IFI2_MOUSE
ID IFI2_MOUSE Reviewed; 445 AA.
AC Q9R002; E9QLD9; P15091; Q38JF1; Q7TMN6; Q8VEL7;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Interferon-activable protein 202;
DE Short=Ifi-202;
DE AltName: Full=Interferon-inducible protein p202;
DE AltName: Full=Lupus susceptibility protein p202;
GN Name=Ifi202; Synonyms=Ifi202a, Ifi202b;
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].
RC STRAIN=AKR/J;
RX PubMed=2477366; DOI=10.1016/s0021-9258(18)71476-2;
RA Choubey D., Snoddy J., Chaturvedi V., Toniato E., Opdenakker G., Thakur A.,
RA Samanta H., Engel D.A., Lengyel P.;
RT "Interferons as gene activators. Indications for repeated gene duplication
RT during the evolution of a cluster of interferon-activatable genes on murine
RT chromosome 1.";
RL J. Biol. Chem. 264:17182-17189(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=129/Sv;
RX PubMed=10493828; DOI=10.1006/geno.1999.5923;
RA Wang H., Chatterjee G., Meyer J.J., Liu C.J., Manjunath N.A., Bray-Ward P.,
RA Lengyel P.;
RT "Characteristics of three homologous 202 genes (Ifi202a, ifi202b, and
RT ifi202c) from the murine interferon-activatable gene 200 cluster.";
RL Genomics 60:281-294(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=NZB;
RA Chen J., Choubey D.;
RT "Coding cDNA sequence for p202 in New Zealand Black mice.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
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 [6]
RP MUTAGENESIS OF HIS-84 AND HIS-283.
RX PubMed=8910340; DOI=10.1074/jbc.271.44.27544;
RA Datta B., Li B., Choubey D., Nallur G., Lengyel P.;
RT "p202, an interferon-inducible modulator of transcription, inhibits
RT transcriptional activation by the p53 tumor suppressor protein, and a
RT segment from the p53-binding protein 1 that binds to p202 overcomes this
RT inhibition.";
RL J. Biol. Chem. 271:27544-27555(1996).
RN [7]
RP POLYMORPHISM.
RX PubMed=11567633; DOI=10.1016/s1074-7613(01)00196-0;
RA Rozzo S.J., Allard J.D., Choubey D., Vyse T.J., Izui S., Peltz G.,
RA Kotzin B.L.;
RT "Evidence for an interferon-inducible gene, Ifi202, in the susceptibility
RT to systemic lupus.";
RL Immunity 15:435-443(2001).
RN [8]
RP INDUCTION BY IL6.
RX PubMed=14764608; DOI=10.1074/jbc.m313140200;
RA Pramanik R., Jorgensen T.N., Xin H., Kotzin B.L., Choubey D.;
RT "Interleukin-6 induces expression of Ifi202, an interferon-inducible
RT candidate gene for lupus susceptibility.";
RL J. Biol. Chem. 279:16121-16127(2004).
RN [9]
RP FUNCTION, AND INTERACTION WITH TP53.
RX PubMed=16670293; DOI=10.4049/jimmunol.176.10.5863;
RA Xin H., D'Souza S., Jorgensen T.N., Vaughan A.T., Lengyel P., Kotzin B.L.,
RA Choubey D.;
RT "Increased expression of Ifi202, an IFN-activatable gene, in B6.Nba2 lupus
RT susceptible mice inhibits p53-mediated apoptosis.";
RL J. Immunol. 176:5863-5870(2006).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19131592; DOI=10.1126/science.1169841;
RA Roberts T.L., Idris A., Dunn J.A., Kelly G.M., Burnton C.M., Hodgson S.,
RA Hardy L.L., Garceau V., Sweet M.J., Ross I.L., Hume D.A., Stacey K.J.;
RT "HIN-200 proteins regulate caspase activation in response to foreign
RT cytoplasmic DNA.";
RL Science 323:1057-1060(2009).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.69 ANGSTROMS) OF 46-242 IN COMPLEX WITH DNA,
RP FUNCTION, DOMAIN, MUTAGENESIS OF LYS-48; LYS-53; GLY-54; LYS-76; LYS-79;
RP SER-166; 182-ASN--SER-185; THR-187; LYS-189; LYS-198; 222-HIS--ARG-224;
RP GLY-226; ASN-227; LYS-229 AND ASN-236, AND DNA BINDING.
