MIF_HUMAN
ID MIF_HUMAN Reviewed; 115 AA.
AC P14174; A5Z1R8; B2R4S3; Q2V4Y5; Q6FHV0;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 240.
DE RecName: Full=Macrophage migration inhibitory factor {ECO:0000303|PubMed:2552447};
DE Short=MIF {ECO:0000303|PubMed:2552447};
DE EC=5.3.2.1 {ECO:0000269|PubMed:11439086};
DE AltName: Full=Glycosylation-inhibiting factor {ECO:0000250|UniProtKB:P34884};
DE Short=GIF {ECO:0000250|UniProtKB:P34884};
DE AltName: Full=L-dopachrome isomerase;
DE AltName: Full=L-dopachrome tautomerase;
DE EC=5.3.3.12 {ECO:0000269|PubMed:17526494};
DE AltName: Full=Phenylpyruvate tautomerase;
GN Name=MIF {ECO:0000303|PubMed:2552447, ECO:0000312|HGNC:HGNC:7097};
GN Synonyms=GLIF, MMIF;
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 [MRNA], INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=2552447; DOI=10.1073/pnas.86.19.7522;
RA Weiser W.Y., Temple P.A., Witek-Giannotti J.S., Remold H.G., Clark S.C.,
RA David J.R.;
RT "Molecular cloning of a cDNA encoding a human macrophage migration
RT inhibitory factor.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:7522-7526(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RX PubMed=8234256; DOI=10.1073/pnas.90.21.10056;
RA Mikayama T., Nakano T., Gomi H., Nakagawa Y., Liu Y.C., Iwamatsu A.,
RA Weiser W.Y., Ishizaka K., Sato M., Ishii Y.;
RT "Molecular cloning and functional expression of a cDNA encoding
RT glycosylation-inhibiting factor.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:10056-10060(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7947826; DOI=10.1021/bi00251a025;
RA Bernhagen J., Mitchell R.A., Calandra T., Voelter W., Cerami A., Bucala R.;
RT "Purification, bioactivity, and secondary structure analysis of mouse and
RT human macrophage migration inhibitory factor (MIF).";
RL Biochemistry 33:14144-14155(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8188240; DOI=10.1006/geno.1994.1011;
RA Paralkar V., Wistow G.J.;
RT "Cloning the human gene for macrophage migration inhibitory factor (MIF).";
RL Genomics 19:48-51(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Shan Z.X., Yu X.Y., Lin S.G., Lin Q.X., Fu Y.H., Tan H.H.;
RT "The effect of macrophage migration inhibitory factor in the atherogenesis
RT process.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wu S.H., Xie J., Shang H.X., Li Y., Zhang Z.;
RT "Amplification and expression of macrophage migration inhibitory factor
RT (MIF) in tissue of squamous carcinoma of the cervix.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [12]
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 [13]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Lung, Skin, and Uterus;
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 [14]
RP PROTEIN SEQUENCE OF 2-12.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [15]
RP PROTEIN SEQUENCE OF 2-11.
RC TISSUE=Liver;
RX PubMed=1286669; DOI=10.1002/elps.11501301201;
RA Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F.,
RA Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R.,
RA Appel R.D., Hughes G.J.;
RT "Human liver protein map: a reference database established by
RT microsequencing and gel comparison.";
RL Electrophoresis 13:992-1001(1992).
RN [16]
RP PROTEIN SEQUENCE OF 3-24.
RX PubMed=7683862; DOI=10.1006/abbi.1993.1257;
RA Zeng F.Y., Weiser W.Y., Kratzin H., Stahl B., Karas M., Gabius H.J.;
RT "The major binding protein of the interferon antagonist sarcolectin in
RT human placenta is a macrophage migration inhibitory factor.";
RL Arch. Biochem. Biophys. 303:74-80(1993).
RN [17]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 10-115.
RC TISSUE=Lens;
RX PubMed=7679497; DOI=10.1073/pnas.90.4.1272;
RA Wistow G.J., Shaughnessy M., Lee D.C., Hodin J., Zelenka P.S.;
RT "A macrophage migration inhibitory factor is expressed in the
RT differentiating cells of the eye lens.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:1272-1275(1993).
RN [18]
RP INTERACTION WITH COPS5, AND SUBCELLULAR LOCATION.
RX PubMed=11089976; DOI=10.1038/35041591;
RA Kleemann R., Hausser A., Geiger G., Mischke R., Burger-Kentischer A.,
RA Flieger O., Johannes F.-J., Roger T., Calandra T., Kapurniotu A., Grell M.,
RA Finkelmeier D., Brunner H., Bernhagen J.;
RT "Intracellular action of the cytokine MIF to modulate AP-1 activity and the
RT cell cycle through Jab1.";
RL Nature 408:211-216(2000).
RN [19]
RP INVOLVEMENT IN RASJ.
RX PubMed=11508429;
RX DOI=10.1002/1529-0131(200108)44:8<1782::aid-art314>3.0.co;2-#;
RG The British peadiatric rheumatology study group;
RA Donn R.P., Shelley E., Ollier W.E.R., Thomson W.;
RT "A novel 5'-flanking region polymorphism of macrophage migration inhibitory
RT factor is associated with systemic-onset juvenile idiopathic arthritis.";
RL Arthritis Rheum. 44:1782-1785(2001).
