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Protein

Allograft inflammatory factor 1

Gene

Aif1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.5 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi58 – 69121PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi94 – 105122Add
BLAST

GO - Molecular functioni

  1. actin filament binding Source: UniProtKB
  2. calcium ion binding Source: UniProtKB

GO - Biological processi

  1. actin filament bundle assembly Source: UniProtKB
  2. actin filament polymerization Source: UniProtKB
  3. cellular response to extracellular stimulus Source: Ensembl
  4. cellular response to hormone stimulus Source: Ensembl
  5. cellular response to hydroperoxide Source: Ensembl
  6. cellular response to interferon-gamma Source: UniProtKB
  7. cellular response to morphine Source: Ensembl
  8. inflammatory response Source: UniProtKB
  9. microglial cell activation Source: UniProtKB
  10. negative regulation of apoptotic process Source: Ensembl
  11. negative regulation of gene expression Source: Ensembl
  12. negative regulation of smooth muscle cell chemotaxis Source: MGI
  13. negative regulation of smooth muscle cell proliferation Source: MGI
  14. phagocytosis, engulfment Source: UniProtKB
  15. positive regulation of G1/S transition of mitotic cell cycle Source: UniProtKB
  16. positive regulation of monocyte chemotaxis Source: UniProtKB
  17. positive regulation of muscle hyperplasia Source: Ensembl
  18. positive regulation of nitric oxide biosynthetic process Source: Ensembl
  19. positive regulation of protein phosphorylation Source: Ensembl
  20. positive regulation of smooth muscle cell chemotaxis Source: UniProtKB
  21. positive regulation of smooth muscle cell proliferation Source: UniProtKB
  22. positive regulation of T cell migration Source: UniProtKB
  23. positive regulation of T cell proliferation Source: UniProtKB
  24. Rac protein signal transduction Source: UniProtKB
  25. response to axon injury Source: Ensembl
  26. response to electrical stimulus Source: Ensembl
  27. ruffle assembly Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Actin-binding, Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Allograft inflammatory factor 1
Short name:
AIF-1
Alternative name(s):
Ionized calcium-binding adapter molecule 1
Gene namesi
Name:Aif1
Synonyms:Iba1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1343098. Aif1.

Subcellular locationi

  1. Cytoplasmcytoskeleton
  2. Cell projectionruffle membrane; Peripheral membrane protein; Cytoplasmic side

  3. Note: Associated with the actin cytoskeleton at membrane ruffles and at sites of phagocytosis.

GO - Cellular componenti

  1. actin filament Source: MGI
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: UniProtKB
  4. lamellipodium Source: UniProtKB
  5. nucleus Source: UniProtKB
  6. perikaryon Source: Ensembl
  7. perinuclear region of cytoplasm Source: MGI
  8. phagocytic cup Source: UniProtKB
  9. ruffle Source: MGI
  10. ruffle membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 147146Allograft inflammatory factor 1PRO_0000073867Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei11 – 111N6-acetyllysineBy similarity

Post-translational modificationi

Phosphorylated on serine residues.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO70200.
PaxDbiO70200.
PRIDEiO70200.

PTM databases

PhosphoSiteiO70200.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiO70200.
CleanExiMM_AIF1.
ExpressionAtlasiO70200. baseline and differential.
GenevestigatoriO70200.

Interactioni

Subunit structurei

Homodimer (Potential). Monomer. Interacts with LCP1.Curated2 Publications

Protein-protein interaction databases

BioGridi198041. 2 interactions.