RX PubMed=23567559; DOI=10.1038/cr.2013.52;
RA Ru H., Ni X., Zhao L., Crowley C., Ding W., Hung L.W., Shaw N., Cheng G.,
RA Liu Z.J.;
RT "Structural basis for termination of AIM2-mediated signaling by p202.";
RL Cell Res. 23:855-858(2013).
CC -!- FUNCTION: Inhibits the transcriptional activity of several
CC transcription factors, including NF-kappa-B p50 and p65, FOS, JUN,
CC E2F1, E2F4, MYOD1 and myogenin. Has anti-apoptotic effects due to
CC inhibition of the transcriptional activity of p53. Binds dsDNA in the
CC cytosol. Is involved in innate immune response and has anti-
CC inflammatory activity. Inhibits caspase activation in response to
CC cytosolic DNA and inhibits the activation of the AIM2 inflammasome,
CC probably by sequestering cytoplasmic DNA and preventing its being bound
CC by AIM2. {ECO:0000269|PubMed:16670293, ECO:0000269|PubMed:19131592,
CC ECO:0000269|PubMed:23567559}.
CC -!- SUBUNIT: Binds to several transcription factors, including NF-kappa-B
CC p50 and p65, FOS, JUN, E2F1, E2F4, MYOD1 and myogenin. Also binds p53,
CC the hypophosphorylated, growth-inhibitory form of the retinoblastoma
CC protein and the p53-binding protein 1 (53BP1).
CC {ECO:0000269|PubMed:23567559}.
CC -!- INTERACTION:
CC Q9R002; P13405: Rb1; NbExp=7; IntAct=EBI-3043899, EBI-971782;
CC Q9R002; P06400: RB1; Xeno; NbExp=5; IntAct=EBI-3043899, EBI-491274;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19131592}. Nucleus
CC {ECO:0000269|PubMed:19131592}. Note=Accumulates first in the cytoplasm,
CC and is translocated to the nucleus after a delay, where it is primarily
CC chromatin-associated.
CC -!- INDUCTION: By beta interferon. By IL6 in splenocytes (at protein
CC level). {ECO:0000269|PubMed:14764608}.
CC -!- DOMAIN: The HIN-20 domains mediate dsDNA binding via electrostatic
CC interactions. {ECO:0000269|PubMed:23567559}.
CC -!- PTM: Phosphorylated.
CC -!- POLYMORPHISM: NZB mice express 10 to 100 fold more Ifi202 in spleen
CC than B6 or NZW mice. This could account for the high susceptibility of
CC NZB mice to systemic lupus.
CC -!- SIMILARITY: Belongs to the HIN-200 family. {ECO:0000305}.
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DR EMBL; M31418; AAA39312.1; -; mRNA.
DR EMBL; AF140672; AAF04260.1; -; mRNA.
DR EMBL; DQ222946; ABB00055.1; -; mRNA.
DR EMBL; AC170584; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC018233; AAH18233.1; -; mRNA.
DR EMBL; BC055888; AAH55888.1; -; mRNA.
DR CCDS; CCDS35794.1; -.
DR PIR; A34457; A34457.
DR RefSeq; NP_032353.2; NM_008327.2.
DR RefSeq; NP_036070.2; NM_011940.2.
DR RefSeq; XP_006536966.1; XM_006536903.2.
DR PDB; 4JBJ; X-ray; 2.69 A; A/B=46-242.
DR PDB; 4JBK; X-ray; 2.96 A; A/B/C/D=46-242.
DR PDB; 4L5Q; X-ray; 2.23 A; A=46-243.
DR PDB; 4L5R; X-ray; 1.87 A; C=46-243.
DR PDB; 4L5S; X-ray; 2.94 A; A/B=46-243.
DR PDB; 4L5T; X-ray; 3.40 A; A/B/C/D=244-445.