RN [20]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=11439086; DOI=10.1042/0264-6021:3570373;
RA Tan T.H.P., Edgerton S.A.V., Kumari R., McAlister M.S.B., Roe S.M.,
RA Nagl S., Pearl L.H., Selkirk M.E., Bianco A.E., Totty N.F., Engwerda C.,
RA Gray C.A., Meyer D.J., Rowe S.M.;
RT "Macrophage migration inhibitory factor of the parasitic nematode
RT Trichinella spiralis.";
RL Biochem. J. 357:373-383(2001).
RN [21]
RP INTERACTION WITH BNIPL.
RX PubMed=12681488; DOI=10.1016/s0014-5793(03)00229-1;
RA Shen L., Hu J., Lu H., Wu M., Qin W., Wan D., Li Y.-Y., Gu J.;
RT "The apoptosis-associated protein BNIPL interacts with two cell
RT proliferation-related proteins, MIF and GFER.";
RL FEBS Lett. 540:86-90(2003).
RN [22]
RP INTERACTION WITH CD74.
RX PubMed=12782713; DOI=10.1084/jem.20030286;
RA Leng L., Metz C.N., Fang Y., Xu J., Donnelly S., Baugh J., Delohery T.,
RA Chen Y., Mitchell R.A., Bucala R.;
RT "MIF signal transduction initiated by binding to CD74.";
RL J. Exp. Med. 197:1467-1476(2003).
RN [23]
RP FUNCTION, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15908412; DOI=10.1128/iai.73.6.3783-3786.2005;
RA Oddo M., Calandra T., Bucala R., Meylan P.R.A.;
RT "Macrophage migration inhibitory factor reduces the growth of virulent
RT Mycobacterium tuberculosis in human macrophages.";
RL Infect. Immun. 73:3783-3786(2005).
RN [24]
RP ROLE IN SEPSIS-RELATED DEATH.
RX PubMed=17443469; DOI=10.1086/514344;
RA Emonts M., Sweep F.C.G.J., Grebenchtchikov N., Geurts-Moespot A., Knaup M.,
RA Chanson A.L., Erard V., Renner P., Hermans P.W.M., Hazelzet J.A.,
RA Calandra T.;
RT "Association between high levels of blood macrophage migration inhibitory
RT factor, inappropriate adrenal response, and early death in patients with
RT severe sepsis.";
RL Clin. Infect. Dis. 44:1321-1328(2007).
RN [25]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH USO1.
RX PubMed=19454686; DOI=10.4049/jimmunol.0803710;
RA Merk M., Baugh J., Zierow S., Leng L., Pal U., Lee S.J., Ebert A.D.,
RA Mizue Y., Trent J.O., Mitchell R., Nickel W., Kavathas P.B., Bernhagen J.,
RA Bucala R.;
RT "The Golgi-associated protein p115 mediates the secretion of macrophage
RT migration inhibitory factor.";
RL J. Immunol. 182:6896-6906(2009).
RN [26]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-78, 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 [27]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [28]
RP CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [29]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [30]
RP IDENTIFICATION BY 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 [31]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [32]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX PubMed=8766818; DOI=10.1016/0014-5793(96)00553-4;
RA Sugimoto H., Suzuki M., Nakagawa A., Tanaka I., Nishihira J.;
RT "Crystal structure of macrophage migration inhibitory factor from human
RT lymphocyte at 2.1-A resolution.";
RL FEBS Lett. 389:145-148(1996).
RN [33]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND SUBUNIT.
RX PubMed=8610159; DOI=10.1073/pnas.93.7.3007;
RA Kato Y., Muto T., Tomura T., Tsumura H., Watarai H., Mikayama T.,
RA Ishizaka K., Kuroki R.;
RT "The crystal structure of human glycosylation-inhibiting factor is a
RT trimeric barrel with three 6-stranded beta-sheets.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:3007-3010(1996).
RN [34]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX PubMed=8643551; DOI=10.1073/pnas.93.11.5191;
RA Sun H.W., Bernhagen J., Bucala R., Lolis E.;
RT "Crystal structure at 2.6-A resolution of human macrophage migration
RT inhibitory factor.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:5191-5196(1996).
RN [35]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=10353846; DOI=10.1021/bi990306m;
RA Lubetsky J.B., Swope M., Dealwis C., Blake P., Lolis E.;
RT "Pro-1 of macrophage migration inhibitory factor functions as a catalytic
RT base in the phenylpyruvate tautomerase activity.";
RL Biochemistry 38:7346-7354(1999).
RN [36]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH TAUTOMERASE
RP INHIBITOR, AND CATALYTIC ACTIVITY.
RX PubMed=11170644; DOI=10.1021/jm000386o;
RA Orita M., Yamamoto S., Katayama N., Aoki M., Takayama K., Yamagiwa Y.,
RA Seki N., Suzuki H., Kurihara H., Sakashita H., Takeuchi M., Fujita S.,
RA Yamada T., Tanaka A.;
RT "Coumarin and chromen-4-one analogues as tautomerase inhibitors of
RT macrophage migration inhibitory factor: discovery and X-ray
RT crystallography.";
RL J. Med. Chem. 44:540-547(2001).
