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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.
11-DEC-2019, entry version 144.
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; DOI=10.1046/j.1471-4159.2003.02213.x;
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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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.
PDB; 1WY9; X-ray; 2.10 A; A=1-147.
PDBsum; 1WY9; -.
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; -.
InParanoid; O70200; -.
KO; K18617; -.
OMA; DDPKYST; -.
OrthoDB; 1557466at2759; -.
PhylomeDB; O70200; -.
TreeFam; TF320736; -.
ChiTaRS; Aif1; mouse.
EvolutionaryTrace; O70200; -.
PRO; PR:O70200; -.
Proteomes; UP000000589; Chromosome 17.
RNAct; O70200; protein.
Bgee; ENSMUSG00000024397; Expressed in 150 organ(s), highest expression level in testis.
ExpressionAtlas; O70200; baseline and differential.
Genevisible; O70200; MM.
GO; GO:0005884; C:actin filament; IDA:MGI.
GO; GO:0042995; C:cell projection; ISO: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; ISO:MGI.
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; IMP:ARUK-UCL.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0051764; P:actin crosslink formation; IMP:ARUK-UCL.
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:0034599; P:cellular response to oxidative stress; ISO:MGI.
GO; GO:0021549; P:cerebellum development; 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; ISO:MGI.
GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
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:0030046; P:parallel actin filament bundle assembly; IDA:ARUK-UCL.
GO; GO:0006911; P:phagocytosis, engulfment; IMP:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
GO; GO:0090197; P:positive regulation of chemokine secretion; ISO:MGI.
GO; GO:0050921; P:positive regulation of chemotaxis; ISO:MGI.
GO; GO:0090271; P:positive regulation of fibroblast growth factor production; ISO:MGI.
GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISS:UniProtKB.
GO; GO:2000778; P:positive regulation of interleukin-6 secretion; ISO:MGI.
GO; GO:0090026; P:positive regulation of monocyte chemotaxis; ISS:UniProtKB.
GO; GO:0071677; P:positive regulation of mononuclear cell migration; ISO:MGI.
GO; GO:0014739; P:positive regulation of muscle hyperplasia; ISO:MGI.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISO:MGI.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
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; IPR042433; AIF1/AIF1L.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR002048; EF_hand_dom.
PANTHER; PTHR10356; PTHR10356; 1.
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; Cytoplasm; Cytoskeleton; Membrane; Metal-binding;
Phosphoprotein; Reference proteome; Repeat.
INIT_MET 1
/note="Removed"
/evidence="ECO:0000250|UniProtKB:P81076"
CHAIN 2..147
/note="Allograft inflammatory factor 1"
/id="PRO_0000073867"
DOMAIN 45..80
/note="EF-hand 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
DOMAIN 81..115
/note="EF-hand 2; degenerate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
CA_BIND 58..69
/note="1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
CA_BIND 94..105
/note="2"
MOD_RES 2
/note="N-acetylserine"
/evidence="ECO:0000250|UniProtKB:P81076"
MOD_RES 11
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P55008"
HELIX 18..31
/evidence="ECO:0000244|PDB:1WY9"
HELIX 35..38
/evidence="ECO:0000244|PDB:1WY9"
HELIX 43..54
/evidence="ECO:0000244|PDB:1WY9"
STRAND 63..66
/evidence="ECO:0000244|PDB:1WY9"
HELIX 67..76
/evidence="ECO:0000244|PDB:1WY9"
HELIX 83..93
/evidence="ECO:0000244|PDB:1WY9"
HELIX 103..110
/evidence="ECO:0000244|PDB:1WY9"
HELIX 114..123
/evidence="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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[Ticam2 Tirp Tram] TIR domain-containing adapter molecule 2 (TICAM-2) (TRIF-related adapter molecule) (Toll/interleukin-1 receptor domain-containing protein)
[S100A9 CAGB CFAG MRP14] Protein S100-A9 (Calgranulin-B) (Calprotectin L1H subunit) (Leukocyte L1 complex heavy chain) (Migration inhibitory factor-related protein 14) (MRP-14) (p14) (S100 calcium-binding protein A9)
[S100A8 CAGA CFAG MRP8] Protein S100-A8 (Calgranulin-A) (Calprotectin L1L subunit) (Cystic fibrosis antigen) (CFAG) (Leukocyte L1 complex light chain) (Migration inhibitory factor-related protein 8) (MRP-8) (p8) (S100 calcium-binding protein A8) (Urinary stone protein band A)
