AIF1_MOUSE
ID AIF1_MOUSE Reviewed; 147 AA.
AC O70200;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Allograft inflammatory factor 1;
DE Short=AIF-1;
DE AltName: Full=Ionized calcium-binding adapter molecule 1;
GN Name=Aif1; Synonyms=Iba1;
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 [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11722645; DOI=10.1046/j.1365-2567.2001.01301.x;
RA Watano K., Iwabuchi K., Fujii S., Ishimori N., Mitsuhashi S., Ato M.,
RA Kitabatake A., Onoe K.;
RT "Allograft inflammatory factor-1 augments productions of interleukin-6,
RT -10, -12 by a mouse macrophage line.";
RL Immunology 104:307-316(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=129/SvJ;
RA Imai Y., Ohsawa K., Kohsaka S.;
RT "Structure of the mouse iba1 gene.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=129/Sv;
RA Hu S.P., Russell M.E.;
RT "Allograft inflammatory factor-1 gene.";
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129;
RX PubMed=14656967; DOI=10.1101/gr.1736803;
RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D.,
RA Hood L.;
RT "Analysis of the gene-dense major histocompatibility complex class III
RT region and its comparison to mouse.";
RL Genome Res. 13:2621-2636(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=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 [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10934045; DOI=10.1242/jcs.113.17.3073;
RA Ohsawa K., Imai Y., Kanazawa H., Sasaki Y., Kohsaka S.;
RT "Involvement of Iba1 in membrane ruffling and phagocytosis of
RT macrophages/microglia.";
RL J. Cell Sci. 113:3073-3084(2000).
RN [8]
RP FUNCTION.
RX PubMed=11500035; DOI=10.1006/bbrc.2001.5388;
RA Sasaki Y., Ohsawa K., Kanazawa H., Kohsaka S., Imai Y.;
RT "Iba1 is an actin-cross-linking protein in macrophages/microglia.";
RL Biochem. Biophys. Res. Commun. 286:292-297(2001).
RN [9]
RP FUNCTION.
RX PubMed=11916959; DOI=10.1074/jbc.m109218200;
RA Kanazawa H., Ohsawa K., Sasaki Y., Kohsaka S., Imai Y.;
RT "Macrophage/microglia-specific protein Iba1 enhances membrane ruffling and
RT Rac activation via phospholipase C-gamma -dependent pathway.";
RL J. Biol. Chem. 277:20026-20032(2002).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH LCP1.
RX PubMed=14756805; DOI=10.1046/j.1471-4159.2003.02213.x;
RA Ohsawa K., Imai Y., Sasaki Y., Kohsaka S.;
RT "Microglia/macrophage-specific protein Iba1 binds to fimbrin and enhances
RT its actin-bundling activity.";
RL J. Neurochem. 88:844-856(2004).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Liver, Spleen, and Testis;
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 [12]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH CALCIUM IONS,
RP CALCIUM-BINDING, AND SUBUNIT.
RX PubMed=17011575; DOI=10.1016/j.jmb.2006.09.027;
RA Yamada M., Ohsawa K., Imai Y., Kohsaka S., Kamitori S.;
RT "X-ray structures of the microglia/macrophage-specific protein Iba1 from
RT human and mouse demonstrate novel molecular conformation change induced by
RT calcium binding.";
RL J. Mol. Biol. 364:449-457(2006).
CC -!- FUNCTION: Actin-binding protein that enhances membrane ruffling and RAC
CC activation. Enhances the actin-bundling activity of LCP1. Binds
CC calcium. Plays a role in RAC signaling and in phagocytosis. May play a
CC role in macrophage activation and function. Promotes the proliferation
CC of vascular smooth muscle cells and of T-lymphocytes. Enhances
CC lymphocyte migration. Plays a role in vascular inflammation.
CC {ECO:0000269|PubMed:10934045, ECO:0000269|PubMed:11500035,
CC ECO:0000269|PubMed:11722645, ECO:0000269|PubMed:11916959,
CC ECO:0000269|PubMed:14756805}.