RN [37]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH CARBONYLOXIME-BASED
RP INHIBITORS, SUBUNIT, CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=17526494; DOI=10.1074/jbc.m701825200;
RA Crichlow G.V., Cheng K.F., Dabideen D., Ochani M., Aljabari B.,
RA Pavlov V.A., Miller E.J., Lolis E., Al-Abed Y.;
RT "Alternative chemical modifications reverse the binding orientation of a
RT pharmacophore scaffold in the active site of macrophage migration
RT inhibitory factor.";
RL J. Biol. Chem. 282:23089-23095(2007).
RN [38]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH THE INHIBITOR
RP N-ACETYL-P-BENZOQUINONE IMINE, SUBUNIT, AND CATALYTIC ACTIVITY.
RX PubMed=19090677; DOI=10.1021/bi8014423;
RA Crichlow G.V., Lubetsky J.B., Leng L., Bucala R., Lolis E.J.;
RT "Structural and kinetic analyses of macrophage migration inhibitory factor
RT active site interactions.";
RL Biochemistry 48:132-139(2009).
RN [39]
RP X-RAY CRYSTALLOGRAPHY (2.33 ANGSTROMS), SUBUNIT, FUNCTION, CATALYTIC
RP ACTIVITY, INTERACTION WITH CD74, AND MUTAGENESIS OF ASN-111.
RX PubMed=23776208; DOI=10.1073/pnas.1221817110;
RA Fan C., Rajasekaran D., Syed M.A., Leng L., Loria J.P., Bhandari V.,
RA Bucala R., Lolis E.J.;
RT "MIF intersubunit disulfide mutant antagonist supports activation of CD74
RT by endogenous MIF trimer at physiologic concentrations.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:10994-10999(2013).
CC -!- FUNCTION: Pro-inflammatory cytokine involved in the innate immune
CC response to bacterial pathogens (PubMed:15908412, PubMed:17443469,
CC PubMed:23776208). The expression of MIF at sites of inflammation
CC suggests a role as mediator in regulating the function of macrophages
CC in host defense (PubMed:15908412, PubMed:17443469, PubMed:23776208).
CC Counteracts the anti-inflammatory activity of glucocorticoids
CC (PubMed:15908412, PubMed:17443469, PubMed:23776208). Has phenylpyruvate
CC tautomerase and dopachrome tautomerase activity (in vitro), but the
CC physiological substrate is not known (PubMed:11439086,
CC PubMed:17526494). It is not clear whether the tautomerase activity has
CC any physiological relevance, and whether it is important for cytokine
CC activity (PubMed:11439086, PubMed:17526494).
CC {ECO:0000269|PubMed:11439086, ECO:0000269|PubMed:15908412,
CC ECO:0000269|PubMed:17443469, ECO:0000269|PubMed:17526494,
CC ECO:0000269|PubMed:23776208}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-phenylpyruvate = enol-phenylpyruvate; Xref=Rhea:RHEA:17097,
CC ChEBI:CHEBI:16815, ChEBI:CHEBI:18005; EC=5.3.2.1;
CC Evidence={ECO:0000269|PubMed:11439086};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-dopachrome = 5,6-dihydroxyindole-2-carboxylate;
CC Xref=Rhea:RHEA:13041, ChEBI:CHEBI:16875, ChEBI:CHEBI:57509;
CC EC=5.3.3.12; Evidence={ECO:0000269|PubMed:17526494};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=249 uM for phenylpyruvate {ECO:0000269|PubMed:11439086};
CC KM=168 uM for p-hydroxyphenylpyruvate {ECO:0000269|PubMed:11439086};
CC Vmax=2113 umol/min/mg enzyme toward phenylpyruvate
CC {ECO:0000269|PubMed:11439086};
CC Vmax=524 umol/min/mg enzyme toward p-hydroxyphenylpyruvate
CC {ECO:0000269|PubMed:11439086};
CC -!- SUBUNIT: Homotrimer (PubMed:8610159, PubMed:23776208). Interacts with
CC CXCR2 extracellular domain (By similarity). Interacts with the CD74
CC extracellular domain, USO1, COPS5 and BNIPL (PubMed:11089976,
CC PubMed:12681488, PubMed:12782713, PubMed:19454686, PubMed:23776208).
CC {ECO:0000250|UniProtKB:P34884, ECO:0000269|PubMed:11089976,
CC ECO:0000269|PubMed:12681488, ECO:0000269|PubMed:12782713,
CC ECO:0000269|PubMed:19454686, ECO:0000269|PubMed:23776208,
CC ECO:0000269|PubMed:8610159}.
CC -!- INTERACTION:
CC P14174; O43521-2: BCL2L11; NbExp=5; IntAct=EBI-372712, EBI-526420;
CC P14174; P00533: EGFR; NbExp=3; IntAct=EBI-372712, EBI-297353;
CC P14174; Q92743: HTRA1; NbExp=3; IntAct=EBI-372712, EBI-352256;
CC P14174; P14174: MIF; NbExp=7; IntAct=EBI-372712, EBI-372712;
CC P14174; Q96HA8: NTAQ1; NbExp=4; IntAct=EBI-372712, EBI-741158;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15908412,
CC ECO:0000269|PubMed:19454686, ECO:0000269|PubMed:2552447,
CC ECO:0000269|PubMed:8234256}. Cytoplasm {ECO:0000269|PubMed:11089976,
CC ECO:0000269|PubMed:19454686}. Note=Does not have a cleavable signal
CC sequence and is secreted via a specialized, non-classical pathway.
