ID AIF1_HUMAN Reviewed; 147 AA. AC P55008; A8K406; O43904; Q9UIV4; Q9UKS9; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 04-NOV-2026, entry version 203. DE RecName: Full=Allograft inflammatory factor 1; DE Short=AIF-1; DE AltName: Full=Ionized calcium-binding adapter molecule 1; DE AltName: Full=Protein G1; GN Name=AIF1; Synonyms=G1, IBA1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS 1; 2 RP AND 3). RX PubMed=8081366; DOI=10.1093/hmg/3.5.793; RA Albertella M.R., Campbell D.R.; RT "Characterization of a novel gene in the human major histocompatibility RT complex that encodes a potential new member of the I kappa B family of RT proteins."; RL Hum. Mol. Genet. 3:793-799(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2 AND 3). RX PubMed=7590964; DOI=10.1007/bf00179392; RA Holzinger I., de Baey A., Messer G., Kick G., Zwierzina H., Weiss E.H.; RT "Cloning and genomic characterization of LST1: a new gene in the human TNF RT region."; RL Immunogenetics 42:315-322(1995). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Lymphocyte; RX PubMed=8912632; DOI=10.1006/bbrc.1996.1612; RA Autieri M.V.; RT "cDNA cloning of human allograft inflammatory factor-1: tissue RT distribution, cytokine induction, and mRNA expression in injured rat RT carotid arteries."; RL Biochem. Biophys. Res. Commun. 228:29-37(1996). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=8629302; DOI=10.1097/00007890-199605150-00018; RA Utans U., Quist W.C., McManus B.M., Wilson J.E., Arceci R.J., Wallace A.F., RA Russell M.E.; RT "Allograft inflammatory factory-1. A cytokine-responsive macrophage RT molecule expressed in transplanted human hearts."; RL Transplantation 61:1387-1392(1996). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2 AND 3), AND ALTERNATIVE RP SPLICING. RX PubMed=9367684; DOI=10.1006/geno.1997.4963; RA de Baey A., Fellerhoff B., Maier S., Martinozzi S., Weidle U., Weiss E.H.; RT "Complex expression pattern of the TNF region gene LST1 through RT differential regulation, initiation, and alternative splicing."; RL Genomics 45:591-600(1997). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2 AND 3). RX PubMed=10202016; RA Neville M.J., Campbell R.D.; RT "A new member of the Ig superfamily and a V-ATPase G subunit are among the RT predicted products of novel genes close to the TNF locus in the human RT MHC."; RL J. Immunol. 162:4745-4754(1999). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). RA Imai Y., Ohsawa K., Kohsaka S.; RT "Novel calcium binding protein, Iba1 (ionized calcium binding adapter RT molecule 1), which is phosphorylated on serine."; RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Glial tumor; RA Deininger M.H., Trautmann K.; RT "Upregulation of Allograft inflammatory factor (AIF) is induced by Ab- RT stimulation in vitro and in human Alzheimer's disease brain."; RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RA Del Galdo F., Artlett C., Jimenez S.A.; RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-14. RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [12] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-14. 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 [13] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Shiina S., Tamiya G., Oka A., Inoko H.; RT "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region."; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. RN [14] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [15] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [16] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Prostate; 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 [17] RP FUNCTION. RX PubMed=15117732; DOI=10.1161/01.atv.0000130024.50058.de; RA Chen X., Kelemen S.E., Autieri M.V.; RT "AIF-1 expression modulates proliferation of human vascular smooth muscle RT cells by autocrine expression of G-CSF."; RL Arterioscler. Thromb. Vasc. Biol. 24:1217-1222(2004). RN [18] RP FUNCTION, INTERACTION WITH ACTIN, AND TISSUE SPECIFICITY. RX PubMed=16049345; DOI=10.1016/s0002-9440(10)63003-9; RA Kelemen S.E., Autieri M.V.; RT "Expression of allograft inflammatory factor-1 in T lymphocytes: a role in RT T-lymphocyte activation and proliferative arteriopathies."; RL Am. J. Pathol. 