ID CH3L1_MOUSE Reviewed; 389 AA. AC Q61362; B0FEU7; D3Z2P2; Q3U291; Q4FJW9; Q8BKL8; Q99J84; DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot. DT 14-MAY-2014, sequence version 3. DT 20-JUN-2018, entry version 150. DE RecName: Full=Chitinase-3-like protein 1; DE AltName: Full=BRP39 protein; DE AltName: Full=Breast regression protein 39; DE AltName: Full=Cartilage glycoprotein 39; DE Short=CGP-39; DE Short=GP-39; DE Flags: Precursor; GN Name=Chi3l1; Synonyms=Brp39, Chil1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC STRAIN=FVB/N; TISSUE=Mammary gland; RX PubMed=7970700; RA Morrison B.W., Leder P.; RT "neu and ras initiate murine mammary tumors that share genetic markers RT generally absent in c-myc and int-2-initiated tumors."; RL Oncogene 9:3417-3426(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, MUTAGENESIS OF RP LEU-136, AND CRYSTALLIZATION. RC TISSUE=Mammary gland; RX PubMed=19041398; DOI=10.1016/j.pep.2008.11.001; RA Mohanty A.K., Fisher A.J., Yu Z., Pradeep M.A., Janjanam J., RA Kaushik J.K.; RT "Cloning, expression, characterization and crystallization of BRP39, a RT signalling glycoprotein expressed during mammary gland apoptosis."; RL Protein Expr. Purif. 64:213-218(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=C57BL/6J, and NOD; TISSUE=Dendritic cell, and Spinal ganglion; 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RA Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., RA Mollenhauer J., Wiemann S., Schick M., Korn B.; RT "Cloning of mouse full open reading frames in Gateway(R) system entry RT vector (pDONR201)."; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] 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., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION. RX PubMed=16472595; DOI=10.1053/j.gastro.2005.12.007; RA Mizoguchi E.; RT "Chitinase 3-like-1 exacerbates intestinal inflammation by enhancing RT bacterial adhesion and invasion in colonic epithelial cells."; RL Gastroenterology 130:398-411(2006). RN [8] RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE. RX PubMed=19414556; DOI=10.1084/jem.20081271; RA Lee C.G., Hartl D., Lee G.R., Koller B., Matsuura H., Da Silva C.A., RA Sohn M.H., Cohn L., Homer R.J., Kozhich A.A., Humbles A., Kearley J., RA Coyle A., Chupp G., Reed J., Flavell R.A., Elias J.A.; RT "Role of breast regression protein 39 (BRP-39)/chitinase 3-like-1 in RT Th2 and IL-13-induced tissue responses and apoptosis."; RL J. Exp. Med. 206:1149-1166(2009). RN [9] RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND RP DISRUPTION PHENOTYPE. RX PubMed=20558631; DOI=10.1164/rccm.200912-1793OC; RA Sohn M.H., Kang M.J., Matsuura H., Bhandari V., Chen N.Y., Lee C.G., RA Elias J.A.; RT "The chitinase-like proteins breast regression protein-39 and YKL-40 RT regulate hyperoxia-induced acute lung injury."; RL Am. J. Respir. Crit. Care Med. 182:918-928(2010). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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 RT expression."; RL Cell 143:1174-1189(2010). RN [11] RP FUNCTION, SUBCELLULAR LOCATION, AND REGION. RX PubMed=21546314; DOI=10.1016/j.clim.2011.04.007; RA Chen C.C., Llado V., Eurich K., Tran H.T., Mizoguchi E.; RT "Carbohydrate-binding motif in chitinase 3-like 1 (CHI3L1/YKL-40) RT specifically activates Akt signaling pathway in colonic epithelial RT cells."; RL Clin. Immunol. 