Structurei

Secondary structure

1
147
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi18 – 3114Combined sources
Helixi35 – 384Combined sources
Helixi43 – 5412Combined sources
Beta strandi63 – 664Combined sources
Helixi67 – 7610Combined sources
Helixi83 – 9311Combined sources
Helixi103 – 1108Combined sources
Helixi114 – 12310Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WY9X-ray2.10A1-147[»]
ProteinModelPortaliO70200.
SMRiO70200. Positions 17-127.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO70200.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini45 – 8036EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini81 – 11535EF-hand 2; degeneratePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 2 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG262998.
HOGENOMiHOG000231928.
HOVERGENiHBG004002.
InParanoidiO70200.
KOiK18617.
OMAiAFKKKYM.
OrthoDBiEOG73FQPC.
PhylomeDBiO70200.
TreeFamiTF320736.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR002048. EF_hand_dom.
[Graphical view]
PROSITEiPS50222. EF_HAND_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O70200-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQSRDLQGG KAFGLLKAQQ EERLEGINKQ FLDDPKYSND EDLPSKLEAF
60 70 80 90 100
KVKYMEFDLN GNGDIDIMSL KRMLEKLGVP KTHLELKRLI REVSSGSEET
110 120 130 140
FSYSDFLRMM LGKRSAILRM ILMYEEKNKE HKRPTGPPAK KAISELP
Length:147
Mass (Da):16,911
Last modified:August 1, 1998 - v1
Checksum:iD8974825C153D3CA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS28689.1.
RefSeqiNP_062340.1. NM_019467.2.
XP_006523566.1. XM_006523503.2.
XP_006523567.1. XM_006523504.2.
XP_006525340.1. XM_006525277.2.
XP_006525341.1. XM_006525278.2.
XP_006536565.1. XM_006536502.2.
XP_006536566.1. XM_006536503.2.
XP_006537298.1. XM_006537235.2.
XP_006537299.1. XM_006537236.2.
UniGeneiMm.10747.

Genome annotation databases

EnsembliENSMUST00000025257; ENSMUSP00000025257; ENSMUSG00000024397.
ENSMUST00000172693; ENSMUSP00000134214; ENSMUSG00000024397.
ENSMUST00000173324; ENSMUSP00000133709; ENSMUSG00000024397.
GeneIDi11629.
KEGGimmu:11629.
UCSCiuc008cgl.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS28689.1.
RefSeqiNP_062340.1. NM_019467.2.
XP_006523566.1. XM_006523503.2.
XP_006523567.1. XM_006523504.2.
XP_006525340.1. XM_006525277.2.
XP_006525341.1. XM_006525278.2.
XP_006536565.1. XM_006536502.2.
XP_006536566.1. XM_006536503.2.
XP_006537298.1. XM_006537235.2.
XP_006537299.1. XM_006537236.2.
UniGeneiMm.10747.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WY9X-ray2.10A1-147[»]
ProteinModelPortaliO70200.
SMRiO70200. Positions 17-127.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198041. 2 interactions.

PTM databases

PhosphoSiteiO70200.

Proteomic databases

MaxQBiO70200.
PaxDbiO70200.
PRIDEiO70200.

Protocols and materials databases

DNASUi11629.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025257; ENSMUSP00000025257; ENSMUSG00000024397.
ENSMUST00000172693; ENSMUSP00000134214; ENSMUSG00000024397.
ENSMUST00000173324; ENSMUSP00000133709; ENSMUSG00000024397.
GeneIDi11629.
KEGGimmu:11629.
UCSCiuc008cgl.1. mouse.

Organism-specific databases

CTDi199.
MGIiMGI:1343098. Aif1.

Phylogenomic databases

eggNOGiNOG262998.
HOGENOMiHOG000231928.
HOVERGENiHBG004002.
InParanoidiO70200.
KOiK18617.
OMAiAFKKKYM.
OrthoDBiEOG73FQPC.
PhylomeDBiO70200.
TreeFamiTF320736.

Miscellaneous databases

EvolutionaryTraceiO70200.
NextBioi279187.
PROiO70200.
SOURCEiSearch...

Gene expression databases

BgeeiO70200.
CleanExiMM_AIF1.
ExpressionAtlasiO70200. baseline and differential.
GenevestigatoriO70200.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR002048. EF_hand_dom.
[Graphical view]
PROSITEiPS50222. EF_HAND_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiAIF1_MOUSE
AccessioniPrimary (citable) accession number: O70200
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: August 1, 1998
Last modified: April 1, 2015
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.