MIF_MOUSE
ID MIF_MOUSE Reviewed; 115 AA.
AC P34884;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Macrophage migration inhibitory factor;
DE Short=MIF;
DE EC=5.3.2.1 {ECO:0000269|PubMed:10933783, ECO:0000269|PubMed:16780921, ECO:0000269|PubMed:19188446};
DE AltName: Full=Delayed early response protein 6;
DE Short=DER6;
DE AltName: Full=Glycosylation-inhibiting factor {ECO:0000303|PubMed:1508193};
DE Short=GIF {ECO:0000303|PubMed:1508193};
DE AltName: Full=L-dopachrome isomerase;
DE AltName: Full=L-dopachrome tautomerase;
DE EC=5.3.3.12 {ECO:0000269|PubMed:10933783, ECO:0000269|PubMed:16780921, ECO:0000269|PubMed:19188446};
DE AltName: Full=Phenylpyruvate tautomerase;
GN Name=Mif {ECO:0000303|PubMed:8413654, ECO:0000312|MGI:MGI:96982};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-28.
RC TISSUE=Pituitary;
RX PubMed=8413654; DOI=10.1038/365756a0;
RA Bernhagen J., Calandra T., Mitchell R.A., Martin S.B., Tracey K.J.,
RA Voelter W., Manogue K.R., Cerami A., Bucala R.;
RT "MIF is a pituitary-derived cytokine that potentiates lethal
RT endotoxaemia.";
RL Nature 365:756-759(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=1508193; DOI=10.1128/mcb.12.9.3919-3929.1992;
RA Lanahan A.A., Williams J.B., Sanders L.K., Nathans D.;
RT "Growth factor-induced delayed early response genes.";
RL Mol. Cell. Biol. 12:3919-3929(1992).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=7706726;
RA Mitchell R., Bacher M., Bernhagen J., Pushkarskaya T., Seldin M.F.,
RA Bucala R.;
RT "Cloning and characterization of the gene for mouse macrophage migration
RT inhibitory factor (MIF).";
RL J. Immunol. 154:3863-3870(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=7558021; DOI=10.1006/geno.1995.1071;
RA Bozza M., Kolakowski L.F. Jr., Jenkins N.A., Gilbert D.J., Copeland N.G.,
RA David J.R., Gerard C.;
RT "Structural characterization and chromosomal location of the mouse
RT macrophage migration inhibitory factor gene and pseudogenes.";
RL Genomics 27:412-419(1995).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=7558020; DOI=10.1006/geno.1995.1070;
RA Kozak C.A., Adamson M.C., Buckler C.E., Segovia L., Paralkar V., Wistow G.;
RT "Genomic cloning of mouse MIF (macrophage inhibitory factor) and genetic
RT mapping of the human and mouse expressed gene and nine mouse pseudogenes.";
RL Genomics 27:405-411(1995).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney, and Mammary gland;
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 [8]
RP PROTEIN SEQUENCE OF 2-12, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-115.
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 [10]
RP CHARACTERIZATION.
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 [11]
RP SUBCELLULAR LOCATION, AND ROLE OF TAUTOMERASE INHIBITORS IN IMPROVED
RP SURVIVAL IN CASE OF SEPSIS.
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 [12]
RP INTERACTION WITH CD74; CXCR2 AND COPS5, CATALYTIC ACTIVITY, ACTIVE SITE,
RP AND MUTAGENESIS OF PRO-2.
RX PubMed=19188446; DOI=10.1128/mcb.01907-08;
RA Fingerle-Rowson G., Kaleswarapu D.R., Schlander C., Kabgani N., Brocks T.,
RA Reinart N., Busch R., Schuetz A., Lue H., Du X., Liu A., Xiong H., Chen Y.,
RA Nemajerova A., Hallek M., Bernhagen J., Leng L., Bucala R.;
RT "A tautomerase-null macrophage migration-inhibitory factor (MIF) gene
RT knock-in mouse model reveals that protein interactions and not enzymatic
RT activity mediate MIF-dependent growth regulation.";
RL Mol. Cell. Biol. 29:1922-1932(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-78, SUCCINYLATION [LARGE SCALE
RP ANALYSIS] AT LYS-78, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=10360941; DOI=10.1021/bi9904048;
RA Taylor A.B., Johnson W.H. Jr., Czerwinski R.M., Li H.S., Hackert M.L.,
RA Whitman C.P.;
RT "Crystal structure of macrophage migration inhibitory factor complexed with
RT (E)-2-fluoro-p-hydroxycinnamate at 1.8 A resolution: implications for
RT enzymatic catalysis and inhibition.";
RL Biochemistry 38:7444-7452(1999).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), TAUTOMERASE ACTIVITY, IDENTIFICATION
RP BY MASS SPECTROMETRY, CLEAVAGE OF INITIATOR METHIONINE, ACTIVE SITE, AND
RP MUTAGENESIS OF PRO-2.
