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Q8C4Q6 (AIDA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Axin interactor, dorsalization-associated protein
Alternative name(s):
Axin interaction partner and dorsalization antagonist
Gene names
Name:Aida
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length305 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as a ventralizing factor during embryogenesis By similarity. Inhibits axin-mediated JNK activation by binding axin and disrupting axin homodimerization. This in turn antagonizes a Wnt/beta-catenin-independent dorsalization pathway activated by AXIN/JNK-signaling. Ref.4

Subunit structure

Interacts with AXIN1. Ref.4

Sequence similarities

Belongs to the AIDA family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8C4Q6-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8C4Q6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     153-234: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 305305Axin interactor, dorsalization-associated protein
PRO_0000305279

Regions

Region153 – 22068Axin-binding
Coiled coil27 – 6236 Potential

Natural variations

Alternative sequence153 – 23482Missing in isoform 2.
VSP_028323

Experimental info

Sequence conflict1381G → V in AAH66829. Ref.2
Sequence conflict1711R → K in BAE31624. Ref.1
Sequence conflict2311R → K in BAE34358. Ref.1

Secondary structure

......................................... 305
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: A285C564AF5333D0

FASTA30534,888
        10         20         30         40         50         60 
MSEVTRSLLQ RWGASLRRGA DFDSWGQLVE AIDEYQILAR HLQKEAQAQH NNSEFTEEQK 

        70         80         90        100        110        120 
KTIGKIATCL ELRSAALQST QSQEEFKLED LKKLEPILKN ILTYNKEFPF DVQPIPLRRI 

       130        140        150        160        170        180 
LAPGEEENLE FEEDEEGGAG AGPPDSFSAR VPGTLLPRLP SEPGMTLLTI RIEKIGLKDA 

       190        200        210        220        230        240 
GQCIDPYITV SVKDLNGIDL TPVQDTPVAS RKEDTYVHFN VDIELQKHVE RLTKGAAIFF 

       250        260        270        280        290        300 
EFKHYKPKKR FTSTKCFAFM EMDEIKPGPI VIELYKKPTD FKRKKLQLLT KKPLYLHLHQ 


SLHKE 

« Hide

Isoform 2 [UniParc].

Checksum: F80B8D98D3B0A126
Show »

FASTA22325,750

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6J and NOD.
Tissue: Bone marrow, Embryo, Head, Inner ear, Placenta and Spleen.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: C57BL/6 and Czech II.
Tissue: Brain, Embryonic germ cell and Mammary tumor.
[3]"Solution structure of four helical up-and-down bundle domain of the hypothetical protein 2610208m17RIK similar to the protein FLJ12806."
RIKEN structural genomics initiative (RSGI)
Submitted (AUG-2004) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 1-115.
[4]"A beta-catenin-independent dorsalization pathway activated by Axin/JNK signaling and antagonized by aida."
Rui Y., Xu Z., Xiong B., Cao Y., Lin S., Zhang M., Chan S.-C., Luo W., Han Y., Lu Z., Ye Z., Zhou H.-M., Han J., Meng A., Lin S.-C.
Dev. Cell 13:268-282(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH AXIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK027971 mRNA. Translation: BAC25682.1.
AK081494 mRNA. Translation: BAC38234.1.
AK143716 mRNA. Translation: BAE25512.1.
AK149788 mRNA. Translation: BAE29085.1.
AK150639 mRNA. Translation: BAE29727.1.
AK150702 mRNA. Translation: BAE29781.1.
AK152961 mRNA. Translation: BAE31624.1.
AK153448 mRNA. Translation: BAE32003.1.
AK159318 mRNA. Translation: BAE34985.1.
AK167520 mRNA. Translation: BAE39592.1.
AK172451 mRNA. Translation: BAE43012.1.
AK158103 mRNA. Translation: BAE34358.1.
BC057183 mRNA. Translation: AAH57183.1.
BC066829 mRNA. Translation: AAH66829.1.
BC086763 mRNA. Translation: AAH86763.1.
IPIIPI00311123.
IPI00664676.
RefSeqNP_859421.1. NM_181732.4.
UniGeneMm.290502.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1UG7NMR-A1-115[»]
2QZ5X-ray2.60A/B151-305[»]
ProteinModelPortalQ8C4Q6.
SMRQ8C4Q6. Positions 3-115, 151-304.
ModBaseSearch...

PTM databases

PhosphoSiteQ8C4Q6.

2D gel databases

REPRODUCTION-2DPAGEQ8C4Q6.

Proteomic databases

PaxDbQ8C4Q6.
PRIDEQ8C4Q6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000109166; ENSMUSP00000104795; ENSMUSG00000042901.
GeneID108909.
KEGGmmu:108909.
UCSCuc008icu.2. mouse.

Organism-specific databases

CTD64853.
MGIMGI:1919737. Aida.

Phylogenomic databases

eggNOGNOG48105.
GeneTreeENSGT00390000016465.
HOVERGENHBG057354.
InParanoidQ8C4Q6.
OMAATCLEMR.
OrthoDBEOG4640CJ.

Gene expression databases

BgeeQ8C4Q6.
GenevestigatorQ8C4Q6.

Family and domain databases

Gene3D1.20.120.360. 1 hit.
InterProIPR015006. AIDA.
IPR025939. Aida_C.
IPR023421. AIDA_N.
[Graphical view]
PfamPF08910. Aida-C2. 1 hit.
PF14186. Aida_C2. 1 hit.
[Graphical view]
SUPFAMSSF109779. SSF109779. 1 hit.
ProtoNetSearch...

Other

ChiTaRSAIDA. mouse.
EvolutionaryTraceQ8C4Q6.
NextBio361453.
SOURCESearch...

Entry information

Entry nameAIDA_MOUSE
AccessionPrimary (citable) accession number: Q8C4Q6
Secondary accession number(s): Q3U6V0 expand/collapse secondary AC list , Q3UP85, Q6NXY2, Q6PG77, Q78W09, Q99K80
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: March 1, 2003
Last modified: April 3, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families