CH3L2_HUMAN
ID CH3L2_HUMAN Reviewed; 390 AA.
AC Q15782; A6NNY3; B4DPR7; Q15749; Q15783; Q5VUV7; Q96F97;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Chitinase-3-like protein 2;
DE AltName: Full=Chondrocyte protein 39;
DE AltName: Full=YKL-39;
DE Flags: Precursor;
GN Name=CHI3L2;
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 [MRNA] (ISOFORM 2).
RA Grossman A., Matsuyama T., Baker E., Waterhouse P., Sutherland G.R.,
RA Mak T.W.;
RT "Cloning of a novel lymphoid restricted human chitinase and localization to
RT 1p13.3.";
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 39-51, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Articular cartilage;
RX PubMed=8702629; DOI=10.1074/jbc.271.32.19415;
RA Hu B., Trinh K., Figueira W.F., Price P.A.;
RT "Isolation and sequence of a novel human chondrocyte protein related to
RT mammalian members of the chitinase protein family.";
RL J. Biol. Chem. 271:19415-19420(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-182.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-182.
RC TISSUE=Brain;
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 X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 26-390 IN COMPLEX WITH
RP CHITOOLIGOSACCHARIDE, FUNCTION, ABSENCE OF CHITINASE ACTIVITY, AND
RP MUTAGENESIS OF SER-143 AND ILE-145.
RX PubMed=22742450; DOI=10.1042/bj20120377;
RA Schimpl M., Rush C.L., Betou M., Eggleston I.M., Recklies A.D.,
RA van Aalten D.M.;
RT "Human YKL-39 is a pseudo-chitinase with retained chitooligosaccharide-
RT binding properties.";
RL Biochem. J. 446:149-157(2012).
CC -!- FUNCTION: Lectin that binds chitooligosaccharides and other glycans
CC with high affinity, but not heparin. Has no chitinase activity.
CC {ECO:0000269|PubMed:22742450}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q15782-4; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15782-5; Sequence=VSP_044262;
CC Name=3;
CC IsoId=Q15782-6; Sequence=VSP_047245;
CC -!- TISSUE SPECIFICITY: Highest expression in chondrocytes, followed by
CC synoviocytes, lung and heart. Not detected in spleen, pancreas, and
CC liver. May also be expressed in developing brain and placenta.
CC {ECO:0000269|PubMed:8702629}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. {ECO:0000305}.
CC -!- CAUTION: Lacks the conserved sequence motif DxxDxDxE that is essential
CC for the catalytic activity of chitinases of the glycosyl hydrolase 18
CC family, and therefore has no chitinase activity. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB04534.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAC50597.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U58515; AAB04534.1; ALT_INIT; mRNA.
DR EMBL; U58514; AAB04533.1; -; mRNA.
DR EMBL; U49835; AAC50597.1; ALT_INIT; mRNA.
DR EMBL; BT006767; AAP35413.1; -; mRNA.
DR EMBL; AK298466; BAG60679.1; -; mRNA.
DR EMBL; AL355816; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL513202; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471122; EAW56481.1; -; Genomic_DNA.
DR EMBL; BC011460; AAH11460.1; -; mRNA.
DR CCDS; CCDS30802.1; -. [Q15782-4]
DR CCDS; CCDS30803.1; -. [Q15782-6]
DR CCDS; CCDS41367.1; -. [Q15782-5]
DR RefSeq; NP_001020368.1; NM_001025197.1. [Q15782-6]
DR RefSeq; NP_001020370.1; NM_001025199.1. [Q15782-5]
DR RefSeq; NP_003991.2; NM_004000.2. [Q15782-4]
DR PDB; 4AY1; X-ray; 1.95 A; A/B/C/D/E/F/G/H/I/J/K/L=26-390.
DR PDB; 4P8U; X-ray; 2.40 A; A=27-390.
DR PDB; 4P8V; X-ray; 1.64 A; A=27-390.
DR PDB; 4P8W; X-ray; 1.87 A; A=27-390.
DR PDB; 4P8X; X-ray; 2.48 A; A=27-390.
DR PDBsum; 4AY1; -.
DR PDBsum; 4P8U; -.
DR PDBsum; 4P8V; -.
DR PDBsum; 4P8W; -.
DR PDBsum; 4P8X; -.