RX PubMed=10933783; DOI=10.1021/bi000373c;
RA Stamps S.L., Taylor A.B., Wang S.C., Hackert M.L., Whitman C.P.;
RT "Mechanism of the phenylpyruvate tautomerase activity of macrophage
RT migration inhibitory factor: properties of the P1G, P1A, Y95F, and N97A
RT mutants.";
RL Biochemistry 39:9671-9678(2000).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH INHIBITOR, FUNCTION,
RP CATALYTIC ACTIVITY, IDENTIFICATION BY MASS SPECTROMETRY, AND SUBUNIT.
RX PubMed=16780921; DOI=10.1016/j.bioorg.2006.05.001;
RA Golubkov P.A., Johnson W.H. Jr., Czerwinski R.M., Person M.D., Wang S.C.,
RA Whitman C.P., Hackert M.L.;
RT "Inactivation of the phenylpyruvate tautomerase activity of macrophage
RT migration inhibitory factor by 2-oxo-4-phenyl-3-butynoate.";
RL Bioorg. Chem. 34:183-199(2006).
CC -!- FUNCTION: Pro-inflammatory cytokine involved in the innate immune
CC response to bacterial pathogens (By similarity). The expression of MIF
CC at sites of inflammation suggests a role as mediator in regulating the
CC function of macrophages in host defense (By similarity). Counteracts
CC the anti-inflammatory activity of glucocorticoids (By similarity). Has
CC phenylpyruvate tautomerase and dopachrome tautomerase activity (in
CC vitro), but the physiological substrate is not known (PubMed:19188446,
CC PubMed:10933783, PubMed:16780921). It is not clear whether the
CC tautomerase activity has any physiological relevance, and whether it is
CC important for cytokine activit (PubMed:19188446, PubMed:10933783,
CC PubMed:16780921). {ECO:0000250|UniProtKB:P14174,
CC ECO:0000269|PubMed:10933783, ECO:0000269|PubMed:16780921,
CC ECO:0000269|PubMed:19188446}.
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:10933783, ECO:0000269|PubMed:16780921,
CC ECO:0000269|PubMed:19188446};
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:10933783,
CC ECO:0000269|PubMed:16780921, ECO:0000269|PubMed:19188446};
CC -!- SUBUNIT: Homotrimer (PubMed:16780921). Interacts with CD74 and CXCR2
CC extracellular domain and COPS5 (PubMed:19188446). Interacts with the
CC USO1 and BNIPL (By similarity). {ECO:0000250|UniProtKB:P14174,
CC ECO:0000269|PubMed:16780921, ECO:0000269|PubMed:19188446}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17526494,
CC ECO:0000269|PubMed:8234256}. Cytoplasm {ECO:0000250|UniProtKB:P14174}.
CC Note=Does not have a cleavable signal sequence and is secreted via a
CC specialized, non-classical pathway. Secreted by macrophages upon
CC stimulation by bacterial lipopolysaccharide (LPS), or by M.tuberculosis
CC antigens (By similarity). {ECO:0000250|UniProtKB:P14174}.
CC -!- SIMILARITY: Belongs to the MIF family. {ECO:0000305}.
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DR EMBL; Z23048; CAA80583.1; -; mRNA.
DR EMBL; U19825; AAA91637.1; -; Genomic_DNA.
DR EMBL; L10613; AAA37693.1; -; mRNA.
DR EMBL; U20156; AAA91638.1; -; Genomic_DNA.
DR EMBL; L39357; AAA74321.1; -; Genomic_DNA.
DR EMBL; BC024895; AAH24895.1; -; mRNA.
DR EMBL; BC086928; AAH86928.1; -; mRNA.
DR EMBL; L07607; AAA37111.1; -; mRNA.
DR CCDS; CCDS23934.1; -.
DR PIR; A44499; A44499.
DR RefSeq; NP_034928.1; NM_010798.2.
DR PDB; 1MFF; X-ray; 2.00 A; A/B/C=2-115.
DR PDB; 1MFI; X-ray; 1.80 A; A/B/C=2-115.
DR PDB; 2GDG; X-ray; 1.45 A; A/B/C=2-115.
DR PDBsum; 1MFF; -.
DR PDBsum; 1MFI; -.
DR PDBsum; 2GDG; -.
DR AlphaFoldDB; P34884; -.
DR SMR; P34884; -.
DR BioGRID; 201418; 6.
DR STRING; 10090.ENSMUSP00000041149; -.
DR BindingDB; P34884; -.
DR ChEMBL; CHEMBL1926491; -.
DR iPTMnet; P34884; -.
DR PhosphoSitePlus; P34884; -.
DR SwissPalm; P34884; -.
DR CPTAC; non-CPTAC-3842; -.
DR EPD; P34884; -.
DR jPOST; P34884; -.
DR PaxDb; P34884; -.
DR PeptideAtlas; P34884; -.
DR PRIDE; P34884; -.
DR ProteomicsDB; 292331; -.
DR TopDownProteomics; P34884; -.
DR ABCD; P34884; 10 sequenced antibodies.
DR Antibodypedia; 34865; 753 antibodies from 44 providers.
DR DNASU; 17319; -.
DR Ensembl; ENSMUST00000038169; ENSMUSP00000041149; ENSMUSG00000033307.
DR GeneID; 17319; -.
DR KEGG; mmu:17319; -.
