Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O70200

- AIF1_MOUSE

UniProt

O70200 - AIF1_MOUSE

Protein

Allograft inflammatory factor 1

Gene

Aif1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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
    3. protein binding Source: MGI

    GO - Biological processi

    1. actin filament bundle assembly Source: UniProtKB
    2. actin filament polymerization Source: UniProtKB
    3. cellular response to interferon-gamma Source: UniProtKB
    4. inflammatory response Source: UniProtKB
    5. microglial cell activation Source: UniProtKB
    6. negative regulation of smooth muscle cell chemotaxis Source: Ensembl
    7. negative regulation of smooth muscle cell proliferation Source: Ensembl
    8. phagocytosis, engulfment Source: UniProtKB
    9. positive regulation of G1/S transition of mitotic cell cycle Source: UniProtKB
    10. positive regulation of monocyte chemotaxis Source: UniProtKB
    11. positive regulation of smooth muscle cell chemotaxis Source: UniProtKB
    12. positive regulation of smooth muscle cell proliferation Source: UniProtKB
    13. positive regulation of T cell migration Source: UniProtKB
    14. positive regulation of T cell proliferation Source: UniProtKB
    15. Rac protein signal transduction Source: UniProtKB
    16. ruffle assembly Source: UniProtKB

    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: Chromosome 17

    Organism-specific databases

    MGIiMGI:1343098. Aif1.

    Subcellular locationi

    Cytoplasmcytoskeleton. Cell projectionruffle membrane; Peripheral membrane protein; Cytoplasmic side
    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. perinuclear region of cytoplasm Source: Ensembl
    7. phagocytic cup Source: UniProtKB
    8. ruffle Source: MGI
    9. ruffle membrane Source: UniProtKB

    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

    ArrayExpressiO70200.
    BgeeiO70200.
    CleanExiMM_AIF1.
    GenevestigatoriO70200.

    Interactioni

    Subunit structurei

    Homodimer Potential. Monomer. Interacts with LCP1.2 PublicationsCurated

    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 – 3114
    Helixi35 – 384
    Helixi43 – 5412
    Beta strandi63 – 664
    Helixi67 – 7610
    Helixi83 – 9311
    Helixi103 – 1108
    Helixi114 – 12310

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    OMAiDIDIMEL.
    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

    MSQSRDLQGG KAFGLLKAQQ EERLEGINKQ FLDDPKYSND EDLPSKLEAF    50
    KVKYMEFDLN GNGDIDIMSL KRMLEKLGVP KTHLELKRLI REVSSGSEET 100
    FSYSDFLRMM LGKRSAILRM ILMYEEKNKE HKRPTGPPAK KAISELP 147
    Length:147
    Mass (Da):16,911
    Last modified:August 1, 1998 - v1
    Checksum:iD8974825C153D3CA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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_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.
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS28689.1.
    RefSeqi NP_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.
    UniGenei Mm.10747.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WY9 X-ray 2.10 A 1-147 [» ]
    ProteinModelPortali O70200.
    SMRi O70200. Positions 17-127.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198041. 2 interactions.

    PTM databases

    PhosphoSitei O70200.

    Proteomic databases

    MaxQBi O70200.
    PaxDbi O70200.
    PRIDEi O70200.

    Protocols and materials databases

    DNASUi 11629.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000025257 ; ENSMUSP00000025257 ; ENSMUSG00000024397 .
    ENSMUST00000172693 ; ENSMUSP00000134214 ; ENSMUSG00000024397 .
    ENSMUST00000173324 ; ENSMUSP00000133709 ; ENSMUSG00000024397 .
    GeneIDi 11629.
    KEGGi mmu:11629.
    UCSCi uc008cgl.1. mouse.

    Organism-specific databases

    CTDi 199.
    MGIi MGI:1343098. Aif1.

    Phylogenomic databases

    eggNOGi NOG262998.
    HOGENOMi HOG000231928.
    HOVERGENi HBG004002.
    InParanoidi O70200.
    OMAi DIDIMEL.
    OrthoDBi EOG73FQPC.
    PhylomeDBi O70200.
    TreeFami TF320736.

    Miscellaneous databases

    EvolutionaryTracei O70200.
    NextBioi 279187.
    PROi O70200.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O70200.
    Bgeei O70200.
    CleanExi MM_AIF1.
    Genevestigatori O70200.

    Family and domain databases

    Gene3Di 1.10.238.10. 1 hit.
    InterProi IPR011992. EF-hand-dom_pair.
    IPR002048. EF_hand_dom.
    [Graphical view ]
    PROSITEi PS50222. EF_HAND_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 112 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