CC -!- SUBUNIT: Homodimer (Potential). Monomer. Interacts with LCP1.
CC {ECO:0000269|PubMed:14756805, ECO:0000269|PubMed:17011575,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:10934045}. Cell projection, ruffle membrane
CC {ECO:0000269|PubMed:10934045, ECO:0000269|PubMed:14756805}; Peripheral
CC membrane protein; Cytoplasmic side. Cell projection, phagocytic cup
CC {ECO:0000269|PubMed:10934045, ECO:0000269|PubMed:14756805}.
CC Note=Associated with the actin cytoskeleton at membrane ruffles and at
CC sites of phagocytosis. {ECO:0000269|PubMed:10934045}.
CC -!- TISSUE SPECIFICITY: Abundantly expressed in the testis, moderately in
CC the spleen and lymph nodes and at low levels in the liver and thymus.
CC Detected in macrophages. {ECO:0000269|PubMed:11722645}.
CC -!- PTM: Phosphorylated on serine residues. {ECO:0000250}.
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DR EMBL; AB013745; BAA28216.1; -; mRNA.
DR EMBL; AB036423; BAB20758.1; -; Genomic_DNA.
DR EMBL; D86382; BAA86387.1; -; mRNA.
DR EMBL; AF074959; AAC25604.1; -; mRNA.
DR EMBL; U82792; AAC24189.1; -; Genomic_DNA.
DR EMBL; AK006184; BAB24445.1; -; mRNA.
DR EMBL; AK006562; BAB24654.1; -; mRNA.
DR EMBL; AF109719; AAC82481.1; -; Genomic_DNA.
DR EMBL; BC021539; AAH21539.1; -; mRNA.
DR CCDS; CCDS28689.1; -.
DR RefSeq; NP_062340.1; NM_019467.2.
DR RefSeq; XP_006523566.1; XM_006523503.3.
DR RefSeq; XP_006523567.1; XM_006523504.3.
DR PDB; 1WY9; X-ray; 2.10 A; A=1-147.
DR PDBsum; 1WY9; -.
DR AlphaFoldDB; O70200; -.
DR SMR; O70200; -.
DR BioGRID; 198041; 2.
DR STRING; 10090.ENSMUSP00000025257; -.
DR iPTMnet; O70200; -.
DR PhosphoSitePlus; O70200; -.
DR PaxDb; O70200; -.
DR PRIDE; O70200; -.
DR ProteomicsDB; 296343; -.
DR Antibodypedia; 27285; 873 antibodies from 44 providers.
DR DNASU; 11629; -.
DR Ensembl; ENSMUST00000025257; ENSMUSP00000025257; ENSMUSG00000024397.
DR Ensembl; ENSMUST00000172693; ENSMUSP00000134214; ENSMUSG00000024397.
DR Ensembl; ENSMUST00000173324; ENSMUSP00000133709; ENSMUSG00000024397.
DR GeneID; 11629; -.
DR KEGG; mmu:11629; -.
DR UCSC; uc008cgl.1; mouse.
DR CTD; 199; -.
DR MGI; MGI:1343098; Aif1.
DR VEuPathDB; HostDB:ENSMUSG00000024397; -.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00390000013846; -.
DR HOGENOM; CLU_134149_0_0_1; -.
DR InParanoid; O70200; -.
DR OMA; NKYMEFD; -.
DR OrthoDB; 1557466at2759; -.
DR PhylomeDB; O70200; -.
DR TreeFam; TF320736; -.
DR BioGRID-ORCS; 11629; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Aif1; mouse.
DR EvolutionaryTrace; O70200; -.
DR PRO; PR:O70200; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; O70200; protein.
DR Bgee; ENSMUSG00000024397; Expressed in seminiferous tubule of testis and 133 other tissues.
DR ExpressionAtlas; O70200; baseline and differential.
DR Genevisible; O70200; MM.