DR PDB; 4LNQ; X-ray; 2.00 A; A/B=53-245.
DR PDBsum; 4JBJ; -.
DR PDBsum; 4JBK; -.
DR PDBsum; 4L5Q; -.
DR PDBsum; 4L5R; -.
DR PDBsum; 4L5S; -.
DR PDBsum; 4L5T; -.
DR PDBsum; 4LNQ; -.
DR AlphaFoldDB; Q9R002; -.
DR SMR; Q9R002; -.
DR BioGRID; 204945; 4.
DR ELM; Q9R002; -.
DR IntAct; Q9R002; 3.
DR STRING; 10090.ENSMUSP00000000266; -.
DR iPTMnet; Q9R002; -.
DR PhosphoSitePlus; Q9R002; -.
DR MaxQB; Q9R002; -.
DR PaxDb; Q9R002; -.
DR PRIDE; Q9R002; -.
DR ProteomicsDB; 267198; -.
DR DNASU; 26388; -.
DR Ensembl; ENSMUST00000000266; ENSMUSP00000000266; ENSMUSG00000026535.
DR GeneID; 26388; -.
DR KEGG; mmu:26388; -.
DR UCSC; uc007dsk.2; mouse.
DR CTD; 26388; -.
DR MGI; MGI:1347080; Ifi202a.
DR MGI; MGI:1347083; Ifi202b.
DR VEuPathDB; HostDB:ENSMUSG00000026535; -.
DR eggNOG; ENOG502QTQS; Eukaryota.
DR GeneTree; ENSGT00390000013296; -.
DR HOGENOM; CLU_615313_0_0_1; -.
DR InParanoid; Q9R002; -.
DR OMA; CEIGNTI; -.
DR OrthoDB; 1304994at2759; -.
DR PhylomeDB; Q9R002; -.
DR TreeFam; TF337385; -.
DR BioGRID-ORCS; 26388; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Ifi202b; mouse.
DR PRO; PR:Q9R002; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9R002; protein.
DR Bgee; ENSMUSG00000026535; Expressed in conjunctival fornix and 122 other tissues.
DR Genevisible; Q9R002; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0002218; P:activation of innate immune response; IBA:GO_Central.
DR GO; GO:0035458; P:cellular response to interferon-beta; IDA: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:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
DR GO; GO:0045824; P:negative regulation of innate immune response; TAS:UniProtKB.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IBA:GO_Central.
DR GO; GO:0009617; P:response to bacterium; IBA:GO_Central.
DR Gene3D; 2.40.50.140; -; 4.
DR InterPro; IPR040205; HIN-200.
DR InterPro; IPR004021; HIN200/IF120x.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR PANTHER; PTHR12200; PTHR12200; 2.
DR Pfam; PF02760; HIN; 2.
DR PROSITE; PS50834; HIN_200; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA-binding; Immunity; Inflammatory response;
KW Innate immunity; Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..445
FT /note="Interferon-activable protein 202"
FT /id="PRO_0000153719"
FT DOMAIN 46..243
FT /note="HIN-200 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00106"
FT DOMAIN 244..441
FT /note="HIN-200 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00106"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 84
FT /note="Mediates interaction with 53BP1"
FT SITE 283
FT /note="Mediates interaction with 53BP1"
FT MUTAGEN 48
FT /note="K->A: Strongly reduces affinity for DNA; when
FT associated with A-53 and W-54."
FT /evidence="ECO:0000269|PubMed:23567559"
FT MUTAGEN 53
FT /note="K->A: Strongly reduces affinity for DNA; when
FT associated with A-48 and W-54."
FT /evidence="ECO:0000269|PubMed:23567559"
FT MUTAGEN 54
FT /note="G->W: Strongly reduces affinity for DNA; when
FT associated with A-48 and A-53."
FT /evidence="ECO:0000269|PubMed:23567559"
FT MUTAGEN 76
FT /note="K->A: Strongly reduces affinity for DNA; when
FT associated with A-79 and A-236."
FT /evidence="ECO:0000269|PubMed:23567559"
FT MUTAGEN 79
FT /note="K->A: Strongly reduces affinity for DNA; when
FT associated with A-76 and A-236."
