CHIL3_MOUSE
ID CHIL3_MOUSE Reviewed; 398 AA.
AC O35744; P70201; Q3U462; Q3UV87; Q61201;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Chitinase-like protein 3;
DE EC=3.2.1.52;
DE AltName: Full=Beta-N-acetylhexosaminidase Ym1;
DE AltName: Full=Chitinase-3-like protein 3;
DE AltName: Full=ECF-L;
DE AltName: Full=Eosinophil chemotactic cytokine;
DE AltName: Full=Secreted protein Ym1;
DE Flags: Precursor;
GN Name=Chil3; Synonyms=Chi3l3, Ym1;
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 [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=129/SvJ;
RX PubMed=9828134; DOI=10.1006/geno.1998.5593;
RA Jin H.M., Copeland N.G., Gilbert D.J., Jenkins N.A., Kirkpatrick R.B.,
RA Rosenberg M.;
RT "Genetic characterization of the murine Ym1 gene and identification of a
RT cluster of highly homologous genes.";
RL Genomics 54:316-322(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-39, FUNCTION, TISSUE
RP SPECIFICITY, AND INDUCTION.
RC TISSUE=Bone marrow;
RX PubMed=10625674; DOI=10.1074/jbc.275.2.1279;
RA Owhashi M., Arita H., Hayai N.;
RT "Identification of a novel eosinophil chemotactic cytokine (ECF-L) as a
RT chitinase family protein.";
RL J. Biol. Chem. 275:1279-1286(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-48; 109-134; 162-192 AND
RP 210-225, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=Macrophage;
RX PubMed=11297523; DOI=10.1074/jbc.m010417200;
RA Chang N.-C.A., Hung S.-I., Hwa K.-Y., Kato I., Chen J.-E., Liu C.-H.,
RA Chang A.C.;
RT "A macrophage protein, Ym1, transiently expressed during inflammation is a
RT novel mammalian lectin.";
RL J. Biol. Chem. 276:17497-17506(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Bone, and Dendritic cell;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart, and Lung;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 139-398.
RC STRAIN=CBA/J; TISSUE=Bone marrow;
RA Shmelkov S.V., Zinovjeva M.V., Belyavsky A.V.;
RT "Mouse chitinase-related protein mRNA (MCRP), partial cds.";
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11733538; DOI=10.1074/jbc.m110635200;
RA Harbord M., Novelli M., Canas B., Power D., Davis C.,
RA Godovac-Zimmermann J., Roes J., Segal A.W.;
RT "Ym1 is a neutrophil granule protein that crystallizes in p47phox-deficient
RT mice.";
RL J. Biol. Chem. 277:5468-5475(2002).
RN [8]
RP INDUCTION BY IL3 AND IL4.
RX PubMed=12215441; DOI=10.1074/jbc.m205873200;
RA Welch J.S., Escoubet-Lozach L., Sykes D.B., Liddiard K., Greaves D.R.,
RA Glass C.K.;
RT "TH2 cytokines and allergic challenge induce Ym1 expression in macrophages
RT by a STAT6-dependent mechanism.";
RL J. Biol. Chem. 277:42821-42829(2002).
RN [9]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=12101265;
RA Hung S.I., Chang A.C., Kato I., Chang N.C.;
RT "Transient expression of Ym1, a heparin-binding lectin, during
RT developmental hematopoiesis and inflammation.";
RL J. Leukoc. Biol. 72:72-82(2002).
RN [10]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15148607; DOI=10.1007/s00418-004-0654-4;
RA Nio J., Fujimoto W., Konno A., Kon Y., Owhashi M., Iwanaga T.;
RT "Cellular expression of murine Ym1 and Ym2, chitinase family proteins, as
RT revealed by in situ hybridization and immunohistochemistry.";
RL Histochem. Cell Biol. 121:473-482(2004).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, and Spleen;
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 [12]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 22-398, AND DISULFIDE BONDS.
