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Allograft inflammatory factor 1 (AIF-1) (Ionized calcium-binding adapter molecule 1)

 AIF1_MOUSE              Reviewed;         147 AA.
O70200;
26-APR-2005, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 1.
10-MAY-2017, entry version 134.
RecName: Full=Allograft inflammatory factor 1;
Short=AIF-1;
AltName: Full=Ionized calcium-binding adapter molecule 1;
Name=Aif1; Synonyms=Iba1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
PubMed=11722645; DOI=10.1046/j.1365-2567.2001.01301.x;
Watano K., Iwabuchi K., Fujii S., Ishimori N., Mitsuhashi S., Ato M.,
Kitabatake A., Onoe K.;
"Allograft inflammatory factor-1 augments productions of interleukin-
6, -10, -12 by a mouse macrophage line.";
Immunology 104:307-316(2001).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
STRAIN=129/SvJ;
Imai Y., Ohsawa K., Kohsaka S.;
"Structure of the mouse iba1 gene.";
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
STRAIN=129/Sv;
Hu S.P., Russell M.E.;
"Allograft inflammatory factor-1 gene.";
Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=129;
PubMed=14656967; DOI=10.1101/gr.1736803;
Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S.,
Campbell R.D., Hood L.;
"Analysis of the gene-dense major histocompatibility complex class III
region and its comparison to mouse.";
Genome Res. 13:2621-2636(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=10934045;
Ohsawa K., Imai Y., Kanazawa H., Sasaki Y., Kohsaka S.;
"Involvement of Iba1 in membrane ruffling and phagocytosis of
macrophages/microglia.";
J. Cell Sci. 113:3073-3084(2000).
[8]
FUNCTION.
PubMed=11500035; DOI=10.1006/bbrc.2001.5388;
Sasaki Y., Ohsawa K., Kanazawa H., Kohsaka S., Imai Y.;
"Iba1 is an actin-cross-linking protein in macrophages/microglia.";
Biochem. Biophys. Res. Commun. 286:292-297(2001).
[9]
FUNCTION.
PubMed=11916959; DOI=10.1074/jbc.M109218200;
Kanazawa H., Ohsawa K., Sasaki Y., Kohsaka S., Imai Y.;
"Macrophage/microglia-specific protein Iba1 enhances membrane ruffling
and Rac activation via phospholipase C-gamma -dependent pathway.";
J. Biol. Chem. 277:20026-20032(2002).
[10]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH LCP1.
PubMed=14756805;
Ohsawa K., Imai Y., Sasaki Y., Kohsaka S.;
"Microglia/macrophage-specific protein Iba1 binds to fimbrin and
enhances its actin-bundling activity.";
J. Neurochem. 88:844-856(2004).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Liver, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[12]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH CALCIUM IONS,
CALCIUM-BINDING, AND SUBUNIT.
PubMed=17011575; DOI=10.1016/j.jmb.2006.09.027;
Yamada M., Ohsawa K., Imai Y., Kohsaka S., Kamitori S.;
"X-ray structures of the microglia/macrophage-specific protein Iba1
from human and mouse demonstrate novel molecular conformation change
induced by calcium binding.";
J. Mol. Biol. 364:449-457(2006).
-!- 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. {ECO:0000269|PubMed:10934045,
ECO:0000269|PubMed:11500035, ECO:0000269|PubMed:11722645,
ECO:0000269|PubMed:11916959, ECO:0000269|PubMed:14756805}.
-!- SUBUNIT: Homodimer (Potential). Monomer. Interacts with LCP1.
{ECO:0000269|PubMed:14756805, ECO:0000269|PubMed:17011575,
ECO:0000305}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:10934045}. Cell projection, ruffle membrane
{ECO:0000269|PubMed:10934045, ECO:0000269|PubMed:14756805};
Peripheral membrane protein; Cytoplasmic side. Cell projection,
phagocytic cup {ECO:0000269|PubMed:10934045,
ECO:0000269|PubMed:14756805}. Note=Associated with the actin
cytoskeleton at membrane ruffles and at sites of phagocytosis.
{ECO:0000269|PubMed:10934045}.
-!- 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. {ECO:0000269|PubMed:11722645}.
-!- PTM: Phosphorylated on serine residues. {ECO:0000250}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB013745; BAA28216.1; -; mRNA.
EMBL; AB036423; BAB20758.1; -; Genomic_DNA.
EMBL; D86382; BAA86387.1; -; mRNA.
EMBL; AF074959; AAC25604.1; -; mRNA.
EMBL; U82792; AAC24189.1; -; Genomic_DNA.
EMBL; AK006184; BAB24445.1; -; mRNA.
EMBL; AK006562; BAB24654.1; -; mRNA.
EMBL; AF109719; AAC82481.1; -; Genomic_DNA.
EMBL; BC021539; AAH21539.1; -; mRNA.
CCDS; CCDS28689.1; -.
RefSeq; NP_062340.1; NM_019467.2.
RefSeq; XP_006523566.1; XM_006523503.3.
RefSeq; XP_006523567.1; XM_006523504.3.
UniGene; Mm.10747; -.
PDB; 1WY9; X-ray; 2.10 A; A=1-147.
PDBsum; 1WY9; -.
ProteinModelPortal; O70200; -.
SMR; O70200; -.
BioGrid; 198041; 2.