CC Secreted by macrophages upon stimulation by bacterial
CC lipopolysaccharide (LPS), or by M.tuberculosis antigens.
CC {ECO:0000269|PubMed:15908412}.
CC -!- INDUCTION: Up-regulated in concanavalin-A-treated lymphocytes. Up-
CC regulated in macrophages upon exposure to M.tuberculosis antigens.
CC {ECO:0000269|PubMed:15908412, ECO:0000269|PubMed:2552447}.
CC -!- DISEASE: Rheumatoid arthritis systemic juvenile (RASJ) [MIM:604302]: An
CC inflammatory articular disorder with systemic onset beginning before
CC the age of 16. It represents a subgroup of juvenile arthritis
CC associated with severe extraarticular features and occasionally fatal
CC complications. During active phases of the disorder, patients display a
CC typical daily spiking fever, an evanescent macular rash,
CC lymphadenopathy, hepatosplenomegaly, serositis, myalgia and arthritis.
CC {ECO:0000269|PubMed:11508429}. Note=Disease susceptibility is
CC associated with variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: Serum levels of MIF are elevated in patients with severe
CC sepsis or septic shock. High levels of MIF are correlated with low
CC survival. Drugs that inhibit tautomerase activity protect against death
CC due to sepsis. {ECO:0000269|PubMed:17443469}.
CC -!- SIMILARITY: Belongs to the MIF family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/mif/";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/MIFID41365ch22q11.html";
CC ---------------------------------------------------------------------------
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CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
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DR EMBL; M25639; AAA36315.1; -; mRNA.
DR EMBL; L10612; AAA35892.1; -; mRNA.
DR EMBL; Z23063; CAA80598.1; -; mRNA.
DR EMBL; L19686; AAA21814.1; -; Genomic_DNA.
DR EMBL; AF469046; AAL78635.1; -; mRNA.
DR EMBL; EF611126; ABQ95571.1; -; mRNA.
DR EMBL; CR456520; CAG30406.1; -; mRNA.
DR EMBL; AK311929; BAG34870.1; -; mRNA.
DR EMBL; CR407644; CAG28572.1; -; mRNA.
DR EMBL; CR541651; CAG46452.1; -; mRNA.
DR EMBL; BT007148; AAP35812.1; -; mRNA.
DR EMBL; DQ307455; ABB96245.1; -; Genomic_DNA.
DR EMBL; CH471095; EAW59620.1; -; Genomic_DNA.
DR EMBL; BC000447; AAH00447.1; -; mRNA.
DR EMBL; BC007676; AAH07676.1; -; mRNA.
DR EMBL; BC008914; AAH08914.1; -; mRNA.
DR EMBL; BC013976; AAH13976.1; -; mRNA.
DR EMBL; BC022414; AAH22414.1; -; mRNA.
DR EMBL; BC053376; AAH53376.1; -; mRNA.
DR EMBL; M95775; AAA36179.1; -; mRNA.
DR CCDS; CCDS13819.1; -.
DR PIR; A48793; A48793.
DR RefSeq; NP_002406.1; NM_002415.1.
DR PDB; 1CA7; X-ray; 2.50 A; A/B/C=2-115.
DR PDB; 1CGQ; X-ray; 2.00 A; A/B/C=2-115.
DR PDB; 1GCZ; X-ray; 1.90 A; A/B/C=2-115.
DR PDB; 1GD0; X-ray; 1.50 A; A/B/C=2-115.
DR PDB; 1GIF; X-ray; 1.90 A; A/B/C=1-115.
DR PDB; 1LJT; X-ray; 2.00 A; A/B/C=2-115.
DR PDB; 1MIF; X-ray; 2.60 A; A/B/C=1-115.
DR PDB; 1P1G; X-ray; 2.50 A; A/B/C=2-115.
DR PDB; 2OOH; X-ray; 1.85 A; A/B/C=2-115.
DR PDB; 2OOW; X-ray; 1.75 A; A/B/C=2-115.
DR PDB; 2OOZ; X-ray; 1.80 A; A/B/C=2-115.
DR PDB; 3B9S; X-ray; 1.80 A; A/B/C=2-115.
DR PDB; 3CE4; X-ray; 1.55 A; A/B/C=2-115.
DR PDB; 3DJH; X-ray; 1.25 A; A/B/C=2-115.
DR PDB; 3DJI; X-ray; 1.95 A; A/B/C/D/E/F=2-115.
DR PDB; 3HOF; X-ray; 1.90 A; A/B/C=1-115.
DR PDB; 3IJG; X-ray; 1.70 A; A/B/C=2-115.
DR PDB; 3IJJ; X-ray; 1.25 A; A/B/C=2-115.
DR PDB; 3JSF; X-ray; 1.93 A; A/B/C=2-115.
DR PDB; 3JSG; X-ray; 1.58 A; A/B/C=2-115.
DR PDB; 3JTU; X-ray; 1.86 A; A/B/C=2-115.