RX PubMed=11278670; DOI=10.1074/jbc.m010416200;
RA Sun Y.-J., Chang N.-C.A., Hung S.-I., Chang A.C., Chou C.-C., Hsiao C.-D.;
RT "The crystal structure of a novel mammalian lectin, Ym1, suggests a
RT saccharide binding site.";
RL J. Biol. Chem. 276:17507-17514(2001).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.31 ANGSTROMS) OF 22-398, AND DISULFIDE BONDS.
RX PubMed=15522777; DOI=10.1016/j.jsb.2004.07.002;
RA Tsai M.L., Liaw S.H., Chang N.C.;
RT "The crystal structure of Ym1 at 1.31 A resolution.";
RL J. Struct. Biol. 148:290-296(2004).
CC -!- FUNCTION: Lectin that binds saccharides with a free amino group, such
CC as glucosamine or galactosamine. Binding to oligomeric saccharides is
CC much stronger than binding to mono- or disaccharides. Also binds chitin
CC and heparin. Has weak hexosaminidase activity but no chitinase
CC activity. Has chemotactic activity for T-lymphocytes, bone marrow cells
CC and eosinophils. May play a role in inflammation and allergy.
CC {ECO:0000269|PubMed:10625674, ECO:0000269|PubMed:11297523,
CC ECO:0000269|PubMed:11733538}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine
CC residues in N-acetyl-beta-D-hexosaminides.; EC=3.2.1.52;
CC Evidence={ECO:0000269|PubMed:11733538};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=120.8 uM for 4-methylumbelliferone-N-acetylglucosamine (at pH 4-
CC 4.5) {ECO:0000269|PubMed:11733538};
CC Vmax=0.023 umol/min/mg enzyme {ECO:0000269|PubMed:11733538};
CC Note=4-methylumbelliferone-N-acetylglucosamine (MU-(GlcNAc)1) is a
CC GlcNAc2 analog.;
CC pH dependence:
CC Optimum pH is 4.5-5.0. {ECO:0000269|PubMed:11733538};
CC -!- SUBCELLULAR LOCATION: Secreted. Rough endoplasmic reticulum lumen.
CC Nucleus envelope. Cytoplasm. Cytoplasmic granule. Note=Predominantly
CC localizes to the lumen of rough endoplasmic reticulum (rER) and nuclear
CC envelope in alveolar macrophages. Localizes to the dilated lumen of rER
CC in immature neutrophils in spleen and in cytoplasmic granules in
CC peritoneal neutrophils. Detected in needle-shaped crystals present in
CC the cytoplasm of bone marrow macrophages.
CC -!- TISSUE SPECIFICITY: Expressed in peritoneal cavity macrophages and in
CC peritoneal and bone marrow-derived neutrophils. Abundantly expressed in
CC bone marrow, with moderate levels detected in gastric antrum, spleen
CC and in alveolar macrophages in lung. Not detected in brain, heart,
CC liver, kidney, stomach, intestine, skeletal muscle, ovary, testis,
CC thymus and lymph nodes (at protein level). Detected at low levels in
CC bone marrow, spleen, thymus and lung. Barely detectable in intestine,
CC kidney and coecum. {ECO:0000269|PubMed:10625674,
CC ECO:0000269|PubMed:11297523, ECO:0000269|PubMed:11733538,
CC ECO:0000269|PubMed:12101265, ECO:0000269|PubMed:15148607,
CC ECO:0000269|PubMed:9828134}.
CC -!- DEVELOPMENTAL STAGE: In yolk sac, first detected at low levels at 8.5
CC dpc, with significant expression detected at 10.5 dpc in myeloid
CC precursor cells. In liver, expressed from 16.5 dpc to P7.5 with highest
CC levels detected from 18.5 dpc to P0.5. In spleen, first detected at
CC 16.5 dpc, with peak levels detected at 18.5 dpc and P0.5 and expression
CC persisting through the spleen maturation to the adult stage. In bone
CC marrow, high expression levels detected from 16.5 dpc until adulthood.