STRING; 10090.ENSMUSP00000025257; -.
iPTMnet; O70200; -.
PhosphoSitePlus; O70200; -.
PaxDb; O70200; -.
PRIDE; O70200; -.
DNASU; 11629; -.
Ensembl; ENSMUST00000025257; ENSMUSP00000025257; ENSMUSG00000024397.
Ensembl; ENSMUST00000172693; ENSMUSP00000134214; ENSMUSG00000024397.
Ensembl; ENSMUST00000173324; ENSMUSP00000133709; ENSMUSG00000024397.
GeneID; 11629; -.
KEGG; mmu:11629; -.
UCSC; uc008cgl.1; mouse.
CTD; 199; -.
MGI; MGI:1343098; Aif1.
eggNOG; ENOG410KCUI; Eukaryota.
eggNOG; ENOG411206J; LUCA.
GeneTree; ENSGT00390000013846; -.
HOGENOM; HOG000231928; -.
HOVERGEN; HBG004002; -.
InParanoid; O70200; -.
KO; K18617; -.
OMA; AFKKKYM; -.
OrthoDB; EOG091G0ZI9; -.
PhylomeDB; O70200; -.
TreeFam; TF320736; -.
EvolutionaryTrace; O70200; -.
PRO; PR:O70200; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000024397; -.
CleanEx; MM_AIF1; -.
ExpressionAtlas; O70200; baseline and differential.
Genevisible; O70200; MM.
GO; GO:0005884; C:actin filament; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043204; C:perikaryon; IEA:Ensembl.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0001891; C:phagocytic cup; IDA:UniProtKB.
GO; GO:0001726; C:ruffle; IDA:MGI.
GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0051017; P:actin filament bundle assembly; IDA:MGI.
GO; GO:0030041; P:actin filament polymerization; ISS:UniProtKB.
GO; GO:0031668; P:cellular response to extracellular stimulus; IEA:Ensembl.
GO; GO:0032870; P:cellular response to hormone stimulus; IEA:Ensembl.
GO; GO:0071447; P:cellular response to hydroperoxide; IEA:Ensembl.
GO; GO:0071346; P:cellular response to interferon-gamma; ISS:UniProtKB.
GO; GO:0071315; P:cellular response to morphine; IEA:Ensembl.
GO; GO:0006954; P:inflammatory response; ISS:UniProtKB.
GO; GO:0001774; P:microglial cell activation; NAS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
GO; GO:0071672; P:negative regulation of smooth muscle cell chemotaxis; ISO:MGI.
GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; ISO:MGI.
GO; GO:0006911; P:phagocytosis, engulfment; IMP:UniProtKB.
GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISS:UniProtKB.
GO; GO:0090026; P:positive regulation of monocyte chemotaxis; ISS:UniProtKB.
GO; GO:0014739; P:positive regulation of muscle hyperplasia; IEA:Ensembl.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IEA:Ensembl.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl.
GO; GO:0071673; P:positive regulation of smooth muscle cell chemotaxis; ISS:UniProtKB.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISS:UniProtKB.
GO; GO:2000406; P:positive regulation of T cell migration; ISS:UniProtKB.
GO; GO:0042102; P:positive regulation of T cell proliferation; ISS:UniProtKB.
GO; GO:0016601; P:Rac protein signal transduction; IMP:UniProtKB.
GO; GO:0048678; P:response to axon injury; IEA:Ensembl.
GO; GO:0051602; P:response to electrical stimulus; IEA:Ensembl.
GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
GO; GO:0097178; P:ruffle assembly; IMP:UniProtKB.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR002048; EF_hand_dom.
SUPFAM; SSF47473; SSF47473; 1.
PROSITE; PS50222; EF_HAND_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Actin-binding; Calcium; Cell membrane;
Cell projection; Complete proteome; Cytoplasm; Cytoskeleton; Membrane;
Metal-binding; Phosphoprotein; Reference proteome; Repeat.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P81076}.
CHAIN 2 147 Allograft inflammatory factor 1.
/FTId=PRO_0000073867.
DOMAIN 45 80 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 81 115 EF-hand 2; degenerate.
{ECO:0000255|PROSITE-ProRule:PRU00448}.
CA_BIND 58 69 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 94 105 2.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:P81076}.
MOD_RES 11 11 N6-acetyllysine.
{ECO:0000250|UniProtKB:P55008}.
HELIX 18 31 {ECO:0000244|PDB:1WY9}.
HELIX 35 38 {ECO:0000244|PDB:1WY9}.
HELIX 43 54 {ECO:0000244|PDB:1WY9}.
STRAND 63 66 {ECO:0000244|PDB:1WY9}.
HELIX 67 76 {ECO:0000244|PDB:1WY9}.
HELIX 83 93 {ECO:0000244|PDB:1WY9}.
HELIX 103 110 {ECO:0000244|PDB:1WY9}.
HELIX 114 123 {ECO:0000244|PDB:1WY9}.
SEQUENCE 147 AA; 16911 MW; D8974825C153D3CA CRC64;
MSQSRDLQGG KAFGLLKAQQ EERLEGINKQ FLDDPKYSND EDLPSKLEAF KVKYMEFDLN
GNGDIDIMSL KRMLEKLGVP KTHLELKRLI REVSSGSEET FSYSDFLRMM LGKRSAILRM
ILMYEEKNKE HKRPTGPPAK KAISELP


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