DR PDB; 3L5P; X-ray; 1.80 A; A/B/C=2-115.
DR PDB; 3L5R; X-ray; 1.94 A; A/B/C=2-115.
DR PDB; 3L5S; X-ray; 1.86 A; A/B/C=2-115.
DR PDB; 3L5T; X-ray; 1.86 A; A/B/C=2-115.
DR PDB; 3L5U; X-ray; 1.90 A; A/B/C=2-115.
DR PDB; 3L5V; X-ray; 1.70 A; A/B/C=2-115.
DR PDB; 3SMB; X-ray; 1.60 A; A/B/C=2-115.
DR PDB; 3SMC; X-ray; 1.80 A; A/B/C=2-115.
DR PDB; 3U18; X-ray; 1.90 A; A/B/C=2-115.
DR PDB; 3WNR; X-ray; 2.01 A; A/B/C=2-115.
DR PDB; 3WNS; X-ray; 1.66 A; A/B/C=2-115.
DR PDB; 3WNT; X-ray; 2.07 A; A/B/C=2-115.
DR PDB; 4ETG; X-ray; 1.61 A; A/B/C=2-115.
DR PDB; 4EUI; X-ray; 1.70 A; A/B/C=2-115.
DR PDB; 4EVG; X-ray; 1.70 A; A/B/C=2-115.
DR PDB; 4F2K; X-ray; 1.53 A; A/B/C=2-115.
DR PDB; 4GRN; X-ray; 1.25 A; A/B/C=2-115.
DR PDB; 4GRO; X-ray; 2.00 A; A/B/C/D/E/F/G/H=2-115.
DR PDB; 4GRP; X-ray; 1.27 A; A/B/C=2-115.
DR PDB; 4GRQ; X-ray; 1.65 A; A/B/C=2-115.
DR PDB; 4GRR; X-ray; 1.47 A; A/B/C=3-115.
DR PDB; 4GRU; X-ray; 1.92 A; A/B/C=2-115.
DR PDB; 4GUM; X-ray; 2.33 A; A/B/C/D/E/F/G/H/I=2-115.
DR PDB; 4K9G; X-ray; 1.55 A; A/B/C=2-115.
DR PDB; 4OSF; X-ray; 1.62 A; A/B/C=2-115.
DR PDB; 4OYQ; X-ray; 1.70 A; A/B/C=2-115.
DR PDB; 4P01; X-ray; 2.07 A; A/B/C=2-115.
DR PDB; 4P0H; X-ray; 1.93 A; A/B/C=2-115.
DR PDB; 4PKK; X-ray; 1.78 A; A/B/C=2-115.
DR PDB; 4PKZ; X-ray; 1.90 A; A/B/C=2-115.
DR PDB; 4PLU; X-ray; 1.63 A; A/B/C=2-115.
DR PDB; 4TRF; X-ray; 1.63 A; A/B/C=2-115.
DR PDB; 4TRU; X-ray; 1.81 A; A/B/C=2-115.
DR PDB; 4WR8; X-ray; 2.60 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R=2-115.
DR PDB; 4WRB; X-ray; 1.81 A; A/B/C=2-115.
DR PDB; 4XX7; X-ray; 1.77 A; A/B/C=2-115.
DR PDB; 4XX8; X-ray; 1.77 A; A/B/C=3-115.
DR PDB; 4Z15; X-ray; 1.60 A; A/B/C=3-115.
DR PDB; 4Z1T; X-ray; 1.50 A; A/B/C=3-115.
DR PDB; 4Z1U; X-ray; 2.05 A; A/B/C/D/E/F=3-115.
DR PDB; 5B4O; X-ray; 1.37 A; A/B/C=2-115.
DR PDB; 5BS9; X-ray; 1.98 A; A/B/C=2-115.
DR PDB; 5BSC; X-ray; 1.89 A; A/B/C=2-115.
DR PDB; 5BSI; X-ray; 2.00 A; A/B/C/D/E/F/G/J=2-115.
DR PDB; 5BSJ; X-ray; 2.00 A; A/B/C=2-115.
DR PDB; 5EIZ; X-ray; 1.96 A; A/B/C=2-115.
DR PDB; 5HVS; X-ray; 1.75 A; A/B/C=2-115.
DR PDB; 5HVT; X-ray; 1.75 A; A/B/C=2-115.
DR PDB; 5HVV; X-ray; 1.90 A; A/B/C=3-115.
DR PDB; 5J7P; X-ray; 1.85 A; A/B/C=2-115.
DR PDB; 5J7Q; X-ray; 2.05 A; A/B/C=2-115.
DR PDB; 5UMJ; X-ray; 1.61 A; A/B/C=2-115.
DR PDB; 5UMK; X-ray; 1.73 A; A/B/C=2-115.
DR PDB; 5UZY; X-ray; 1.71 A; A/B/C=2-115.
DR PDB; 5V70; X-ray; 1.94 A; A/B/C=2-115.
DR PDB; 5V73; X-ray; 1.68 A; A/B/C=2-115.
DR PDB; 5XEJ; X-ray; 2.50 A; A/B/C=2-115.
DR PDB; 6B1C; X-ray; 2.16 A; A/B/C=2-115.
DR PDB; 6B1K; X-ray; 1.17 A; A/B/C=2-115.