DR AlphaFoldDB; Q15782; -.
DR SMR; Q15782; -.
DR BioGRID; 107541; 17.
DR IntAct; Q15782; 4.
DR MINT; Q15782; -.
DR STRING; 9606.ENSP00000437082; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR UniLectin; Q15782; -.
DR GlyGen; Q15782; 1 site.
DR iPTMnet; Q15782; -.
DR PhosphoSitePlus; Q15782; -.
DR BioMuta; CHI3L2; -.
DR DMDM; 13124005; -.
DR MassIVE; Q15782; -.
DR MaxQB; Q15782; -.
DR PaxDb; Q15782; -.
DR PeptideAtlas; Q15782; -.
DR PRIDE; Q15782; -.
DR ProteomicsDB; 1646; -.
DR ProteomicsDB; 4806; -.
DR ProteomicsDB; 60758; -. [Q15782-4]
DR Antibodypedia; 1462; 250 antibodies from 28 providers.
DR DNASU; 1117; -.
DR Ensembl; ENST00000369744.6; ENSP00000358759.2; ENSG00000064886.14. [Q15782-6]
DR Ensembl; ENST00000369748.9; ENSP00000358763.4; ENSG00000064886.14. [Q15782-4]
DR Ensembl; ENST00000445067.6; ENSP00000437082.1; ENSG00000064886.14. [Q15782-4]
DR Ensembl; ENST00000466741.5; ENSP00000437086.1; ENSG00000064886.14. [Q15782-5]
DR Ensembl; ENST00000524472.5; ENSP00000432049.1; ENSG00000064886.14. [Q15782-5]
DR GeneID; 1117; -.
DR KEGG; hsa:1117; -.
DR MANE-Select; ENST00000369748.9; ENSP00000358763.4; NM_004000.3; NP_003991.2.
DR UCSC; uc001eam.4; human. [Q15782-4]
DR CTD; 1117; -.
DR DisGeNET; 1117; -.
DR GeneCards; CHI3L2; -.
DR HGNC; HGNC:1933; CHI3L2.
DR HPA; ENSG00000064886; Tissue enhanced (brain, lymphoid tissue, salivary gland).
DR MIM; 601526; gene.
DR neXtProt; NX_Q15782; -.
DR OpenTargets; ENSG00000064886; -.
DR PharmGKB; PA26464; -.
DR VEuPathDB; HostDB:ENSG00000064886; -.
DR eggNOG; KOG2806; Eukaryota.
DR GeneTree; ENSGT00940000163351; -.
DR HOGENOM; CLU_002833_3_1_1; -.
DR InParanoid; Q15782; -.
DR OMA; IRAAYWP; -.
DR OrthoDB; 1289629at2759; -.
DR PhylomeDB; Q15782; -.
DR TreeFam; TF315610; -.
DR PathwayCommons; Q15782; -.
DR SignaLink; Q15782; -.
DR BioGRID-ORCS; 1117; 13 hits in 1062 CRISPR screens.
DR GenomeRNAi; 1117; -.
DR Pharos; Q15782; Tbio.
DR PRO; PR:Q15782; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q15782; protein.
DR Bgee; ENSG00000064886; Expressed in cartilage tissue and 137 other tissues.
DR ExpressionAtlas; Q15782; baseline and differential.
DR Genevisible; Q15782; HS.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0008061; F:chitin binding; IDA:UniProtKB.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006032; P:chitin catabolic process; IBA:GO_Central.
DR Gene3D; 3.10.50.10; -; 1.
DR InterPro; IPR028541; CHI3L2.
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:SF82; PTHR11177:SF82; 1.
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; Alternative splicing; Chitin-binding;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase; Lectin;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..26
FT CHAIN 27..390
FT /note="Chitinase-3-like protein 2"
FT /id="PRO_0000011969"
FT DOMAIN 27..390
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 75..76
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 102..105
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 104
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000269|PubMed:22742450"
FT BINDING 146
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258,
FT ECO:0000269|PubMed:22742450"
FT BINDING 210..213
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 213
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000269|PubMed:22742450"
FT BINDING 360
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258,
FT ECO:0000269|PubMed:22742450"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT VAR_SEQ 1..79
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.1"
FT /id="VSP_044262"
FT VAR_SEQ 14..23
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_047245"
FT VARIANT 182
FT /note="A -> V (in dbSNP:rs11556868)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3"
FT /id="VAR_049198"
FT VARIANT 184
FT /note="V -> I (in dbSNP:rs34049547)"
FT /id="VAR_033731"
FT VARIANT 318
FT /note="R -> W (in dbSNP:rs13721)"
FT /id="VAR_061189"
FT MUTAGEN 143
FT /note="S->D: Confers chitinase activity; when associated
FT with E-145."