CC In lung, first detected around the time of birth, with levels
CC increasing significantly from P14.5 towards adulthood.
CC {ECO:0000269|PubMed:12101265}.
CC -!- INDUCTION: Up-regulated in response to IL3 and IL4, during the
CC inflammatory response and upon parasitic infection.
CC {ECO:0000269|PubMed:10625674, ECO:0000269|PubMed:11297523,
CC ECO:0000269|PubMed:12101265, ECO:0000269|PubMed:12215441}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class II subfamily. {ECO:0000305}.
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DR EMBL; D87757; BAA13458.2; -; mRNA.
DR EMBL; M94584; AAB62394.2; -; mRNA.
DR EMBL; AK137503; BAE23385.1; -; mRNA.
DR EMBL; AK154420; BAE32572.1; -; mRNA.
DR EMBL; BC061154; AAH61154.1; -; mRNA.
DR EMBL; U56900; AAB01230.1; -; mRNA.
DR CCDS; CCDS17718.1; -.
DR PIR; S27879; S27879.
DR RefSeq; NP_034022.2; NM_009892.3.
DR PDB; 1E9L; X-ray; 2.50 A; A=22-398.
DR PDB; 1VF8; X-ray; 1.31 A; A=22-398.
DR PDBsum; 1E9L; -.
DR PDBsum; 1VF8; -.
DR AlphaFoldDB; O35744; -.
DR SMR; O35744; -.
DR STRING; 10090.ENSMUSP00000053923; -.
DR ChEMBL; CHEMBL1795141; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR UniLectin; O35744; -.
DR CarbonylDB; O35744; -.
DR GlyGen; O35744; 1 site.
DR CPTAC; non-CPTAC-3641; -.
DR jPOST; O35744; -.
DR PaxDb; O35744; -.
DR PeptideAtlas; O35744; -.
DR PRIDE; O35744; -.
DR ProteomicsDB; 281665; -.
DR DNASU; 12655; -.
DR Ensembl; ENSMUST00000063062; ENSMUSP00000053923; ENSMUSG00000040809.
DR GeneID; 12655; -.
DR KEGG; mmu:12655; -.
DR UCSC; uc008qvw.2; mouse.
DR CTD; 12655; -.
DR MGI; MGI:1330860; Chil3.
DR VEuPathDB; HostDB:ENSMUSG00000040809; -.
DR eggNOG; KOG2806; Eukaryota.
DR GeneTree; ENSGT00940000154557; -.
DR HOGENOM; CLU_002833_3_1_1; -.
DR InParanoid; O35744; -.
DR OMA; YDDPLSI; -.
DR OrthoDB; 1289629at2759; -.
DR PhylomeDB; O35744; -.
DR TreeFam; TF315610; -.
DR BioGRID-ORCS; 12655; 3 hits in 71 CRISPR screens.
DR EvolutionaryTrace; O35744; -.
DR PRO; PR:O35744; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; O35744; protein.
DR Bgee; ENSMUSG00000040809; Expressed in granulocyte and 59 other tissues.
DR ExpressionAtlas; O35744; baseline and differential.
DR Genevisible; O35744; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0048237; C:rough endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IDA:MGI.
DR GO; GO:0030246; F:carbohydrate binding; TAS:MGI.
DR GO; GO:0008061; F:chitin binding; IBA:GO_Central.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
DR GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006032; P:chitin catabolic process; ISO:MGI.
DR GO; GO:0006954; P:inflammatory response; TAS:MGI.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0032722; P:positive regulation of chemokine production; ISO:MGI.
DR GO; GO:0002532; P:production of molecular mediator involved in inflammatory response; ISO:MGI.