167:619-626(2005). RN [19] RP FUNCTION, AND SUBUNIT. RX PubMed=18699778; DOI=10.1111/j.1742-4658.2008.06605.x; RA Schulze J.O., Quedenau C., Roske Y., Adam T., Schueler H., Behlke J., RA Turnbull A.P., Sievert V., Scheich C., Mueller U., Heinemann U., RA Buessow K.; RT "Structural and functional characterization of human Iba proteins."; RL FEBS J. 275:4627-4640(2008). RN [20] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-11, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [23] RP X-RAY CRYSTALLOGRAPHY OF APOPROTEIN. 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). RN [24] RP STRUCTURE BY NMR OF 2-147. RG Center for eukaryotic structural genomics (CESG); RT "NMR structure of the human allograft inflammatory factor 1."; RL Submitted (FEB-2009) to the PDB data bank. 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:15117732, ECO:0000269|PubMed:16049345, CC ECO:0000269|PubMed:18699778}. CC -!- SUBUNIT: Homodimer (Potential). Monomer. Interacts with LCP1. CC {ECO:0000269|PubMed:16049345, ECO:0000269|PubMed:18699778, CC ECO:0000305}. CC -!- INTERACTION: CC P55008; P22607: FGFR3; NbExp=3; IntAct=EBI-9031341, EBI-348399; CC P55008; P06396: GSN; NbExp=3; IntAct=EBI-9031341, EBI-351506; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000250|UniProtKB:O70200}. Cell projection, ruffle membrane CC {ECO:0000250|UniProtKB:O70200}; Peripheral membrane protein CC {ECO:0000250|UniProtKB:O70200}; Cytoplasmic side CC {ECO:0000250|UniProtKB:O70200}. Cell projection, phagocytic cup CC {ECO:0000250|UniProtKB:O70200}. Note=Associated with the actin CC cytoskeleton at membrane ruffles and at sites of phagocytosis. CC {ECO:0000250|UniProtKB:O70200}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P55008-1; Sequence=Displayed; CC Name=2; Synonyms=G1; CC IsoId=P55008-2; Sequence=VSP_043838; CC Name=3; CC IsoId=P55008-3; Sequence=VSP_043837, VSP_043839; CC -!- TISSUE SPECIFICITY: Detected in T-lymphocytes and peripheral blood CC mononuclear cells. {ECO:0000269|PubMed:16049345}. CC -!- PTM: Phosphorylated on serine residues. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U49392; AAA92457.1; -; mRNA. DR EMBL; U95213; AAC24422.1; -; mRNA. DR EMBL; U19713; AAB05003.1; -; mRNA. DR EMBL; Y14768; CAA75060.1; -; Genomic_DNA. DR EMBL; Y14768; CAA75061.1; -; Genomic_DNA. DR EMBL; Y14768; CAA75062.1; -; Genomic_DNA. DR EMBL; D86438; BAA13088.1; -; mRNA. DR EMBL; AF299327; AAG39110.1; -; mRNA. DR EMBL; EF070982; ABK35646.1; -; mRNA. DR EMBL; AK290771; BAF83460.1; -; mRNA. DR EMBL; CR542153; CAG46950.1; -; mRNA. DR EMBL; AF129756; AAD18087.1; -; Genomic_DNA. DR EMBL; BA000025; BAB63392.1; -; Genomic_DNA. DR EMBL; AL662801; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL662847; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL805934; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX248305; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR753892; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR759761; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471081; EAX03442.1; -; Genomic_DNA. DR EMBL; CH471081; EAX03446.1; -; Genomic_DNA. DR EMBL; BC009474; AAH09474.1; -; mRNA. DR CCDS; CCDS34398.1; -. [P55008-2] DR CCDS; CCDS4706.1; -. [P55008-1] DR PIR; JC5246; JC5246. DR RefSeq; NP_001305899.1; NM_001318970.2. [P55008-2] DR RefSeq; NP_001614.3; NM_001623.5. [P55008-1] DR RefSeq; NP_116573.1; NM_032955.3. [P55008-2] DR PDB; 2D58; X-ray; 1.90 A; A=17-123. DR PDB; 2G2B; NMR; -; A=2-147. DR AlphaFoldDB; P55008; -. DR