AIDA_MOUSE
ID AIDA_MOUSE Reviewed; 305 AA.
AC Q8C4Q6; Q3U6V0; Q3UP85; Q6NXY2; Q6PG77; Q78W09; Q99K80;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Axin interactor, dorsalization-associated protein;
DE AltName: Full=Axin interaction partner and dorsalization antagonist;
GN Name=Aida;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Bone marrow, Embryo, Head, Inner ear, Placenta, and Spleen;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and Czech II;
RC TISSUE=Brain, Embryonic germ cell, and Mammary tumor;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, and Spleen;
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 [4]
RP STRUCTURE BY NMR OF 1-115.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of four helical up-and-down bundle domain of the
RT hypothetical protein 2610208m17RIK similar to the protein FLJ12806.";
RL Submitted (AUG-2004) to the PDB data bank.
RN [5]
RP FUNCTION, AND INTERACTION WITH AXIN.
RX PubMed=17681137; DOI=10.1016/j.devcel.2007.07.006;
RA Rui Y., Xu Z., Xiong B., Cao Y., Lin S., Zhang M., Chan S.-C., Luo W.,
RA Han Y., Lu Z., Ye Z., Zhou H.-M., Han J., Meng A., Lin S.-C.;
RT "A beta-catenin-independent dorsalization pathway activated by Axin/JNK
RT signaling and antagonized by aida.";
RL Dev. Cell 13:268-282(2007).
CC -!- FUNCTION: Acts as a ventralizing factor during embryogenesis (By
CC similarity). Inhibits axin-mediated JNK activation by binding axin and
CC disrupting axin homodimerization. This in turn antagonizes a Wnt/beta-
CC catenin-independent dorsalization pathway activated by AXIN/JNK-
CC signaling. {ECO:0000250, ECO:0000269|PubMed:17681137}.
CC -!- SUBUNIT: Interacts with AXIN1. {ECO:0000269|PubMed:17681137}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8C4Q6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C4Q6-2; Sequence=VSP_028323;
CC -!- SIMILARITY: Belongs to the AIDA family. {ECO:0000255|PROSITE-
CC ProRule:PRU01259, ECO:0000305}.
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DR EMBL; AK027971; BAC25682.1; -; mRNA.
DR EMBL; AK081494; BAC38234.1; -; mRNA.
DR EMBL; AK143716; BAE25512.1; -; mRNA.
DR EMBL; AK149788; BAE29085.1; -; mRNA.
DR EMBL; AK150639; BAE29727.1; -; mRNA.
DR EMBL; AK150702; BAE29781.1; -; mRNA.
DR EMBL; AK152961; BAE31624.1; -; mRNA.
DR EMBL; AK153448; BAE32003.1; -; mRNA.
DR EMBL; AK159318; BAE34985.1; -; mRNA.
DR EMBL; AK167520; BAE39592.1; -; mRNA.
DR EMBL; AK172451; BAE43012.1; -; mRNA.
DR EMBL; AK158103; BAE34358.1; -; mRNA.
DR EMBL; BC057183; AAH57183.1; -; mRNA.
DR EMBL; BC066829; AAH66829.1; -; mRNA.
DR EMBL; BC086763; AAH86763.1; -; mRNA.
DR CCDS; CCDS56663.1; -. [Q8C4Q6-1]
DR RefSeq; NP_859421.1; NM_181732.4. [Q8C4Q6-1]
DR PDB; 1UG7; NMR; -; A=1-115.
DR PDB; 2QZ5; X-ray; 2.60 A; A/B=151-305.
DR PDBsum; 1UG7; -.
DR PDBsum; 2QZ5; -.
DR AlphaFoldDB; Q8C4Q6; -.
DR BMRB; Q8C4Q6; -.
DR SMR; Q8C4Q6; -.
DR BioGRID; 224467; 1.
DR IntAct; Q8C4Q6; 2.
DR MINT; Q8C4Q6; -.
DR STRING; 10090.ENSMUSP00000104795; -.
DR iPTMnet; Q8C4Q6; -.
DR PhosphoSitePlus; Q8C4Q6; -.
DR REPRODUCTION-2DPAGE; Q8C4Q6; -.
DR EPD; Q8C4Q6; -.
DR MaxQB; Q8C4Q6; -.
DR PaxDb; Q8C4Q6; -.
DR PeptideAtlas; Q8C4Q6; -.
DR PRIDE; Q8C4Q6; -.
DR ProteomicsDB; 285785; -. [Q8C4Q6-1]
DR ProteomicsDB; 285786; -. [Q8C4Q6-2]
DR Antibodypedia; 34630; 136 antibodies from 23 providers.
DR DNASU; 108909; -.
DR Ensembl; ENSMUST00000109166; ENSMUSP00000104795; ENSMUSG00000042901. [Q8C4Q6-1]
DR Ensembl; ENSMUST00000193625; ENSMUSP00000141649; ENSMUSG00000042901. [Q8C4Q6-2]
DR GeneID; 108909; -.
DR KEGG; mmu:108909; -.