FT /evidence="ECO:0000269|PubMed:23567559"
FT MUTAGEN 84
FT /note="H->F: Loss of interaction with 53BP1; when
FT associated with F-283."
FT /evidence="ECO:0000269|PubMed:8910340"
FT MUTAGEN 166
FT /note="S->A: Strongly reduces affinity for DNA; when
FT associated with."
FT /evidence="ECO:0000269|PubMed:23567559"
FT MUTAGEN 182..185
FT /note="NDKS->ADAA: Strongly reduces affinity for DNA."
FT /evidence="ECO:0000269|PubMed:23567559"
FT MUTAGEN 187
FT /note="T->A: Strongly reduces affinity for DNA; when
FT associated with A-189 and A-198."
FT /evidence="ECO:0000269|PubMed:23567559"
FT MUTAGEN 189
FT /note="K->A: Strongly reduces affinity for DNA; when
FT associated with A-187 and A-198."
FT /evidence="ECO:0000269|PubMed:23567559"
FT MUTAGEN 198
FT /note="K->A: Strongly reduces affinity for DNA; when
FT associated with A-187 and A-189."
FT /evidence="ECO:0000269|PubMed:23567559"
FT MUTAGEN 222..224
FT /note="HLR->ALA: Strongly reduces affinity for DNA."
FT /evidence="ECO:0000269|PubMed:23567559"
FT MUTAGEN 226
FT /note="G->W: Strongly reduces affinity for DNA; when
FT associated with A-166; A-227 and A-229."
FT /evidence="ECO:0000269|PubMed:23567559"
FT MUTAGEN 227
FT /note="N->A: Strongly reduces affinity for DNA; when
FT associated with A-166; W-226 and A-229."
FT /evidence="ECO:0000269|PubMed:23567559"
FT MUTAGEN 229
FT /note="K->A: Strongly reduces affinity for DNA; when
FT associated with A-166; W-226 and A-227."
FT /evidence="ECO:0000269|PubMed:23567559"
FT MUTAGEN 236
FT /note="N->A: Strongly reduces affinity for DNA; when
FT associated with A-76 and A-79."
FT /evidence="ECO:0000269|PubMed:23567559"
FT MUTAGEN 283
FT /note="H->F: Loss of interaction with 53BP1; when
FT associated with F-84."
FT /evidence="ECO:0000269|PubMed:8910340"
FT CONFLICT 13..15
FT /note="EFS -> DLA (in Ref. 2; AAF04260 and 5; AAH55888)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="K -> N (in Ref. 3; ABB00055)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="Q -> K (in Ref. 2; AAF04260 and 5; AAH18233)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="E -> G (in Ref. 3; ABB00055)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="K -> Q (in Ref. 5; AAH18233)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="I -> F (in Ref. 3; ABB00055)"
FT /evidence="ECO:0000305"
FT CONFLICT 141..142
FT /note="II -> MF (in Ref. 1; AAA39312, 2; AAF04260, 3;
FT ABB00055 and 5; AAH18233/AAH55888)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="T -> I (in Ref. 3; ABB00055)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="I -> V (in Ref. 3; ABB00055)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="K -> E (in Ref. 1; AAA39312, 2; AAF04260, 3;
FT ABB00055 and 5; AAH18233/AAH55888)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="I -> V (in Ref. 2; AAF04260)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="L -> P (in Ref. 1; AAA39312, 2; AAF04260, 3;
FT ABB00055 and 5; AAH18233/AAH55888)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="K -> E (in Ref. 1; AAA39312, 2; AAF04260, 3;
FT ABB00055 and 5; AAH18233/AAH55888)"
FT /evidence="ECO:0000305"
FT CONFLICT 368
FT /note="V -> F (in Ref. 1; AAA39312)"
