ID   ILRUN_HUMAN             Reviewed;         298 AA.
AC   Q9H6K1; B2R8K7; Q5VV77; Q96MG5; Q9BUR9;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 2.
DT   13-SEP-2023, entry version 147.
DE   RecName: Full=Protein ILRUN {ECO:0000305};
DE   AltName: Full=Inflammation and lipid regulator with UBA-like and NBR1-like domains protein {ECO:0000312|HGNC:HGNC:21215};
GN   Name=ILRUN {ECO:0000312|HGNC:HGNC:21215};
GN   Synonyms=C6orf106 {ECO:0000312|HGNC:HGNC:21215};
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Skeletal muscle, and Uterus;
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   [2]
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Placenta, 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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215 AND SER-272, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215; SER-222 AND SER-272, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and 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   [11]
RP   TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=25736925; DOI=10.1007/s13277-015-3274-9;
RA   Zhang X., Miao Y., Yu X., Zhang Y., Jiang G., Liu Y., Yu J., Han Q.,
RA   Zhao H., Wang E.;
RT   "C6orf106 enhances NSCLC cell invasion by upregulating vimentin, and
RT   downregulating E-cadherin and P120ctn.";
RL   Tumor Biol. 36:5979-5985(2015).
RN   [12]
RP   FUNCTION, INDUCTION BY DSRNA, INTERACTION WITH IRF3, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=29802199; DOI=10.1074/jbc.ra117.001491;
RA   Ambrose R.L., Liu Y.C., Adams T.E., Bean A.G.D., Stewart C.R.;
RT   "C6orf106 is a novel inhibitor of the interferon-regulatory factor 3-
RT   dependent innate antiviral response.";
RL   J. Biol. Chem. 293:10561-10573(2018).
CC   -!- FUNCTION: Negative regulator of innate antiviral response. Blocks IRF3-
CC       dependent cytokine production such as IFNA, IFNB and TNF
CC       (PubMed:29802199). Interacts with IRF3 and inhibits IRF3 recruitment to
CC       type I IFN promoter sequences while also reducing nuclear levels of the
CC       coactivators EP300 and CREBBP (PubMed:29802199).
CC       {ECO:0000269|PubMed:29802199}.
CC   -!- SUBUNIT: Interacts with IRF3; the interaction inhibits IRF3 binding to
CC       its DNA consensus sequence. {ECO:0000269|PubMed:29802199}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25736925,
CC       ECO:0000269|PubMed:29802199}. Nucleus {ECO:0000269|PubMed:29802199}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9H6K1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9H6K1-2; Sequence=VSP_017259;
CC   -!- TISSUE SPECIFICITY: Expressed in lung (at protein level).
CC       {ECO:0000269|PubMed:25736925}.
CC   -!- INDUCTION: Expression is icreased in presence of dsRNA such as
CC       poly(I:C). {ECO:0000269|PubMed:29802199}.
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DR   EMBL; AK025848; BAB15258.1; ALT_SEQ; mRNA.
DR   EMBL; AK056964; BAB71327.1; -; mRNA.
DR   EMBL; AK313410; BAG36204.1; -; mRNA.
DR   EMBL; AL031577; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL451165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471081; EAX03790.1; -; Genomic_DNA.
DR   EMBL; BC002328; AAH02328.1; -; mRNA.
DR   EMBL; BC010184; AAH10184.1; -; mRNA.
DR   EMBL; BC075810; AAH75810.1; -; mRNA.
DR   CCDS; CCDS4795.1; -. [Q9H6K1-2]
DR   CCDS; CCDS4796.1; -. [Q9H6K1-1]
DR   RefSeq; NP_073595.2; NM_022758.5. [Q9H6K1-2]
DR   RefSeq; NP_077270.1; NM_024294.3. [Q9H6K1-1]
DR   PDB; 6VHI; X-ray; 2.46 A; A=64-185.
DR   PDBsum; 6VHI; -.
DR   AlphaFoldDB; Q9H6K1; -.
DR   SMR; Q9H6K1; -.
DR   BioGRID; 122282; 18.
DR   IntAct; Q9H6K1; 8.
DR   STRING; 9606.ENSP00000363135; -.
DR   GlyGen; Q9H6K1; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q9H6K1; -.
DR   PhosphoSitePlus; Q9H6K1; -.
DR   BioMuta; C6orf106; -.
DR   DMDM; 88984085; -.
DR   EPD; Q9H6K1; -.
DR   jPOST; Q9H6K1; -.
DR   MassIVE; Q9H6K1; -.
DR   MaxQB; Q9H6K1; -.
DR   PaxDb; Q9H6K1; -.
DR   PeptideAtlas; Q9H6K1; -.
DR   ProteomicsDB; 80993; -. [Q9H6K1-1]
DR   ProteomicsDB; 80994; -. [Q9H6K1-2]
DR   Antibodypedia; 49290; 82 antibodies from 16 providers.
DR   DNASU; 64771; -.
DR   Ensembl; ENST00000374023.8; ENSP00000363135.3; ENSG00000196821.10. [Q9H6K1-1]
DR   Ensembl; ENST00000374026.7; ENSP00000363138.3; ENSG00000196821.10. [Q9H6K1-2]
DR   GeneID; 64771; -.