DR Gene3D; 3.10.50.10; -; 1.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF54556; SSF54556; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Chitin-binding; Cytoplasm;
KW Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
KW Glycosidase; Hydrolase; Inflammatory response; Lectin; Nucleus;
KW Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:10625674,
FT ECO:0000269|PubMed:11297523"
FT CHAIN 22..398
FT /note="Chitinase-like protein 3"
FT /id="PRO_0000011970"
FT DOMAIN 22..390
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 70..71
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 97..100
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 141
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 210..213
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 360
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT DISULFID 26..51
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT DISULFID 49..394
FT DISULFID 307..372
FT CONFLICT 105
FT /note="P -> S (in Ref. 1; no nucleotide entry and 2;
FT BAA13458)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="S -> P (in Ref. 3; BAE23385)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="P -> R (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:1VF8"
FT HELIX 30..34
FT /evidence="ECO:0007829|PDB:1VF8"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:1VF8"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:1VF8"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:1VF8"
FT STRAND 52..62
FT /evidence="ECO:0007829|PDB:1VF8"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:1VF8"
FT HELIX 73..82
FT /evidence="ECO:0007829|PDB:1VF8"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:1VF8"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:1VF8"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:1VF8"
FT HELIX 104..110
FT /evidence="ECO:0007829|PDB:1VF8"
FT HELIX 113..129
FT /evidence="ECO:0007829|PDB:1VF8"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:1VF8"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:1E9L"
FT HELIX 150..173
FT /evidence="ECO:0007829|PDB:1VF8"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:1VF8"
FT HELIX 188..194
FT /evidence="ECO:0007829|PDB:1VF8"
FT HELIX 197..203
FT /evidence="ECO:0007829|PDB:1VF8"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:1VF8"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:1VF8"
FT HELIX 236..240
FT /evidence="ECO:0007829|PDB:1VF8"
FT HELIX 243..252
FT /evidence="ECO:0007829|PDB:1VF8"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:1VF8"
FT STRAND 260..274
FT /evidence="ECO:0007829|PDB:1VF8"
FT STRAND 284..288
FT /evidence="ECO:0007829|PDB:1VF8"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:1VF8"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:1VF8"
FT HELIX 303..311
FT /evidence="ECO:0007829|PDB:1VF8"
FT STRAND 315..319
FT /evidence="ECO:0007829|PDB:1VF8"
FT TURN 320..323
FT /evidence="ECO:0007829|PDB:1VF8"
FT STRAND 324..329
FT /evidence="ECO:0007829|PDB:1VF8"
FT STRAND 332..335
FT /evidence="ECO:0007829|PDB:1VF8"
FT HELIX 339..351
FT /evidence="ECO:0007829|PDB:1VF8"
FT STRAND 356..360
FT /evidence="ECO:0007829|PDB:1VF8"
FT HELIX 362..364
FT /evidence="ECO:0007829|PDB:1VF8"
FT TURN 370..372
FT /evidence="ECO:0007829|PDB:1VF8"
FT HELIX 378..386
FT /evidence="ECO:0007829|PDB:1VF8"
SQ SEQUENCE 398 AA; 44458 MW; C11187661B99D1D1 CRC64;
MAKLILVTGL AILLNVQLGS SYQLMCYYTS WAKDRPIEGS FKPGNIDPCL CTHLIYAFAG
MQNNEITYTH EQDLRDYEAL NGLKDKNTEL KTLLAIGGWK FGPAPFSAMV STPQNRQIFI
QSVIRFLRQY NFDGLNLDWQ YPGSRGSPPK DKHLFSVLVK EMRKAFEEES VEKDIPRLLL
TSTGAGIIDV IKSGYKIPEL SQSLDYIQVM TYDLHDPKDG YTGENSPLYK SPYDIGKSAD
LNVDSIISYW KDHGAASEKL IVGFPAYGHT FILSDPSKTG IGAPTISTGP PGKYTDESGL
LAYYEVCTFL NEGATEVWDA PQEVPYAYQG NEWVGYDNVR SFKLKAQWLK DNNLGGAVVW
PLDMDDFSGS FCHQRHFPLT STLKGDLNIH SASCKGPY