[PTN HBNF1 NEGF1] Pleiotrophin (PTN) (Heparin-binding brain mitogen) (HBBM) (Heparin-binding growth factor 8) (HBGF-8) (Heparin-binding growth-associated molecule) (HB-GAM) (Heparin-binding neurite outgrowth-promoting factor) (HBNF) (Heparin-binding neurite outgrowth-promoting factor 1) (HBNF-1) (Osteoblast-specific factor 1) (OSF-1)
[S100a9 Cagb Mrp14] Protein S100-A9 (Calgranulin-B) (Leukocyte L1 complex heavy chain) (Migration inhibitory factor-related protein 14) (MRP-14) (p14) (S100 calcium-binding protein A9)
[Oprm1 Mor Oprm] Mu-type opioid receptor (M-OR-1) (MOR-1)
[Ptn] Pleiotrophin (PTN) (Heparin-binding brain mitogen) (HBBM) (Heparin-binding growth factor 8) (HBGF-8) (Heparin-binding growth-associated molecule) (HB-GAM) (Heparin-binding neutrophic factor) (HBNF) (Osteoblast-specific factor 1) (OSF-1)
[Ptn] Pleiotrophin (PTN) (Heparin-binding brain mitogen) (HBBM) (Heparin-binding growth factor 8) (HBGF-8) (Heparin-binding growth-associated molecule) (HB-GAM) (Heparin-binding neutrophic factor) (HBNF) (Osteoblast-specific factor 1) (OSF-1)
[CASR GPRC2A PCAR1] Extracellular calcium-sensing receptor (CaR) (CaSR) (hCasR) (Parathyroid cell calcium-sensing receptor 1) (PCaR1)
[CAM1 TEF3 YPL048W] Elongation factor 1-gamma 1 (EF-1-gamma 1) (Calcium and membrane-binding protein 1) (Calcium phospholipid-binding protein) (CPBP) (Eukaryotic elongation factor 1Bgamma 1) (eEF1Bgamma 1) (Translation elongation factor 1B gamma 1)
[CCL3 G0S19-1 MIP1A SCYA3] C-C motif chemokine 3 (G0/G1 switch regulatory protein 19-1) (Macrophage inflammatory protein 1-alpha) (MIP-1-alpha) (PAT 464.1) (SIS-beta) (Small-inducible cytokine A3) (Tonsillar lymphocyte LD78 alpha protein) [Cleaved into: MIP-1-alpha(4-69) (LD78-alpha(4-69))]
[Ceacam1 Bgp Bgp1] Carcinoembryonic antigen-related cell adhesion molecule 1 (Biliary glycoprotein 1) (BGP-1) (Biliary glycoprotein D) (MHVR1) (Murine hepatitis virus receptor) (MHV-R) (CD antigen CD66a)
[MAPK14 CSBP CSBP1 CSBP2 CSPB1 MXI2 SAPK2A] Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (Cytokine suppressive anti-inflammatory drug-binding protein) (CSAID-binding protein) (CSBP) (MAP kinase MXI2) (MAX-interacting protein 2) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha) (Stress-activated protein kinase 2a) (SAPK2a)
[LIME1 LIME LP8067] Lck-interacting transmembrane adapter 1 (Lck-interacting membrane protein) (Lck-interacting molecule)
[CSF1R FMS] Macrophage colony-stimulating factor 1 receptor (CSF-1 receptor) (CSF-1-R) (CSF-1R) (M-CSF-R) (EC 2.7.10.1) (Proto-oncogene c-Fms) (CD antigen CD115)
[Lime1 Lime] Lck-interacting transmembrane adapter 1 (Lck-interacting molecule)
[CCL4 LAG1 MIP1B SCYA4] C-C motif chemokine 4 (G-26 T-lymphocyte-secreted protein) (HC21) (Lymphocyte activation gene 1 protein) (LAG-1) (MIP-1-beta(1-69)) (Macrophage inflammatory protein 1-beta) (MIP-1-beta) (PAT 744) (Protein H400) (SIS-gamma) (Small-inducible cytokine A4) (T-cell activation protein 2) (ACT-2) [Cleaved into: MIP-1-beta(3-69)]
[Egfr] Epidermal growth factor receptor (EC 2.7.10.1)
[CCL20 LARC MIP3A SCYA20] C-C motif chemokine 20 (Beta-chemokine exodus-1) (CC chemokine LARC) (Liver and activation-regulated chemokine) (Macrophage inflammatory protein 3 alpha) (MIP-3-alpha) (Small-inducible cytokine A20) [Cleaved into: CCL20(1-67); CCL20(1-64); CCL20(2-70)]
[STAM STAM1] Signal transducing adapter molecule 1 (STAM-1)
[TRAT1 TCRIM HSPC062] T-cell receptor-associated transmembrane adapter 1 (T-cell receptor-interacting molecule) (TRIM) (pp29/30)
[BCL10 CIPER CLAP] B-cell lymphoma/leukemia 10 (B-cell CLL/lymphoma 10) (Bcl-10) (CARD-containing molecule enhancing NF-kappa-B) (CARD-like apoptotic protein) (hCLAP) (CED-3/ICH-1 prodomain homologous E10-like regulator) (CIPER) (Cellular homolog of vCARMEN) (cCARMEN) (Cellular-E10) (c-E10) (Mammalian CARD-containing adapter molecule E10) (mE10)
[RASGRP1 RASGRP] RAS guanyl-releasing protein 1 (Calcium and DAG-regulated guanine nucleotide exchange factor II) (CalDAG-GEFII) (Ras guanyl-releasing protein)

Bibliography :
[29232670] Some Galeomorph Sharks Express a Mammalian Microglia-Specific Protein in Radial Ependymoglia of the Telencephalon.
[28812528] Acute Leukemia in Horses.
[25569805] Loss of Allograft Inflammatory Factor-1 Ameliorates Experimental Autoimmune Encephalomyelitis by Limiting Encephalitogenic CD4 T-Cell Expansion.
[24723370] Microglia of medicinal leech (Hirudo medicinalis) express a specific activation marker homologous to vertebrate ionized calcium-binding adapter molecule 1 (Iba1/alias aif-1).
[17874251] Allograft inflammatory factor-1/Ionized calcium-binding adapter molecule 1 is specifically expressed by most subpopulations of macrophages and spermatids in testis.