BMRB; P55008; -. DR MDposit; P55008; -. DR SMR; P55008; -. DR BioGRID; 106702; 11. DR FunCoup; P55008; 73. DR IntAct; P55008; 13. DR NDEx; IQUERY-CP-AIF1; 3 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000365227; -. DR iPTMnet; P55008; -. DR PhosphoSitePlus; P55008; -. DR BioMuta; AIF1; -. DR DMDM; 1703217; -. DR jPOST; P55008; -. DR MassIVE; P55008; -. DR PaxDb; 9606-ENSP00000365227; -. DR PeptideAtlas; P55008; -. DR ProteomicsDB; 56753; -. [P55008-1] DR ProteomicsDB; 56754; -. [P55008-2] DR ProteomicsDB; 56755; -. [P55008-3] DR Pumba; P55008; -. DR TopDownProteomics; P55008-1; -. [P55008-1] DR Antibodypedia; 27285; 1028 antibodies from 47 providers. DR DNASU; 199; -. DR Ensembl; ENST00000376049.4; ENSP00000365217.4; ENSG00000204472.14. [P55008-2] DR Ensembl; ENST00000376059.8; ENSP00000365227.3; ENSG00000204472.14. [P55008-1] DR Ensembl; ENST00000383473.4; ENSP00000372965.4; ENSG00000206428.9. [P55008-2] DR Ensembl; ENST00000383474.8; ENSP00000372966.4; ENSG00000206428.9. [P55008-1] DR Ensembl; ENST00000413349.6; ENSP00000416061.2; ENSG00000235985.7. [P55008-1] DR Ensembl; ENST00000414149.6; ENSP00000391720.2; ENSG00000237727.7. [P55008-1] DR Ensembl; ENST00000415830.2; ENSP00000413709.2; ENSG00000235985.7. [P55008-2] DR Ensembl; ENST00000416422.2; ENSP00000399901.2; ENSG00000234836.7. [P55008-2] DR Ensembl; ENST00000419376.2; ENSP00000401433.2; ENSG00000237727.7. [P55008-2] DR Ensembl; ENST00000424944.2; ENSP00000399621.2; ENSG00000235588.8. [P55008-2] DR Ensembl; ENST00000425748.6; ENSP00000398013.2; ENSG00000234836.7. [P55008-1] DR Ensembl; ENST00000440907.6; ENSP00000397842.2; ENSG00000235588.8. [P55008-1] DR GeneID; 199; -. DR KEGG; hsa:199; -. DR MANE-Select; ENST00000376059.8; ENSP00000365227.3; NM_001623.5; NP_001614.3. DR UCSC; uc003nva.4; human. [P55008-1] DR AGR; HGNC:352; -. DR ClinPGx; PA24646; -. DR CTD; 199; -. DR DisGeNET; 199; -. DR GeneCards; AIF1; -. DR HGNC; HGNC:352; AIF1. DR HPA; ENSG00000204472; Tissue enhanced (bone marrow, lymphoid tissue). DR MIM; 601833; gene. DR OpenTargets; ENSG00000204472; -. DR VEuPathDB; HostDB:ENSG00000204472; -. DR eggNOG; KOG0027; Eukaryota. DR GeneTree; ENSGT00390000013846; -. DR HOGENOM; CLU_134149_0_0_1; -. DR InParanoid; P55008; -. DR OMA; AAFKXLM; -. DR OrthoDB; 26525at2759; -. DR PAN-GO; P55008; 6 GO annotations based on evolutionary models. DR PhylomeDB; P55008; -. DR PathwayCommons; P55008; -. DR SignaLink; P55008; -. DR Agora; ENSG00000204472; -. DR BioGRID-ORCS; 199; 6 hits in 1120 CRISPR screens. DR ChiTaRS; AIF1; human. DR EvolutionaryTrace; P55008; -. DR GeneWiki; AIF1; -. DR GenomeRNAi; 199; -. DR Pharos; P55008; Tbio. DR PRO; PR:P55008; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; P55008; protein. DR Bgee; ENSG00000204472; Expressed in monocyte and 95 other cell types or tissues. DR ExpressionAtlas; P55008; baseline and differential. DR GO; GO:0005884; C:actin filament; ISS:ARUK-UCL. DR GO; GO:0005737; C:cytoplasm; IDA:ARUK-UCL. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB. DR GO; GO:0001891; C:phagocytic cup; ISS:UniProtKB. DR GO; GO:0001726; C:ruffle; ISS:ARUK-UCL. DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB. DR GO; GO:0051764; P:actin crosslink formation; ISS:ARUK-UCL. DR GO; GO:0051017; P:actin filament bundle assembly; IDA:UniProtKB. DR GO; GO:0030041; P:actin filament polymerization; IDA:UniProtKB. DR GO; GO:0034599; P:cellular response to oxidative stress; IDA:ARUK-UCL. DR GO; GO:0071346; P:cellular response to type II interferon; IEP:UniProtKB. DR GO; GO:0006954; P:inflammatory response; ISS:UniProtKB. DR GO; GO:0001774; P:microglial cell activation; NAS:UniProtKB. DR GO; GO:0071672; P:negative regulation of smooth muscle cell chemotaxis; IDA:UniProtKB. DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IDA:UniProtKB. DR GO; GO:0030046; P:parallel actin filament bundle assembly; ISS:ARUK-UCL. DR GO; GO:0006911; P:phagocytosis, engulfment; ISS:UniProtKB. DR GO; GO:0030335; P:positive regulation of cell migration; IDA:ARUK-UCL. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:ARUK-UCL. DR GO; GO:0032722; P:positive regulation of chemokine production; IDA:ARUK-UCL. DR GO; GO:0050921; P:positive regulation of chemotaxis; IDA:ARUK-UCL. DR GO; GO:0090271; P:positive regulation of fibroblast growth factor production; IDA:ARUK-UCL. DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IDA:UniProtKB. DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:ARUK-UCL. DR GO; GO:0090026; P:positive regulation of monocyte chemotaxis; IDA:UniProtKB. DR GO; GO:0071677; P:positive regulation of mononuclear cell migration; IDA:ARUK-UCL. DR GO; GO:0071673; P:positive regulation of smooth muscle cell chemotaxis; IDA:UniProtKB. DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IDA:UniProtKB. DR GO; GO:2000406; P:positive regulation of T cell migration; IDA:UniProtKB. DR GO; GO:0042102; P:positive regulation of T cell proliferation; IDA:UniProtKB. DR GO; GO:0016601; P:Rac protein signal transduction; ISS:UniProtKB. DR GO; GO:0010468; P:regulation of gene expression; HDA:ARUK-UCL. DR GO; GO:0097178; P:ruffle assembly; ISS:UniProtKB. DR FunFam; 1.10.238.10:FF:000106; Allograft inflammatory factor 1; 1. DR Gene3D; 1.10.238.10; EF-hand; 1. DR InterPro; IPR049025; AIF-1_EF_pair. DR InterPro; IPR042433; AIF1/AIF1L. DR InterPro; IPR011992; EF-hand-dom_pair. DR InterPro; IPR002048; EF_hand_dom. DR PANTHER; PTHR10356:SF4; ALLOGRAFT INFLAMMATORY FACTOR 1; 1. DR PANTHER; PTHR10356; ALLOGRAFT INFLAMMATORY FACTOR-1; 1. DR Pfam; PF21008; AIF-1; 1. DR SUPFAM; SSF47473; EF-hand; 1. DR PROSITE; PS50222; EF_HAND_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Actin-binding; Alternative splicing; Calcium; KW Cell membrane; Cell projection; Cytoplasm; Cytoskeleton; Membrane; KW Metal-binding; Phosphoprotein; Proteomics identification; KW 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_0000073865" 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 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:0007744|PubMed:19608861" FT MOD_RES 39 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT VAR_SEQ 1..65 FT /note="MSQTRDLQGGKAFGLLKAQQEERLDEINKQFLDDPKYSSDEDLPSKLEGFKE FT KYMEFDLNGNGDI -> MEFDLNGNGDIGEKRVICGGRVVCRPKKTEVSPTCSIPHDLG FT GGPPTTVGGRRMGMRKWERRERVSPPSPHPHPLPP (in isoform 3)" FT /evidence="ECO:0000303|PubMed:8912632, ECO:0000303|Ref.9" FT /id="VSP_043837" FT VAR_SEQ 1..54 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.11, ECO:0000303|Ref.7, FT ECO:0000303|Ref.8" FT /id="VSP_043838" FT VAR_SEQ 121..147 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:8912632, ECO:0000303|Ref.9" FT /id="VSP_043839" FT VARIANT 14 FT /note="G -> R (in dbSNP:rs2736182)" FT /evidence="ECO:0000269|PubMed:14656967, FT ECO:0000269|PubMed:14702039" FT /id="VAR_048665" FT CONFLICT 33 FT /note="D -> H (in Ref. 1; AAA92457)" FT /evidence="ECO:0000305" FT CONFLICT 131..147 FT /note="KEKPTGPPAKKAISELP -> RKTNTPPSQESPI (in Ref. 1; FT AAA92457)" FT /evidence="ECO:0000305" FT STRAND 10..13 FT /evidence="ECO:0007829|PDB:2G2B" FT HELIX 20..32 FT /evidence="ECO:0007829|PDB:2D58" FT HELIX 35..37 FT /evidence="ECO:0007829|PDB:2D58" FT HELIX 43..54 FT /evidence="ECO:0007829|PDB:2D58" FT HELIX 67..76 FT /evidence="ECO:0007829|PDB:2D58" FT HELIX 83..93 FT /evidence="ECO:0007829|PDB:2D58" FT STRAND 95..101 FT /evidence="ECO:0007829|PDB:2D58" FT HELIX 103..110 FT /evidence="ECO:0007829|PDB:2D58" FT STRAND 111..114 FT /evidence="ECO:0007829|PDB:2D58" FT HELIX 117..122 FT /evidence="ECO:0007829|PDB:2D58" SQ SEQUENCE 147 AA; 16703 MW; 0104CCF092074E8F CRC64; MSQTRDLQGG KAFGLLKAQQ EERLDEINKQ FLDDPKYSSD EDLPSKLEGF KEKYMEFDLN GNGDIDIMSL KRMLEKLGVP KTHLELKKLI GEVSSGSGET FSYPDFLRMM LGKRSAILKM ILMYEEKARE KEKPTGPPAK KAISELP //