FT /evidence="ECO:0000269|PubMed:22742450"
FT MUTAGEN 145
FT /note="I->E: Confers chitinase activity; when associated
FT with D-143."
FT /evidence="ECO:0000269|PubMed:22742450"
FT STRAND 28..36
FT /evidence="ECO:0007829|PDB:4P8V"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:4P8V"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:4P8V"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:4P8V"
FT STRAND 57..67
FT /evidence="ECO:0007829|PDB:4P8V"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:4P8V"
FT HELIX 78..91
FT /evidence="ECO:0007829|PDB:4P8V"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:4P8V"
FT TURN 104..108
FT /evidence="ECO:0007829|PDB:4P8V"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:4P8V"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:4P8V"
FT HELIX 118..134
FT /evidence="ECO:0007829|PDB:4P8V"
FT STRAND 139..145
FT /evidence="ECO:0007829|PDB:4P8V"
FT HELIX 148..171
FT /evidence="ECO:0007829|PDB:4P8V"
FT STRAND 179..185
FT /evidence="ECO:0007829|PDB:4P8V"
FT HELIX 188..194
FT /evidence="ECO:0007829|PDB:4P8V"
FT HELIX 197..203
FT /evidence="ECO:0007829|PDB:4P8V"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:4P8V"
FT HELIX 238..242
FT /evidence="ECO:0007829|PDB:4P8V"
FT HELIX 245..254
FT /evidence="ECO:0007829|PDB:4P8V"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:4P8V"
FT STRAND 262..278
FT /evidence="ECO:0007829|PDB:4P8V"
FT STRAND 285..289
FT /evidence="ECO:0007829|PDB:4P8V"
FT TURN 294..296
FT /evidence="ECO:0007829|PDB:4P8V"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:4P8V"
FT HELIX 304..310
FT /evidence="ECO:0007829|PDB:4P8V"
FT TURN 311..313
FT /evidence="ECO:0007829|PDB:4P8V"
FT STRAND 315..319
FT /evidence="ECO:0007829|PDB:4P8V"
FT TURN 320..323
FT /evidence="ECO:0007829|PDB:4P8V"
FT STRAND 324..329
FT /evidence="ECO:0007829|PDB:4P8V"
FT STRAND 332..335
FT /evidence="ECO:0007829|PDB:4P8V"
FT HELIX 339..351
FT /evidence="ECO:0007829|PDB:4P8V"
FT STRAND 355..360
FT /evidence="ECO:0007829|PDB:4P8V"
FT HELIX 362..364
FT /evidence="ECO:0007829|PDB:4P8V"
FT TURN 370..372
FT /evidence="ECO:0007829|PDB:4P8V"
FT HELIX 378..388
FT /evidence="ECO:0007829|PDB:4P8V"
SQ SEQUENCE 390 AA; 43501 MW; 97B86A2F3AA35677 CRC64;
MGATTMDQKS LWAGVVVLLL LQGGSAYKLV CYFTNWSQDR QEPGKFTPEN IDPFLCSHLI
YSFASIENNK VIIKDKSEVM LYQTINSLKT KNPKLKILLS IGGYLFGSKG FHPMVDSSTS
RLEFINSIIL FLRNHNFDGL DVSWIYPDQK ENTHFTVLIH ELAEAFQKDF TKSTKERLLL
TAGVSAGRQM IDNSYQVEKL AKDLDFINLL SFDFHGSWEK PLITGHNSPL SKGWQDRGPS
SYYNVEYAVG YWIHKGMPSE KVVMGIPTYG HSFTLASAET TVGAPASGPG AAGPITESSG
FLAYYEICQF LKGAKITRLQ DQQVPYAVKG NQWVGYDDVK SMETKVQFLK NLNLGGAMIW
SIDMDDFTGK SCNQGPYPLV QAVKRSLGSL
