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O70200 (AIF1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 111. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Allograft inflammatory factor 1

Short name=AIF-1
Alternative name(s):
Ionized calcium-binding adapter molecule 1
Gene names
Name:Aif1
Synonyms:Iba1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length147 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Actin-binding protein that enhances membrane ruffling and RAC activation. Enhances the actin-bundling activity of LCP1. Binds calcium. Plays a role in RAC signaling and in phagocytosis. May play a role in macrophage activation and function. Promotes the proliferation of vascular smooth muscle cells and of T-lymphocytes. Enhances lymphocyte migration. Plays a role in vascular inflammation. Ref.1 Ref.7 Ref.8 Ref.9 Ref.10

Subunit structure

Homodimer Potential. Monomer. Interacts with LCP1. Ref.10 Ref.11

Subcellular location

Cytoplasmcytoskeleton. Cell projectionruffle membrane; Peripheral membrane protein; Cytoplasmic side. Note: Associated with the actin cytoskeleton at membrane ruffles and at sites of phagocytosis. Ref.7 Ref.10

Tissue specificity

Abundantly expressed in the testis, moderately in the spleen and lymph nodes and at low levels in the liver and thymus. Detected in macrophages. Ref.1

Post-translational modification

Phosphorylated on serine residues By similarity.

Sequence similarities

Contains 2 EF-hand domains.

Ontologies

Keywords
   Cellular componentCell membrane
Cell projection
Cytoplasm
Cytoskeleton
Membrane
   DomainRepeat
   LigandActin-binding
Calcium
Metal-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRac protein signal transduction

Inferred from mutant phenotype Ref.7. Source: UniProtKB

actin filament bundle assembly

Inferred from sequence or structural similarity. Source: UniProtKB

actin filament polymerization

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to interferon-gamma

Inferred from sequence or structural similarity. Source: UniProtKB

inflammatory response

Inferred from sequence or structural similarity. Source: UniProtKB

microglial cell activation

Non-traceable author statement Ref.11. Source: UniProtKB

negative regulation of smooth muscle cell chemotaxis

Inferred from electronic annotation. Source: Ensembl

negative regulation of smooth muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

phagocytosis, engulfment

Inferred from mutant phenotype Ref.7. Source: UniProtKB

positive regulation of G1/S transition of mitotic cell cycle

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of T cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of T cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of monocyte chemotaxis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of smooth muscle cell chemotaxis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of smooth muscle cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

ruffle assembly

Inferred from mutant phenotype Ref.7. Source: UniProtKB

   Cellular_componentactin filament

Inferred from direct assay Ref.10. Source: MGI

cytoplasm

Inferred from direct assay Ref.7. Source: UniProtKB

cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

lamellipodium

Inferred from direct assay Ref.7. Source: UniProtKB

nucleus

Inferred from direct assay Ref.7. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

phagocytic cup

Inferred from direct assay Ref.7. Source: UniProtKB

ruffle

Inferred from direct assay Ref.10. Source: MGI

ruffle membrane

Inferred from direct assay Ref.7. Source: UniProtKB

   Molecular_functionactin filament binding

Inferred from sequence or structural similarity. Source: UniProtKB

calcium ion binding

Inferred from direct assay Ref.11. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.10. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 147146Allograft inflammatory factor 1
PRO_0000073867

Regions

Domain45 – 8036EF-hand 1
Domain81 – 11535EF-hand 2; degenerate
Calcium binding58 – 69121 Potential
Calcium binding94 – 105122 Ref.11

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue111N6-acetyllysine By similarity

Secondary structure

................ 147
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O70200 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: D8974825C153D3CA

FASTA14716,911
        10         20         30         40         50         60 
MSQSRDLQGG KAFGLLKAQQ EERLEGINKQ FLDDPKYSND EDLPSKLEAF KVKYMEFDLN 

        70         80         90        100        110        120 
GNGDIDIMSL KRMLEKLGVP KTHLELKRLI REVSSGSEET FSYSDFLRMM LGKRSAILRM 