140:268-275(2011). RN [12] RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE. RX PubMed=22817986; DOI=10.1016/j.chom.2012.05.017; RA Dela Cruz C.S., Liu W., He C.H., Jacoby A., Gornitzky A., Ma B., RA Flavell R., Lee C.G., Elias J.A.; RT "Chitinase 3-like-1 promotes Streptococcus pneumoniae killing and RT augments host tolerance to lung antibacterial responses."; RL Cell Host Microbe 12:34-46(2012). RN [13] RP TISSUE SPECIFICITY, AND INDUCTION. RX PubMed=21866546; DOI=10.1002/ijc.26379; RA Libreros S., Garcia-Areas R., Shibata Y., Carrio R., RA Torroella-Kouri M., Iragavarapu-Charyulu V.; RT "Induction of proinflammatory mediators by CHI3L1 is reduced by chitin RT treatment: decreased tumor metastasis in a breast cancer model."; RL Int. J. Cancer 131:377-386(2012). CC -!- FUNCTION: Carbohydrate-binding lectin with a preference for CC chitin. Has no chitinase activity. May play a role in tissue CC remodeling and in the capacity of cells to respond to and cope CC with changes in their environment. Plays a role in T-helper cell CC type 2 (Th2) inflammatory response and IL-13-induced inflammation, CC regulating allergen sensitization, inflammatory cell apoptosis, CC dendritic cell accumulation and M2 macrophage differentiation. CC Facilitates invasion of pathogenic enteric bacteria into colonic CC mucosa and lymphoid organs. Mediates activation of AKT1 signaling CC pathway and subsequent IL8 production in colonic epithelial cells. CC Regulates antibacterial responses in lung by contributing to CC macrophage bacterial killing, controlling bacterial dissemination CC and augmenting host tolerance. Also regulates hyperoxia-induced CC injury, inflammation and epithelial apoptosis in lung. CC {ECO:0000269|PubMed:16472595, ECO:0000269|PubMed:19041398, CC ECO:0000269|PubMed:19414556, ECO:0000269|PubMed:20558631, CC ECO:0000269|PubMed:21546314, ECO:0000269|PubMed:22817986}. CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space. Cytoplasm. CC Endoplasmic reticulum. Note=Detected in bronchoalveolar lavage CC (BAL) fluids. Localizes mainly to endoplasmic reticulum when CC overexpressed in cells, with some protein also detected throughout CC the cytoplasm. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing, Alternative initiation; Named isoforms=3; CC Name=1; CC IsoId=Q61362-1; Sequence=Displayed; CC Name=2; CC IsoId=Q61362-2; Sequence=VSP_054524; CC Note=Produced by alternative initiation at Met-9 of isoform 1.; CC Name=3; CC IsoId=Q61362-3; Sequence=VSP_054523; CC Note=May be produced by alternative splicing of isoform 1. Gene CC prediction based on EST data.; CC -!- TISSUE SPECIFICITY: Detected in lung in pulmonary macrophages and CC alveolar type 2 cells and in bronchoalveolar lavage (BAL) fluids. CC Expressed in mammary tumor cells (at protein level). Expressed in CC lung. Not detected in non-inflammatory colon. CC {ECO:0000269|PubMed:16472595, ECO:0000269|PubMed:19414556, CC ECO:0000269|PubMed:20558631, ECO:0000269|PubMed:21866546}. CC -!- INDUCTION: Up-regulated in colon under several inflammatory CC conditions. Up-regulated upon pulmonary inflammation elicited by CC sensitization and challenge with the chitin-free aeroallergen CC ovalbumin or with chitin-containing antigen house dust mite (HDM) CC extract. Up-regulated in lungs after S.pneumoniae infection. Up- CC regulated in splenic cells of mammary tumor-bearing animals. Down- CC regulated by hyperoxia in lung. {ECO:0000269|PubMed:16472595, CC ECO:0000269|PubMed:19414556, ECO:0000269|PubMed:20558631, CC ECO:0000269|PubMed:21866546, ECO:0000269|PubMed:22817986}. CC -!- DISRUPTION PHENOTYPE: Mice are viable, fertile and appear normal, CC but have defective antigen-induced Th2 inflammatory responses and CC defective IL-13-induced responses, displaying accelerated cell CC death responses and diminished M2 macrophage differentiation. CC Mutant mice are more sensitive to S.pneumoniae infection, CC displaying enhanced mortality, exacerbated lung injury and CC decreased bacterial clearance compared to wild-type mice. Mutant CC mice also have an exacerbated response to hyperoxia, displaying CC enhanced protein leak, tissue inflammation and chemokine CC production and premature death. {ECO:0000269|PubMed:19414556, CC ECO:0000269|PubMed:20558631, ECO:0000269|PubMed:22817986}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. CC {ECO:0000305}. CC -!