DR PDB; 6B2C; X-ray; 2.00 A; A/B/C=2-115.
DR PDB; 6BG6; X-ray; 1.52 A; A/B/C=2-115.
DR PDB; 6BG7; X-ray; 2.54 A; A/B/C=2-115.
DR PDB; 6CB5; X-ray; 1.78 A; A/B/C=2-115.
DR PDB; 6CBF; X-ray; 2.30 A; A/B/C=2-115.
DR PDB; 6CBG; X-ray; 2.00 A; A/B/C=2-115.
DR PDB; 6CBH; X-ray; 2.00 A; A/B/C=2-115.
DR PDB; 6FVE; X-ray; 1.41 A; A/B/C=2-115.
DR PDB; 6FVH; X-ray; 1.40 A; A/B/C=2-115.
DR PDB; 6OY8; X-ray; 1.53 A; A/B/C=2-115.
DR PDB; 6OYB; X-ray; 1.53 A; A/B/C=2-115.
DR PDB; 6OYE; X-ray; 1.53 A; A/B/C=2-115.
DR PDB; 6OYG; X-ray; 1.55 A; A/B/C=2-115.
DR PDB; 6PEG; X-ray; 2.00 A; D/E/F=2-115.
DR PDB; 7KQX; X-ray; 1.60 A; A/B/C=2-115.
DR PDBsum; 1CA7; -.
DR PDBsum; 1CGQ; -.
DR PDBsum; 1GCZ; -.
DR PDBsum; 1GD0; -.
DR PDBsum; 1GIF; -.
DR PDBsum; 1LJT; -.
DR PDBsum; 1MIF; -.
DR PDBsum; 1P1G; -.
DR PDBsum; 2OOH; -.
DR PDBsum; 2OOW; -.
DR PDBsum; 2OOZ; -.
DR PDBsum; 3B9S; -.
DR PDBsum; 3CE4; -.
DR PDBsum; 3DJH; -.
DR PDBsum; 3DJI; -.
DR PDBsum; 3HOF; -.
DR PDBsum; 3IJG; -.
DR PDBsum; 3IJJ; -.
DR PDBsum; 3JSF; -.
DR PDBsum; 3JSG; -.
DR PDBsum; 3JTU; -.
DR PDBsum; 3L5P; -.
DR PDBsum; 3L5R; -.
DR PDBsum; 3L5S; -.
DR PDBsum; 3L5T; -.
DR PDBsum; 3L5U; -.
DR PDBsum; 3L5V; -.
DR PDBsum; 3SMB; -.
DR PDBsum; 3SMC; -.
DR PDBsum; 3U18; -.
DR PDBsum; 3WNR; -.
DR PDBsum; 3WNS; -.
DR PDBsum; 3WNT; -.
DR PDBsum; 4ETG; -.
DR PDBsum; 4EUI; -.
DR PDBsum; 4EVG; -.
DR PDBsum; 4F2K; -.
DR PDBsum; 4GRN; -.
DR PDBsum; 4GRO; -.
DR PDBsum; 4GRP; -.
DR PDBsum; 4GRQ; -.
DR PDBsum; 4GRR; -.
DR PDBsum; 4GRU; -.
DR PDBsum; 4GUM; -.
DR PDBsum; 4K9G; -.
DR PDBsum; 4OSF; -.
DR PDBsum; 4OYQ; -.
DR PDBsum; 4P01; -.
DR PDBsum; 4P0H; -.
DR PDBsum; 4PKK; -.
DR PDBsum; 4PKZ; -.
DR PDBsum; 4PLU; -.
DR PDBsum; 4TRF; -.
DR PDBsum; 4TRU; -.
DR PDBsum; 4WR8; -.
DR PDBsum; 4WRB; -.
DR PDBsum; 4XX7; -.
DR PDBsum; 4XX8; -.
DR PDBsum; 4Z15; -.
DR PDBsum; 4Z1T; -.
DR PDBsum; 4Z1U; -.
DR PDBsum; 5B4O; -.
DR PDBsum; 5BS9; -.
DR PDBsum; 5BSC; -.
DR PDBsum; 5BSI; -.
DR PDBsum; 5BSJ; -.
DR PDBsum; 5EIZ; -.
DR PDBsum; 5HVS; -.
DR PDBsum; 5HVT; -.
DR PDBsum; 5HVV; -.
DR PDBsum; 5J7P; -.
DR PDBsum; 5J7Q; -.
DR PDBsum; 5UMJ; -.
DR PDBsum; 5UMK; -.
DR PDBsum; 5UZY; -.
DR PDBsum; 5V70; -.
DR PDBsum; 5V73; -.
DR PDBsum; 5XEJ; -.
DR PDBsum; 6B1C; -.
DR PDBsum; 6B1K; -.
DR PDBsum; 6B2C; -.
DR PDBsum; 6BG6; -.
DR PDBsum; 6BG7; -.
DR PDBsum; 6CB5; -.
DR PDBsum; 6CBF; -.
DR PDBsum; 6CBG; -.
DR PDBsum; 6CBH; -.
DR PDBsum; 6FVE; -.
DR PDBsum; 6FVH; -.
DR PDBsum; 6OY8; -.
DR PDBsum; 6OYB; -.
