoprotein; Reference proteome; Ubl conjugation;
KW Wnt signaling pathway.
FT CHAIN 1..684
FT /note="Dixin"
FT /id="PRO_0000287225"
FT DOMAIN 20..127
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 602..682
FT /note="DIX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00069"
FT REGION 127..300
FT /note="Actin-binding"
FT /evidence="ECO:0000250|UniProtKB:Q155Q3"
FT REGION 207..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 277..308
FT /evidence="ECO:0000255"
FT COILED 336..461
FT /evidence="ECO:0000255"
FT COMPBIAS 572..597
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 592
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q155Q3"
SQ SEQUENCE 684 AA; 77303 MW; 38917BE82F544568 CRC64;
MLACLTRGNL LDVLQEGFNE QQLQAYVAWV NAQLKKRPSV KPVQDLRQDL RDGVILAYLI
EIVAGEKLSG VQLSPSNQQE MKSNVERVLQ FVASKNIRMH QTSAKDIVEG NLKSIMRLVL
ALAAHFKPGS SRTVSQGRDS RTSVQSHQPH CATAVAQGAA AALADVCHDV SRSGRDVFRY
RQRNASVDEE IENPYWSVRA LVQQYEGQQR SPSESSCSSL TSPSPIHSAK SESIITQSEE
KADFVIIPSE GIENRTDETG SPLSRDWRPG SPGTYLEATW EEQLLEQQEH LEKEMEEAKK
MISGLQALLL NGSLPEDEQE RPVALCEPGV NPEEQLIIIR SRLDQSMEEN QDLKKELLKC
KQEARNLQGI KDALQQRLTQ QDTSVLQLKQ ELLRANMDKD ELHNQNVDLQ RKLDERNRLL
GEYKKDLGQK DRLLQQQQAK LEDALRKLSD ASYQQVDLER ELEQKDVLLA HRVKGDTDEV
TNYNSHSSQR NGFVLPVAGR AATTATHRGP QSSDLQLVRD ALRSLRNSFS GHDPQHHTID
SLEQGISSLI ERLHVIETQK KQERKVRGRS PRNQASSEYR ASWPPNSTLP HSQSSPAVSN
TCTKVLYFTD RSLTPFMVNI PKRLGEVTLK DFKAAIDREG SHRYHFKALD PEFGTVKEEV
FHDDDAIPGW EGKIVAWVED HREN