DR UCSC; uc007ftc.1; mouse.
DR CTD; 4282; -.
DR MGI; MGI:96982; Mif.
DR VEuPathDB; HostDB:ENSMUSG00000033307; -.
DR eggNOG; KOG1759; Eukaryota.
DR GeneTree; ENSGT00940000155608; -.
DR HOGENOM; CLU_129906_1_1_1; -.
DR InParanoid; P34884; -.
DR OMA; YINFFDM; -.
DR OrthoDB; 1451925at2759; -.
DR PhylomeDB; P34884; -.
DR TreeFam; TF313853; -.
DR BRENDA; 5.3.2.1; 3474.
DR Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 17319; 7 hits in 55 CRISPR screens.
DR ChiTaRS; Mif; mouse.
DR EvolutionaryTrace; P34884; -.
DR PRO; PR:P34884; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P34884; protein.
DR Bgee; ENSMUSG00000033307; Expressed in endoderm of midgut and 295 other tissues.
DR ExpressionAtlas; P34884; baseline and differential.
DR Genevisible; P34884; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0042056; F:chemoattractant activity; ISO:MGI.
DR GO; GO:0005125; F:cytokine activity; IDA:BHF-UCL.
DR GO; GO:0005126; F:cytokine receptor binding; ISO:MGI.
DR GO; GO:0004167; F:dopachrome isomerase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0050178; F:phenylpyruvate tautomerase activity; IMP:MGI.
DR GO; GO:0002020; F:protease binding; IPI:BHF-UCL.
DR GO; GO:0019752; P:carboxylic acid metabolic process; ISO:MGI.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; ISO:MGI.
DR GO; GO:0090398; P:cellular senescence; IMP:MGI.
DR GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; IMP:MGI.
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:BHF-UCL.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
DR GO; GO:2000773; P:negative regulation of cellular senescence; ISO:MGI.
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; ISO:MGI.
DR GO; GO:1902166; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; ISO:MGI.
DR GO; GO:0010760; P:negative regulation of macrophage chemotaxis; ISO:MGI.
DR GO; GO:0002906; P:negative regulation of mature B cell apoptotic process; IDA:BHF-UCL.
DR GO; GO:0033033; P:negative regulation of myeloid cell apoptotic process; IMP:BHF-UCL.
DR GO; GO:0051248; P:negative regulation of protein metabolic process; IDA:BHF-UCL.
DR GO; GO:0002821; P:positive regulation of adaptive immune response; NAS:BHF-UCL.
DR GO; GO:0090238; P:positive regulation of arachidonic acid secretion; IDA:BHF-UCL.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:2000343; P:positive regulation of chemokine (C-X-C motif) ligand 2 production; IDA:BHF-UCL.
DR GO; GO:0001819; P:positive regulation of cytokine production; ISO:MGI.
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; IMP:BHF-UCL.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:BHF-UCL.
DR GO; GO:0061081; P:positive regulation of myeloid leukocyte cytokine production involved in immune response; IMP:BHF-UCL.
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; ISO:MGI.
DR GO; GO:0061078; P:positive regulation of prostaglandin secretion involved in immune response; IMP:BHF-UCL.
DR GO; GO:0010739; P:positive regulation of protein kinase A signaling; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:BHF-UCL.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:MGI.
DR GO; GO:0001516; P:prostaglandin biosynthetic process; ISO:MGI.
DR GO; GO:0070207; P:protein homotrimerization; ISO:MGI.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:MGI.
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:10933783,
FT ECO:0000269|PubMed:8413654, ECO:0000269|Ref.8"
FT CHAIN 2..115
FT /note="Macrophage migration inhibitory factor"
FT /id="PRO_0000158066"
FT ACT_SITE 2
FT /note="Proton acceptor; via imino nitrogen"
FT /evidence="ECO:0000269|PubMed:10933783,
FT ECO:0000269|PubMed:19188446"
FT BINDING 33
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16780921"
FT BINDING 65
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14174"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16780921"
FT MOD_RES 78
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 78
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MUTAGEN 2
FT /note="P->G: Loss of tautomerase activity, reduced
FT activation of intracellular signaling pathways, and reduced
FT interaction with CXCR2 and COPS5."
FT /evidence="ECO:0000269|PubMed:10933783,
FT ECO:0000269|PubMed:19188446"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:2GDG"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:2GDG"
FT HELIX 19..31
FT /evidence="ECO:0007829|PDB:2GDG"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:2GDG"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:2GDG"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:2GDG"
FT STRAND 58..66
FT /evidence="ECO:0007829|PDB:2GDG"
FT HELIX 70..88
FT /evidence="ECO:0007829|PDB:2GDG"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:2GDG"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:2GDG"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:2GDG"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:2GDG"
SQ SEQUENCE 115 AA; 12504 MW; 92D207B81B149945 CRC64;
MPMFIVNTNV PRASVPEGFL SELTQQLAQA TGKPAQYIAV HVVPDQLMTF SGTNDPCALC
SLHSIGKIGG AQNRNYSKLL CGLLSDRLHI SPDRVYINYY DMNAANVGWN GSTFA