- CAUTION: Although it belongs to the glycosyl hydrolase 18 family, CC Leu-149 is present instead of the conserved Glu which is an active CC site residue. Therefore this protein lacks chitinase activity. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH03780.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; CC Sequence=AAH04734.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; CC Sequence=AAH05611.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; CC Sequence=CAA63603.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X93035; CAA63603.1; ALT_INIT; mRNA. DR EMBL; EU313768; ABY53363.1; -; mRNA. DR EMBL; AK051475; BAC34654.1; -; mRNA. DR EMBL; AK155412; BAE33251.1; -; mRNA. DR EMBL; CT010283; CAJ18491.1; -; mRNA. DR EMBL; AC137104; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC003780; AAH03780.1; ALT_INIT; mRNA. DR EMBL; BC004734; AAH04734.1; ALT_INIT; mRNA. DR EMBL; BC005611; AAH05611.1; ALT_INIT; mRNA. DR CCDS; CCDS48368.1; -. [Q61362-1] DR PIR; S61551; S61551. DR RefSeq; NP_031721.2; NM_007695.3. [Q61362-1] DR RefSeq; XP_006529174.1; XM_006529111.3. [Q61362-3] DR UniGene; Mm.38274; -. DR PDB; 5XEP; X-ray; 2.60 A; A/B/C/D/E/F=9-389. DR PDBsum; 5XEP; -. DR ProteinModelPortal; Q61362; -. DR SMR; Q61362; -. DR IntAct; Q61362; 1. DR MINT; Q61362; -. DR STRING; 10090.ENSMUSP00000080717; -. DR CAZy; GH18; Glycoside Hydrolase Family 18. DR PhosphoSitePlus; Q61362; -. DR PaxDb; Q61362; -. DR PeptideAtlas; Q61362; -. DR PRIDE; Q61362; -. DR Ensembl; ENSMUST00000082060; ENSMUSP00000080717; ENSMUSG00000064246. [Q61362-1] DR Ensembl; ENSMUST00000153856; ENSMUSP00000117117; ENSMUSG00000064246. [Q61362-2] DR Ensembl; ENSMUST00000156873; ENSMUSP00000119205; ENSMUSG00000064246. [Q61362-3] DR GeneID; 12654; -. DR KEGG; mmu:12654; -. DR UCSC; uc007crg.2; mouse. [Q61362-1] DR CTD; 12654; -. DR MGI; MGI:1340899; Chil1. DR eggNOG; KOG2806; Eukaryota. DR eggNOG; COG3325; LUCA. DR GeneTree; ENSGT00550000074323; -. DR HOGENOM; HOG000111109; -. DR HOVERGEN; HBG011684; -. DR InParanoid; Q61362; -. DR KO; K17523; -. DR OMA; SNDHIDT; -. DR OrthoDB; EOG091G014W; -. DR TreeFam; TF315610; -. DR Reactome; R-MMU-6798695; Neutrophil degranulation. DR ChiTaRS; Chil1; mouse. DR PRO; PR:Q61362; -. DR Proteomes; UP000000589; Chromosome 1. DR Bgee; ENSMUSG00000064246; -. DR CleanEx; MM_CHI3L1; -. DR ExpressionAtlas; Q61362; baseline and differential. DR Genevisible; Q61362; MM. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; IBA:GO_Central. DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB. DR GO; GO:0008061; F:chitin binding; ISS:UniProtKB. DR GO; GO:0007250; P:activation of NF-kappaB-inducing kinase activity; IDA:UniProtKB. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0071356; P:cellular response to tumor necrosis factor; ISS:UniProtKB. DR GO; GO:0006954; P:inflammatory response; ISS:UniProtKB. DR GO; GO:0072606; P:interleukin-8 secretion; IDA:UniProtKB. DR GO; GO:0030324; P:lung development; ISS:UniProtKB. DR GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB. DR GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IDA:UniProtKB. DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:UniProtKB. DR GO; GO:0070555; P:response to interleukin-1; ISS:UniProtKB. DR GO; GO:0070741; P:response to interleukin-6; ISS:UniProtKB. DR GO; GO:0009612; P:response to mechanical stimulus; ISS:UniProtKB. DR GO; GO:0034612; P:response to tumor necrosis factor; ISS:UniProtKB. DR Gene3D; 3.10.50.10; -; 1. DR InterPro; IPR028538; CHI3L1. DR InterPro; IPR011583; Chitinase_II. DR InterPro; IPR029070; Chitinase_insertion_sf. DR InterPro; IPR001223; Glyco_hydro18_cat. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR PANTHER; PTHR11177:SF202; PTHR11177:SF202; 1. DR Pfam; PF00704; Glyco_hydro_18; 1. DR SMART; SM00636; Glyco_18; 1. DR SUPFAM; SSF51445; SSF51445; 2. DR SUPFAM; SSF54556; SSF54556; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative initiation; Alternative splicing; KW Antimicrobial; Apoptosis; Complete proteome; Cytoplasm; KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; KW Inflammatory response; Reference proteome; Secreted; Signal. FT SIGNAL 1 29 {ECO:0000250}. FT CHAIN 30 389 Chitinase-3-like protein 1. FT /FTId=PRO_0000011966. FT REGION 79 80 Chitooligosaccharide binding. FT {ECO:0000250}. FT REGION 106 109 Chitooligosaccharide binding. FT {ECO:0000250}. FT REGION 213 216 Chitooligosaccharide binding. FT {ECO:0000250}. FT REGION 333 347 Important for AKT1 activation and IL8 FT production. FT BINDING 150 150 Chitooligosaccharide. {ECO:0000250}. FT BINDING 361 361 Chitooligosaccharide. {ECO:0000250}. FT CARBOHYD 68 68 N-linked (GlcNAc...) asparagine. FT {ECO:0000250}. FT DISULFID 34 59 {ECO:0000250}. FT DISULFID 309 372 {ECO:0000250}. FT VAR_SEQ 1 16 MHTSTEARMGMRAALT -> MTLQLA (in isoform FT 3). {ECO:0000305}. FT /FTId=VSP_054523. FT VAR_SEQ 1 8 Missing (in isoform 2). FT {ECO:0000303|PubMed:19041398, FT ECO:0000303|Ref.4}. FT /FTId=VSP_054524. FT MUTAGEN 136 136 L->E: No effect on chiting-binding. No FT restoration of chitinase activity. FT {ECO:0000269|PubMed:19041398}. FT CONFLICT 112 112 E -> G (in Ref. 4; ABY53363). FT {ECO:0000305}. FT CONFLICT 258 258 A -> V (in Ref. 3; BAE33251). FT {ECO:0000305}. FT CONFLICT 339 339 D -> H (in Ref. 1; CAA63603). FT {ECO:0000305}. FT CONFLICT 348 348 G -> R (in Ref. 4; ABY53363). FT {ECO:0000305}. FT STRAND 31 38 {ECO:0000244|PDB:5XEP}. FT HELIX 39 42 {ECO:0000244|PDB:5XEP}. FT HELIX 45 47 {ECO:0000244|PDB:5XEP}. FT HELIX 51 53 {ECO:0000244|PDB:5XEP}. FT STRAND 60 69 {ECO:0000244|PDB:5XEP}. FT HELIX 82 90 {ECO:0000244|PDB:5XEP}. FT HELIX 91 94 {ECO:0000244|PDB:5XEP}. FT STRAND 100 106 {ECO:0000244|PDB:5XEP}. FT TURN 108 110 {ECO:0000244|PDB:5XEP}. FT HELIX 112 119 {ECO:0000244|PDB:5XEP}. FT HELIX 122 139 {ECO:0000244|PDB:5XEP}. FT STRAND 143 147 {ECO:0000244|PDB:5XEP}. FT HELIX 153 155 {ECO:0000244|PDB:5XEP}. FT HELIX 156 173 {ECO:0000244|PDB:5XEP}. FT STRAND 182 188 {ECO:0000244|PDB:5XEP}. FT HELIX 191 197 {ECO:0000244|PDB:5XEP}. FT HELIX 200 204 {ECO:0000244|PDB:5XEP}. FT STRAND 208 213 {ECO:0000244|PDB:5XEP}. FT HELIX 220 222 {ECO:0000244|PDB:5XEP}. FT STRAND 242 245 {ECO:0000244|PDB:5XEP}. FT HELIX 246 255 {ECO:0000244|PDB:5XEP}. FT HELIX 260 262 {ECO:0000244|PDB:5XEP}. FT STRAND 263 279 {ECO:0000244|PDB:5XEP}. FT STRAND 286 290 {ECO:0000244|PDB:5XEP}. FT TURN 295 297 {ECO:0000244|PDB:5XEP}. FT HELIX 305 312 {ECO:0000244|PDB:5XEP}. FT STRAND 316 319 {ECO:0000244|PDB:5XEP}. FT TURN 321 323 {ECO:0000244|PDB:5XEP}. FT STRAND 326 330 {ECO:0000244|PDB:5XEP}. FT STRAND 333 336 {ECO:0000244|PDB:5XEP}. FT HELIX 340 352 {ECO:0000244|PDB:5XEP}. FT STRAND 356 361 {ECO:0000244|PDB:5XEP}. FT HELIX 363 365 {ECO:0000244|PDB:5XEP}. FT HELIX 379 388 {ECO:0000244|PDB:5XEP}. SQ SEQUENCE 389 AA; 43893 MW; 9E7D66069B233834 CRC64; MHTSTEARMG MRAALTGFAV LMLLQSCSAY KLVCYFTSWS QYREGVGSFL PDAIQPFLCT HIIYSFANIS SDNMLSTWEW NDESNYDKLN KLKTRNTNLK TLLSVGGWKF GEKRFSEIAS NTERRTAFVR SVAPFLRSYG FDGLDLAWLY PRLRDKQYFS TLIKELNAEF TKEVQPGREK LLLSAALSAG KVAIDTGYDI AQIAQHLDFI NLMTYDFHGV WRQITGHHSP LFQGQKDTRF DRYSNVNYAV QYMIRLGAQA SKLLMGIPTF GKSFTLASSE NQLGAPISGE GLPGRFTKEA GTLAYYEICD FLKGAEVHRL SNEKVPFATK GNQWVGYEDK ESVKNKVGFL KEKKLAGAMV WALDLDDFQG TCQPKEFFPL TNAIKDALA //