DR GO; GO:0005884; C:actin filament; IDA:MGI.
DR GO; GO:0042995; C:cell projection; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0097386; C:glial cell projection; IDA:MGI.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0043204; C:perikaryon; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0001891; C:phagocytic cup; IDA:UniProtKB.
DR GO; GO:0001726; C:ruffle; IDA:MGI.
DR GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IMP:ARUK-UCL.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0051764; P:actin crosslink formation; IMP:ARUK-UCL.
DR GO; GO:0051017; P:actin filament bundle assembly; IDA:MGI.
DR GO; GO:0030041; P:actin filament polymerization; ISS:UniProtKB.
DR GO; GO:0071346; P:cellular response to interferon-gamma; ISS:UniProtKB.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISO:MGI.
DR GO; GO:0006954; P:inflammatory response; ISS:UniProtKB.
DR GO; GO:0001774; P:microglial cell activation; NAS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0071672; P:negative regulation of smooth muscle cell chemotaxis; ISO:MGI.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0030046; P:parallel actin filament bundle assembly; IDA:ARUK-UCL.
DR GO; GO:0006911; P:phagocytosis, engulfment; IMP:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0032722; P:positive regulation of chemokine production; ISO:MGI.
DR GO; GO:0050921; P:positive regulation of chemotaxis; ISO:MGI.
DR GO; GO:0090271; P:positive regulation of fibroblast growth factor production; ISO:MGI.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; ISO:MGI.
DR GO; GO:0090026; P:positive regulation of monocyte chemotaxis; ISS:UniProtKB.
DR GO; GO:0071677; P:positive regulation of mononuclear cell migration; ISO:MGI.
DR GO; GO:0014739; P:positive regulation of muscle hyperplasia; ISO:MGI.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0071673; P:positive regulation of smooth muscle cell chemotaxis; ISS:UniProtKB.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISS:UniProtKB.
DR GO; GO:2000406; P:positive regulation of T cell migration; ISS:UniProtKB.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; ISS:UniProtKB.
DR GO; GO:0016601; P:Rac protein signal transduction; IMP:UniProtKB.
DR GO; GO:0097178; P:ruffle assembly; IMP:UniProtKB.
DR DisProt; DP02956; -.
DR InterPro; IPR042433; AIF1/AIF1L.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR PANTHER; PTHR10356; PTHR10356; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Calcium; Cell membrane;
KW Cell projection; Cytoplasm; Cytoskeleton; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P81076"
FT CHAIN 2..147
FT /note="Allograft inflammatory factor 1"
FT /id="PRO_0000073867"
FT DOMAIN 45..80
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 81..115
FT /note="EF-hand 2; degenerate"
FT /evidence="ECO:0000305"
FT REGION 128..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 58
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 60
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 62
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 98
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 100
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 105
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P81076"
FT MOD_RES 11
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P55008"
FT HELIX 18..31
FT /evidence="ECO:0007829|PDB:1WY9"
FT HELIX 35..38
FT /evidence="ECO:0007829|PDB:1WY9"
FT HELIX 43..54
FT /evidence="ECO:0007829|PDB:1WY9"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:1WY9"
FT HELIX 67..76
FT /evidence="ECO:0007829|PDB:1WY9"
FT HELIX 83..93
FT /evidence="ECO:0007829|PDB:1WY9"
FT HELIX 103..110
FT /evidence="ECO:0007829|PDB:1WY9"
FT HELIX 114..123
FT /evidence="ECO:0007829|PDB:1WY9"
SQ SEQUENCE 147 AA; 16911 MW; D8974825C153D3CA CRC64;
MSQSRDLQGG KAFGLLKAQQ EERLEGINKQ FLDDPKYSND EDLPSKLEAF KVKYMEFDLN
GNGDIDIMSL KRMLEKLGVP KTHLELKRLI REVSSGSEET FSYSDFLRMM LGKRSAILRM
ILMYEEKNKE HKRPTGPPAK KAISELP