       130        140 
ILMYEEKNKE HKRPTGPPAK KAISELP 

« Hide

References

« Hide 'large scale' references
[1]"Allograft inflammatory factor-1 augments productions of interleukin-6, -10, -12 by a mouse macrophage line."
Watano K., Iwabuchi K., Fujii S., Ishimori N., Mitsuhashi S., Ato M., Kitabatake A., Onoe K.
Immunology 104:307-316(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
[2]"Structure of the mouse iba1 gene."
Imai Y., Ohsawa K., Kohsaka S.
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Strain: 129/SvJ.
[3]"Allograft inflammatory factor-1 gene."
Hu S.P., Russell M.E.
Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Strain: 129/Sv.
[4]"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].
Strain: C57BL/6J.
Tissue: Testis.
[5]"Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse."
Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L.
Genome Res. 13:2621-2636(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 129.
[6]"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].
Strain: FVB/N.
Tissue: Mammary tumor.
[7]"Involvement of Iba1 in membrane ruffling and phagocytosis of macrophages/microglia."
Ohsawa K., Imai Y., Kanazawa H., Sasaki Y., Kohsaka S.
J. Cell Sci. 113:3073-3084(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[8]"Iba1 is an actin-cross-linking protein in macrophages/microglia."
Sasaki Y., Ohsawa K., Kanazawa H., Kohsaka S., Imai Y.
Biochem. Biophys. Res. Commun. 286:292-297(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Macrophage/microglia-specific protein Iba1 enhances membrane ruffling and Rac activation via phospholipase C-gamma -dependent pathway."
Kanazawa H., Ohsawa K., Sasaki Y., Kohsaka S., Imai Y.
J. Biol. Chem. 277:20026-20032(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"Microglia/macrophage-specific protein Iba1 binds to fimbrin and enhances its actin-bundling activity."
Ohsawa K., Imai Y., Sasaki Y., Kohsaka S.
J. Neurochem. 88:844-856(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH LCP1.
[11]"X-ray structures of the microglia/macrophage-specific protein Iba1 from human and mouse demonstrate novel molecular conformation change induced by calcium binding."
Yamada M., Ohsawa K., Imai Y., Kohsaka S., Kamitori S.
J. Mol. Biol. 364:449-457(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH CALCIUM IONS, CALCIUM-BINDING, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB013745 mRNA. Translation: BAA28216.1.
AB036423 Genomic DNA. Translation: BAB20758.1.
D86382 mRNA. Translation: BAA86387.1.
AF074959 mRNA. Translation: AAC25604.1.
U82792 Genomic DNA. Translation: AAC24189.1.
AK006184 mRNA. Translation: BAB24445.1.
AK006562 mRNA. Translation: BAB24654.1.
AF109719 Genomic DNA. Translation: AAC82481.1.
BC021539 mRNA. Translation: AAH21539.1.
CCDSCCDS28689.1.
RefSeqNP_062340.1. NM_019467.2.
XP_006523565.1. XM_006523502.1.
XP_006523566.1. XM_006523503.1.
XP_006523567.1. XM_006523504.1.
XP_006525339.1. XM_006525276.1.
XP_006525340.1. XM_006525277.1.
XP_006525341.1. XM_006525278.1.
XP_006536564.1. XM_006536501.1.
XP_006536565.1. XM_006536502.1.
XP_006536566.1. XM_006536503.1.
XP_006537297.1. XM_006537234.1.
XP_006537298.1. XM_006537235.1.
XP_006537299.1. XM_006537236.1.
UniGeneMm.10747.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WY9X-ray2.10A1-147[»]
ProteinModelPortalO70200.
SMRO70200. Positions 17-127.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198041. 2 interactions.

PTM databases

PhosphoSiteO70200.

Proteomic databases

MaxQBO70200.
PaxDbO70200.
PRIDEO70200.

Protocols and materials databases

DNASU11629.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025257; ENSMUSP00000025257; ENSMUSG00000024397.
ENSMUST00000172693; ENSMUSP00000134214; ENSMUSG00000024397.
ENSMUST00000173324; ENSMUSP00000133709; ENSMUSG00000024397.
GeneID11629.
KEGGmmu:11629.
UCSCuc008cgl.1. mouse.

Organism-specific databases

CTD199.
MGIMGI:1343098. Aif1.

Phylogenomic databases

eggNOGNOG262998.
HOGENOMHOG000231928.
HOVERGENHBG004002.
InParanoidO70200.
OMADIDIMEL.
OrthoDBEOG73FQPC.
PhylomeDBO70200.
TreeFamTF320736.

Gene expression databases

ArrayExpressO70200.
BgeeO70200.
CleanExMM_AIF1.
GenevestigatorO70200.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
InterProIPR011992. EF-hand-dom_pair.
IPR002048. EF_hand_dom.
[Graphical view]
PROSITEPS50222. EF_HAND_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO70200.
NextBio279187.
PROO70200.
SOURCESearch...

Entry information

Entry nameAIF1_MOUSE
AccessionPrimary (citable) accession number: O70200
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: August 1, 1998
Last modified: July 9, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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