AIF1_HUMAN
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 03-AUG-2022, entry version 183.
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 (1.9 ANGSTROMS) OF 17-123 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_001318970.1. [P55008-2]
DR RefSeq; NP_001614.3; NM_001623.4. [P55008-1]
DR RefSeq; NP_116573.1; NM_032955.2. [P55008-2]
DR RefSeq; XP_016865821.1; XM_017010332.1. [P55008-3]
DR PDB; 2D58; X-ray; 1.90 A; A=17-123.
DR PDB; 2G2B; NMR; -; A=2-147.
DR PDBsum; 2D58; -.
DR PDBsum; 2G2B; -.
DR AlphaFoldDB; P55008; -.
DR BMRB; P55008; -.
DR SMR; P55008; -.
DR BioGRID; 106702; 9.
DR IntAct; P55008; 6.
DR MINT; P55008; -.
DR STRING; 9606.ENSP00000365227; -.
DR iPTMnet; P55008; -.
DR PhosphoSitePlus; P55008; -.
DR BioMuta; AIF1; -.
DR DMDM; 1703217; -.
DR EPD; P55008; -.
DR jPOST; P55008; -.
DR MassIVE; P55008; -.
DR MaxQB; P55008; -.
DR PaxDb; P55008; -.
DR PeptideAtlas; P55008; -.
DR PRIDE; P55008; -.
DR ProteomicsDB; 56753; -. [P55008-1]
DR ProteomicsDB; 56754; -. [P55008-2]
DR ProteomicsDB; 56755; -. [P55008-3]
DR TopDownProteomics; P55008-1; -. [P55008-1]
DR Antibodypedia; 27285; 873 antibodies from 44 providers.
DR DNASU; 199; -.
DR Ensembl; ENST00000376049.4; ENSP00000365217.4; ENSG00000204472.13. [P55008-2]
DR Ensembl; ENST00000376059.8; ENSP00000365227.3; ENSG00000204472.13. [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 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 neXtProt; NX_P55008; -.
DR OpenTargets; ENSG00000204472; -.
DR PharmGKB; PA24646; -.
DR VEuPathDB; HostDB:ENSG00000204472; -.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00390000013846; -.
DR HOGENOM; CLU_134149_0_0_1; -.
DR InParanoid; P55008; -.
DR OMA; NKYMEFD; -.
DR OrthoDB; 1557466at2759; -.
DR PhylomeDB; P55008; -.
DR TreeFam; TF320736; -.
DR PathwayCommons; P55008; -.
DR SignaLink; P55008; -.
DR BioGRID-ORCS; 199; 5 hits in 1042 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 93 other tissues.
DR ExpressionAtlas; P55008; baseline and differential.
DR Genevisible; P55008; HS.
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:0097386; C:glial cell projection; IEA:Ensembl.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:Ensembl.
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:0031668; P:cellular response to extracellular stimulus; IEA:Ensembl.
DR GO; GO:0032870; P:cellular response to hormone stimulus; IEA:Ensembl.
DR GO; GO:0071447; P:cellular response to hydroperoxide; IEA:Ensembl.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IEP:UniProtKB.
DR GO; GO:0071315; P:cellular response to morphine; IEA:Ensembl.
DR GO; GO:0034599; P:cellular response to oxidative stress; IDA:ARUK-UCL.
DR GO; GO:0021549; P:cerebellum development; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
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:0014739; P:positive regulation of muscle hyperplasia; IEA:Ensembl.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IEA:Ensembl.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl.
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:0048678; P:response to axon injury; IEA:Ensembl.
DR GO; GO:0051602; P:response to electrical stimulus; IEA:Ensembl.
DR GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR GO; GO:0097178; P:ruffle assembly; ISS:UniProtKB.
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; Alternative splicing; Calcium;
KW Cell membrane; Cell projection; Cytoplasm; Cytoskeleton; Membrane;
KW Metal-binding; 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_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