DR PDBsum; 6OYE; -.
DR PDBsum; 6OYG; -.
DR PDBsum; 6PEG; -.
DR PDBsum; 7KQX; -.
DR AlphaFoldDB; P14174; -.
DR SASBDB; P14174; -.
DR SMR; P14174; -.
DR BioGRID; 110428; 148.
DR DIP; DIP-31137N; -.
DR IntAct; P14174; 32.
DR MINT; P14174; -.
DR STRING; 9606.ENSP00000215754; -.
DR BindingDB; P14174; -.
DR ChEMBL; CHEMBL2085; -.
DR DrugBank; DB01880; 3,4-Dihydroxycinnamic Acid.
DR DrugBank; DB07888; 3-(4-HYDROXYPHENYL)-4,5-DIHYDRO-5-ISOXAZOLE-ACETIC ACID METHYL ESTER.
DR DrugBank; DB08334; 3-FLUORO-4-HYDROXYBENZALDEHYDE O-(CYCLOHEXYLCARBONYL)OXIME.
DR DrugBank; DB08335; 4-HYDROXYBENZALDEHYDE O-(3,3-DIMETHYLBUTANOYL)OXIME.
DR DrugBank; DB08333; 4-HYDROXYBENZALDEHYDE O-(CYCLOHEXYLCARBONYL)OXIME.
DR DrugBank; DB07718; 4-Hydroxyphenylpyruvic acid.
DR DrugBank; DB08765; 6-HYDROXY-1,3-BENZOTHIAZOLE-2-SULFONAMIDE.
DR DrugBank; DB02728; 7-Hydroxy-2-Oxo-Chromene-3-Carboxylic Acid Ethyl Ester.
DR GlyGen; P14174; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; P14174; -.
DR MetOSite; P14174; -.
DR PhosphoSitePlus; P14174; -.
DR SwissPalm; P14174; -.
DR BioMuta; MIF; -.
DR DMDM; 1170955; -.
DR SWISS-2DPAGE; P14174; -.
DR EPD; P14174; -.
DR jPOST; P14174; -.
DR MassIVE; P14174; -.
DR MaxQB; P14174; -.
DR PaxDb; P14174; -.
DR PeptideAtlas; P14174; -.
DR PRIDE; P14174; -.
DR ProteomicsDB; 53030; -.
DR TopDownProteomics; P14174; -.
DR ABCD; P14174; 12 sequenced antibodies.
DR Antibodypedia; 34865; 753 antibodies from 44 providers.
DR DNASU; 4282; -.
DR Ensembl; ENST00000215754.8; ENSP00000215754.7; ENSG00000240972.2.
DR Ensembl; ENST00000613839.2; ENSP00000482779.1; ENSG00000276701.2.
DR GeneID; 4282; -.
DR KEGG; hsa:4282; -.
DR MANE-Select; ENST00000215754.8; ENSP00000215754.7; NM_002415.2; NP_002406.1.
DR UCSC; uc002zyr.2; human.
DR CTD; 4282; -.
DR DisGeNET; 4282; -.
DR GeneCards; MIF; -.
DR HGNC; HGNC:7097; MIF.
DR HPA; ENSG00000240972; Low tissue specificity.
DR MalaCards; MIF; -.
DR MIM; 153620; gene.
DR MIM; 604302; phenotype.
DR neXtProt; NX_P14174; -.
DR OpenTargets; ENSG00000240972; -.
DR Orphanet; 586; Cystic fibrosis.
DR Orphanet; 85414; Systemic-onset juvenile idiopathic arthritis.
DR PharmGKB; PA30819; -.
DR VEuPathDB; HostDB:ENSG00000240972; -.
DR eggNOG; KOG1759; Eukaryota.
DR GeneTree; ENSGT00940000155608; -.
DR HOGENOM; CLU_129906_1_1_1; -.
DR InParanoid; P14174; -.
DR OMA; YINFFDM; -.
DR OrthoDB; 1451925at2759; -.
DR PhylomeDB; P14174; -.
DR TreeFam; TF313853; -.
DR BRENDA; 5.3.2.1; 2681.
DR BRENDA; 5.3.3.12; 2681.
DR PathwayCommons; P14174; -.
DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation.
DR SignaLink; P14174; -.
DR SIGNOR; P14174; -.
DR BioGRID-ORCS; 4282; 9 hits in 1074 CRISPR screens.
DR ChiTaRS; MIF; human.
DR EvolutionaryTrace; P14174; -.
DR GeneWiki; Macrophage_migration_inhibitory_factor; -.
DR GenomeRNAi; 4282; -.
DR Pharos; P14174; Tchem.
DR PRO; PR:P14174; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P14174; protein.
DR Bgee; ENSG00000240972; Expressed in adenohypophysis and 95 other tissues.
DR ExpressionAtlas; P14174; baseline and differential.
DR Genevisible; P14174; HS.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:ARUK-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR GO; GO:0031982; C:vesicle; HDA:UniProtKB.
DR GO; GO:0042056; F:chemoattractant activity; IDA:BHF-UCL.
DR GO; GO:0005125; F:cytokine activity; IDA:UniProtKB.
DR GO; GO:0005126; F:cytokine receptor binding; IDA:BHF-UCL.