FT /evidence="ECO:0000305"
FT CONFLICT 379
FT /note="T -> S (in Ref. 1; AAA39312, 2; AAF04260, 3;
FT ABB00055 and 5; AAH18233/AAH55888)"
FT /evidence="ECO:0000305"
FT CONFLICT 432
FT /note="S -> A (in Ref. 1; AAA39312, 2; AAF04260, 3;
FT ABB00055 and 5; AAH18233/AAH55888)"
FT /evidence="ECO:0000305"
FT TURN 47..50
FT /evidence="ECO:0007829|PDB:4L5R"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:4L5R"
FT STRAND 62..69
FT /evidence="ECO:0007829|PDB:4L5R"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:4L5R"
FT TURN 76..79
FT /evidence="ECO:0007829|PDB:4L5R"
FT STRAND 80..88
FT /evidence="ECO:0007829|PDB:4L5R"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:4L5R"
FT HELIX 101..106
FT /evidence="ECO:0007829|PDB:4L5R"
FT STRAND 112..121
FT /evidence="ECO:0007829|PDB:4L5R"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:4L5R"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:4L5R"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:4L5R"
FT HELIX 146..153
FT /evidence="ECO:0007829|PDB:4L5R"
FT HELIX 158..161
FT /evidence="ECO:0007829|PDB:4L5R"
FT STRAND 169..181
FT /evidence="ECO:0007829|PDB:4L5R"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:4L5R"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:4L5R"
FT TURN 211..213
FT /evidence="ECO:0007829|PDB:4L5S"
FT STRAND 216..224
FT /evidence="ECO:0007829|PDB:4L5R"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:4L5R"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:4L5R"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:4L5R"
FT STRAND 253..256
FT /evidence="ECO:0007829|PDB:4L5T"
FT STRAND 260..267
FT /evidence="ECO:0007829|PDB:4L5T"
FT STRAND 271..274
FT /evidence="ECO:0007829|PDB:4L5T"
FT TURN 275..278
FT /evidence="ECO:0007829|PDB:4L5T"
FT STRAND 279..287
FT /evidence="ECO:0007829|PDB:4L5T"
FT STRAND 289..297
FT /evidence="ECO:0007829|PDB:4L5T"
FT HELIX 300..306
FT /evidence="ECO:0007829|PDB:4L5T"
FT STRAND 311..314
FT /evidence="ECO:0007829|PDB:4L5T"
FT STRAND 316..320
FT /evidence="ECO:0007829|PDB:4L5T"
FT STRAND 323..326
FT /evidence="ECO:0007829|PDB:4L5T"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:4L5T"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:4L5T"
FT HELIX 356..361
FT /evidence="ECO:0007829|PDB:4L5T"
FT STRAND 368..379
FT /evidence="ECO:0007829|PDB:4L5T"
FT STRAND 381..389
FT /evidence="ECO:0007829|PDB:4L5T"
FT STRAND 395..399
FT /evidence="ECO:0007829|PDB:4L5T"
FT HELIX 401..405
FT /evidence="ECO:0007829|PDB:4L5T"
FT STRAND 413..422
FT /evidence="ECO:0007829|PDB:4L5T"
FT STRAND 429..441
FT /evidence="ECO:0007829|PDB:4L5T"
SQ SEQUENCE 445 AA; 50466 MW; 5EA0E93E143C58EA CRC64;
MSNRNLRSST NSEFSEGQHQ TPSSDSSGHG EDQPQASPGP NKKSHTPKKN ISKGAVLHEK
PMTVMVLTAT EPFNYKEGKE NMFHATVATE SQYYRVKVFN MDLKEKFTEN KFITISKYFN
SSGILEINET ATVSEAAPNQ IIEVPKNIIR SAKETLKISK IKELDSGTLI YGVFAVEKKK
VNDKSITFKI KDNEDNIKVV WDKKQHNINY EKGDKLQLFS FHLRKGNGKP ILHSGNHSFI
KGEKLLKESF EGDGYHKGPK QVVALKATKL FTYDSIKSKK MFHATVATDT EFFRVMVFEE
NLEKKFIPGN TIALSDYFGM YGSLAIHEYS SVSEVKSQNK EDSSSSDERL IEHLKICDLH
LQTKERLVDG EFKVYRKSTG NNCICYGIWD DTGAMKVVVS GQLTSVNCEI GNTIRLVCFE
LTSNADEWFL RSTRYSYMEV IMPEK