DR UCSC; uc008icu.2; mouse. [Q8C4Q6-1]
DR CTD; 64853; -.
DR MGI; MGI:1919737; Aida.
DR VEuPathDB; HostDB:ENSMUSG00000042901; -.
DR eggNOG; ENOG502QSD5; Eukaryota.
DR GeneTree; ENSGT00390000016465; -.
DR HOGENOM; CLU_064322_0_0_1; -.
DR InParanoid; Q8C4Q6; -.
DR OMA; KLHAAWC; -.
DR OrthoDB; 1196787at2759; -.
DR PhylomeDB; Q8C4Q6; -.
DR TreeFam; TF328541; -.
DR BioGRID-ORCS; 108909; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Aida; mouse.
DR EvolutionaryTrace; Q8C4Q6; -.
DR PRO; PR:Q8C4Q6; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8C4Q6; protein.
DR Bgee; ENSMUSG00000042901; Expressed in embryonic post-anal tail and 243 other tissues.
DR ExpressionAtlas; Q8C4Q6; baseline and differential.
DR Genevisible; Q8C4Q6; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0035091; F:phosphatidylinositol binding; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; IPI:MGI.
DR GO; GO:0048264; P:determination of ventral identity; ISO:MGI.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; ISS:UniProtKB.
DR GO; GO:2000016; P:negative regulation of determination of dorsal identity; ISO:MGI.
DR GO; GO:0046329; P:negative regulation of JNK cascade; IMP:UniProtKB.
DR GO; GO:0043508; P:negative regulation of JUN kinase activity; IDA:MGI.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; IMP:UniProtKB.
DR GO; GO:0043254; P:regulation of protein-containing complex assembly; IMP:MGI.
DR Gene3D; 1.20.120.360; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR025939; Aida_C.
DR InterPro; IPR023421; AIDA_N.
DR InterPro; IPR036818; AIDA_N_sf.
DR InterPro; IPR035892; C2_domain_sf.
DR Pfam; PF14186; Aida_C2; 1.
DR Pfam; PF08910; Aida_N; 1.
DR SUPFAM; SSF109779; SSF109779; 1.
DR PROSITE; PS51911; C2_AIDA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Developmental protein;
KW Reference proteome.
FT CHAIN 1..305
FT /note="Axin interactor, dorsalization-associated protein"
FT /id="PRO_0000305279"
FT DOMAIN 156..303
FT /note="C2 Aida-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01259"
FT REGION 128..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..220
FT /note="Axin-binding"
FT COILED 27..62
FT /evidence="ECO:0000255"
FT VAR_SEQ 153..234
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028323"
FT CONFLICT 138
FT /note="G -> V (in Ref. 2; AAH66829)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="R -> K (in Ref. 1; BAE31624)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="R -> K (in Ref. 1; BAE34358)"
FT /evidence="ECO:0000305"
FT HELIX 4..25
FT /evidence="ECO:0007829|PDB:1UG7"
FT HELIX 28..46
FT /evidence="ECO:0007829|PDB:1UG7"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:1UG7"
FT HELIX 57..78
FT /evidence="ECO:0007829|PDB:1UG7"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:1UG7"
FT HELIX 94..99
FT /evidence="ECO:0007829|PDB:1UG7"
FT TURN 100..103
FT /evidence="ECO:0007829|PDB:1UG7"
FT STRAND 167..176
FT /evidence="ECO:0007829|PDB:2QZ5"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:2QZ5"
FT STRAND 184..193
FT /evidence="ECO:0007829|PDB:2QZ5"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:2QZ5"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:2QZ5"
FT STRAND 216..224
FT /evidence="ECO:0007829|PDB:2QZ5"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:2QZ5"
FT STRAND 237..246
FT /evidence="ECO:0007829|PDB:2QZ5"
FT TURN 247..250
FT /evidence="ECO:0007829|PDB:2QZ5"
FT STRAND 251..261
FT /evidence="ECO:0007829|PDB:2QZ5"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:2QZ5"
FT STRAND 267..272
FT /evidence="ECO:0007829|PDB:2QZ5"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:2QZ5"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:2QZ5"
FT STRAND 296..303
FT /evidence="ECO:0007829|PDB:2QZ5"
SQ SEQUENCE 305 AA; 34888 MW; A285C564AF5333D0 CRC64;
MSEVTRSLLQ RWGASLRRGA DFDSWGQLVE AIDEYQILAR HLQKEAQAQH NNSEFTEEQK
KTIGKIATCL ELRSAALQST QSQEEFKLED LKKLEPILKN ILTYNKEFPF DVQPIPLRRI
LAPGEEENLE FEEDEEGGAG AGPPDSFSAR VPGTLLPRLP SEPGMTLLTI RIEKIGLKDA
GQCIDPYITV SVKDLNGIDL TPVQDTPVAS RKEDTYVHFN VDIELQKHVE RLTKGAAIFF
EFKHYKPKKR FTSTKCFAFM EMDEIKPGPI VIELYKKPTD FKRKKLQLLT KKPLYLHLHQ
SLHKE