DR GO; GO:0004167; F:dopachrome isomerase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0050178; F:phenylpyruvate tautomerase activity; IDA:BHF-UCL.
DR GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IDA:BHF-UCL.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0090398; P:cellular senescence; IEA:Ensembl.
DR GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; IEA:Ensembl.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; IMP:ARUK-UCL.
DR GO; GO:2000773; P:negative regulation of cellular senescence; IDA:BHF-UCL.
DR GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; IDA:BHF-UCL.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:BHF-UCL.
DR GO; GO:1902166; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IDA:BHF-UCL.
DR GO; GO:0010760; P:negative regulation of macrophage chemotaxis; IDA:BHF-UCL.
DR GO; GO:0002906; P:negative regulation of mature B cell apoptotic process; IEA:Ensembl.
DR GO; GO:0033033; P:negative regulation of myeloid cell apoptotic process; IEA:Ensembl.
DR GO; GO:0051248; P:negative regulation of protein metabolic process; IEA:Ensembl.
DR GO; GO:0090238; P:positive regulation of arachidonic acid secretion; IEA:Ensembl.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; IDA:BHF-UCL.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:BHF-UCL.
DR GO; GO:2000343; P:positive regulation of chemokine (C-X-C motif) ligand 2 production; IEA:Ensembl.
DR GO; GO:0001819; P:positive regulation of cytokine production; IDA:BHF-UCL.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:BHF-UCL.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IDA:BHF-UCL.
DR GO; GO:0031666; P:positive regulation of lipopolysaccharide-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IEA:Ensembl.
DR GO; GO:0061081; P:positive regulation of myeloid leukocyte cytokine production involved in immune response; IEA:Ensembl.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:BHF-UCL.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:BHF-UCL.
DR GO; GO:0042327; P:positive regulation of phosphorylation; IDA:BHF-UCL.
DR GO; GO:0061078; P:positive regulation of prostaglandin secretion involved in immune response; IEA:Ensembl.
DR GO; GO:0010739; P:positive regulation of protein kinase A signaling; IDA:BHF-UCL.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:BHF-UCL.
DR GO; GO:0001516; P:prostaglandin biosynthetic process; IDA:UniProtKB.
DR GO; GO:0070207; P:protein homotrimerization; IPI:UniProtKB.
DR GO; GO:0043030; P:regulation of macrophage activation; NAS:UniProtKB.
DR Gene3D; 3.30.429.10; -; 1.
DR InterPro; IPR001398; Macrophage_inhib_fac.
DR InterPro; IPR019829; Macrophage_inhib_fac_CS.
DR InterPro; IPR014347; Tautomerase/MIF_sf.
DR PANTHER; PTHR11954; PTHR11954; 1.
DR Pfam; PF01187; MIF; 1.
DR SUPFAM; SSF55331; SSF55331; 1.
DR PROSITE; PS01158; MIF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytokine; Cytoplasm; Direct protein sequencing;
KW Immunity; Inflammatory response; Innate immunity; Isomerase;
KW Reference proteome; Secreted.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801,
FT ECO:0000269|PubMed:1286669, ECO:0007744|PubMed:22223895"
FT CHAIN 2..115
FT /note="Macrophage migration inhibitory factor"
FT /id="PRO_0000158062"
FT ACT_SITE 2
FT /note="Proton acceptor; via imino nitrogen"
FT /evidence="ECO:0000250|UniProtKB:P34884"
FT BINDING 33
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11170644,
FT ECO:0000269|PubMed:17526494, ECO:0000269|PubMed:19090677"
FT BINDING 65
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11170644,
FT ECO:0000269|PubMed:17526494, ECO:0000269|PubMed:19090677"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11170644,
FT ECO:0000269|PubMed:17526494, ECO:0000269|PubMed:19090677"
FT MOD_RES 78
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 78
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P34884"
FT MUTAGEN 111
FT /note="N->C: Causes formation of interchain disulfide bonds
FT with Cys-81 from another subunit."
FT /evidence="ECO:0000269|PubMed:23776208"
FT CONFLICT 57..59
FT /note="CAL -> WAF (in Ref. 6; ABQ95571)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="K -> R (in Ref. 9; CAG46452)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="L -> Q (in Ref. 9; CAG46452)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="C -> F (in Ref. 6; ABQ95571)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="N -> S (in Ref. 1; AAA36315)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="T -> P (in Ref. 6; ABQ95571)"
FT /evidence="ECO:0000305"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:6B1K"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:6B1K"
FT HELIX 19..31
FT /evidence="ECO:0007829|PDB:6B1K"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:6B1K"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:6B1K"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:6B1K"
FT STRAND 58..66
FT /evidence="ECO:0007829|PDB:6B1K"
FT HELIX 70..88
FT /evidence="ECO:0007829|PDB:6B1K"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:6B1K"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:6B1K"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:6B1K"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:6B1K"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:1GD0"
SQ SEQUENCE 115 AA; 12476 MW; 56D51107C05286B2 CRC64;
MPMFIVNTNV PRASVPDGFL SELTQQLAQA TGKPPQYIAV HVVPDQLMAF GGSSEPCALC
SLHSIGKIGG AQNRSYSKLL CGLLAERLRI SPDRVYINYY DMNAANVGWN NSTFA