DR   KEGG; hsa:64771; -.
DR   MANE-Select; ENST00000374023.8; ENSP00000363135.3; NM_024294.4; NP_077270.1.
DR   UCSC; uc003ojr.4; human. [Q9H6K1-1]
DR   AGR; HGNC:21215; -.
DR   CTD; 64771; -.
DR   DisGeNET; 64771; -.
DR   GeneCards; ILRUN; -.
DR   HGNC; HGNC:21215; ILRUN.
DR   HPA; ENSG00000196821; Tissue enhanced (skeletal).
DR   MIM; 612217; gene.
DR   neXtProt; NX_Q9H6K1; -.
DR   OpenTargets; ENSG00000196821; -.
DR   PharmGKB; PA134935866; -.
DR   VEuPathDB; HostDB:ENSG00000196821; -.
DR   eggNOG; KOG4351; Eukaryota.
DR   GeneTree; ENSGT00490000043415; -.
DR   HOGENOM; CLU_076188_1_0_1; -.
DR   InParanoid; Q9H6K1; -.
DR   OMA; NWNVETA; -.
DR   OrthoDB; 145583at2759; -.
DR   PhylomeDB; Q9H6K1; -.
DR   TreeFam; TF105872; -.
DR   PathwayCommons; Q9H6K1; -.
DR   SignaLink; Q9H6K1; -.
DR   BioGRID-ORCS; 64771; 18 hits in 1121 CRISPR screens.
DR   ChiTaRS; C6orf106; human.
DR   GenomeRNAi; 64771; -.
DR   Pharos; Q9H6K1; Tbio.
DR   PRO; PR:Q9H6K1; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q9H6K1; Protein.
DR   Bgee; ENSG00000196821; Expressed in gastrocnemius and 204 other tissues.
DR   ExpressionAtlas; Q9H6K1; baseline and differential.
DR   Genevisible; Q9H6K1; HS.
DR   GO; GO:0005813; C:centrosome; IDA:HPA.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0000407; C:phagophore assembly site; IBA:GO_Central.
DR   GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0016236; P:macroautophagy; IBA:GO_Central.
DR   GO; GO:0050687; P:negative regulation of defense response to virus; IMP:UniProtKB.
DR   GO; GO:0043392; P:negative regulation of DNA binding; IDA:UniProtKB.
DR   GO; GO:1900181; P:negative regulation of protein localization to nucleus; IMP:UniProtKB.
DR   GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IMP:UniProtKB.
DR   GO; GO:0032480; P:negative regulation of type I interferon production; IMP:UniProtKB.
DR   CDD; cd14947; NBR1_like; 1.
DR   CDD; cd14349; UBA_CF106; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR039517; C6orf106_UBA-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR032350; N_BRCA1_central.
DR   InterPro; IPR009060; UBA-like_sf.
DR   PANTHER; PTHR20930; OVARIAN CARCINOMA ANTIGEN CA125-RELATED; 1.
DR   PANTHER; PTHR20930:SF0; PROTEIN ILRUN; 1.
DR   Pfam; PF16158; N_BRCA1_IG; 1.
DR   Pfam; PF14555; UBA_4; 1.
DR   SUPFAM; SSF46934; UBA-like; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytoplasm; Immunity; Innate immunity;
KW   Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..298
FT                   /note="Protein ILRUN"
FT                   /id="PRO_0000089519"
FT   REGION          199..277
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        199..221
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        254..277
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         215
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         222
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         272
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         105..170
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_017259"
FT   CONFLICT        54
FT                   /note="N -> S (in Ref. 1; BAB71327)"
FT                   /evidence="ECO:0000305"
FT   STRAND          76..83
FT                   /evidence="ECO:0007829|PDB:6VHI"
FT   STRAND          94..102
FT                   /evidence="ECO:0007829|PDB:6VHI"
FT   STRAND          105..107
FT                   /evidence="ECO:0007829|PDB:6VHI"
FT   STRAND          114..120
FT                   /evidence="ECO:0007829|PDB:6VHI"
FT   STRAND          128..130
FT                   /evidence="ECO:0007829|PDB:6VHI"
FT   STRAND          139..147
FT                   /evidence="ECO:0007829|PDB:6VHI"
FT   STRAND          153..162
FT                   /evidence="ECO:0007829|PDB:6VHI"
FT   STRAND          168..179
FT                   /evidence="ECO:0007829|PDB:6VHI"
SQ   SEQUENCE   298 AA;  32872 MW;  3BA3E7F7B4D26D76 CRC64;
     MEGMDVDLDP ELMQKFSCLG TTDKDVLISE FQRLLGFQLN PAGCAFFLDM TNWNLQAAIG
     AYYDFESPNI SVPSMSFVED VTIGEGESIP PDTQFVKTWR IQNSGAEAWP PGVCLKYVGG
     DQFGHVNMVM VRSLEPQEIA DVSVQMCSPS RAGMYQGQWR MCTATGLYYG DVIWVILSVE
     VGGLLGVTQQ LSSFETEFNT QPHRKVEGNF NPFASPQKNR QSDENNLKDP GGSEFDSISK
     NTWAPAPDTW APAPDQTEQD QNRLSQNSVN LSPSSHANNL SVVTYSKGLH GPYPFGQS
//