IL15_HUMAN
ID IL15_HUMAN Reviewed; 162 AA.
AC P40933; D3DNZ2; O00440; O43512; Q495Z8; Q6FGX7; Q93058; Q9UBA3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Interleukin-15;
DE Short=IL-15;
DE Flags: Precursor;
GN Name=IL15;
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 IL15-S48AA), AND FUNCTION.
RC TISSUE=Bone marrow;
RX PubMed=8178155; DOI=10.1126/science.8178155;
RA Grabstein K.H., Eisenman J., Shanebeck K., Rauch C., Srinivasan S.,
RA Fung V., Beers C., Richardson J., Schoenborn M.A., Ahdieh M., Johnson L.,
RA Alderson M.R., Watson J.D., Anderson D.M., Giri J.G.;
RT "Cloning of a T cell growth factor that interacts with the beta chain of
RT the interleukin-2 receptor.";
RL Science 264:965-968(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8932977; DOI=10.1006/cyto.1996.0089;
RA Krause H., Jandrig B., Wernicke C., Bulfone-Paus S., Pohl T.,
RA Diamantstein T.;
RT "Genomic sequence and chromosomal location of the human interleukin-15 gene
RT (IL15).";
RL Cytokine 8:667-674(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IL15-S21AA).
RC TISSUE=Lung cancer;
RX PubMed=8668345;
RA Meazza R., Verdiani S., Biassoni R., Coppolecchia M., Gaggero A.,
RA Orengo A.M., Colombo M.P., Azzarone B., Ferrini S.;
RT "Identification of a novel interleukin-15 (IL-15) transcript isoform
RT generated by alternative splicing in human small cell lung cancer cell
RT lines.";
RL Oncogene 12:2187-2192(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IL15-S21AA).
RC TISSUE=Testis;
RX PubMed=9405632; DOI=10.1073/pnas.94.26.14444;
RA Tagaya Y., Kurys G., Thies T.A., Losi J.M., Azimi N., Hanover J.A.,
RA Bamford R.N., Waldmann T.A.;
RT "Generation of secretable and nonsecretable interleukin 15 isoforms through
RT alternate usage of signal peptides.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:14444-14449(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Meazza R., Ferrini S.;
RT "Expression of two IL-15 mRNA isoforms in human tumors does not correlate
RT with secretion: role of different signal peptides.";
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IL15-S21AA).
RA Li C.;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IL15-S21AA).
RC TISSUE=Cerebellum, and Heart;
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IL15-S21AA).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [9]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS IL15-S48AA AND
RP IL15-S21AA).
RC TISSUE=Colon;
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 [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 49-162.
RC TISSUE=Epidermis;
RA Sorel M.A., Jacques Y.;
RT "IL15 expression in human keratinocytes.";
RL Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP FUNCTION.
RX PubMed=15123770; DOI=10.1189/jlb.0605298;
RA Ratthe C., Girard D.;
RT "Interleukin-15 enhances human neutrophil phagocytosis by a Syk-dependent
RT mechanism: importance of the IL-15Ralpha chain.";
RL J. Leukoc. Biol. 76:162-168(2004).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 49-162 IN COMPLEX WITH ANTIBODY,
RP AND DISULFIDE BONDS.
RX PubMed=21167836; DOI=10.1016/j.jmb.2010.12.017;
RA Lowe D.C., Gerhardt S., Ward A., Hargreaves D., Anderson M., Ferraro F.,
RA Pauptit R.A., Pattison D.V., Buchanan C., Popovic B., Finch D.K.,
RA Wilkinson T., Sleeman M., Vaughan T.J., Mallinder P.R.;
RT "Engineering a high-affinity anti-IL-15 antibody: crystal structure reveals
RT an alpha-helix in VH CDR3 as key component of paratope.";
RL J. Mol. Biol. 406:160-175(2011).
CC -!- FUNCTION: Cytokine that stimulates the proliferation of T-lymphocytes
CC (PubMed:8178155). Stimulation by IL15 requires interaction of IL15 with
CC components of the IL2 receptor, including IL2RB and probably IL2RG but
CC not IL2RA (PubMed:8178155). In neutrophils, stimulates phagocytosis
CC probably by signaling through the IL15 receptor, composed of the
CC subunits IL15RA, IL2RB and IL2RG, which results in kinase SYK
CC activation (PubMed:15123770). {ECO:0000269|PubMed:15123770,
CC ECO:0000269|PubMed:8178155}.
CC -!- INTERACTION:
CC P40933; Q13261: IL15RA; NbExp=5; IntAct=EBI-980274, EBI-980354;
CC P40933; P14784: IL2RB; NbExp=3; IntAct=EBI-980274, EBI-2866779;
CC -!- SUBCELLULAR LOCATION: [Isoform IL15-S48AA]: Secreted.
CC -!- SUBCELLULAR LOCATION: [Isoform IL15-S21AA]: Cytoplasm. Nucleus.
CC Note=IL15-S21AA is not secreted, but rather is stored intracellularly,
CC appearing in the nucleus and cytoplasmic components.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=IL15-S48AA;
CC IsoId=P40933-1; Sequence=Displayed;
CC Name=IL15-S21AA;
CC IsoId=P40933-2; Sequence=VSP_002660;
CC -!- TISSUE SPECIFICITY: Most abundant in placenta and skeletal muscle. It
CC is also detected in the heart, lung, liver and kidney. IL15-S21AA is
CC preferentially expressed in tissues such as testis and thymus.
CC -!- SIMILARITY: Belongs to the IL-15/IL-21 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA71044.1; Type=Miscellaneous discrepancy; Note=Man-made cDNA with a signal peptide sequence to increase protein secretion (substitution with a signal peptide derived from the mouse IgV kappa chain).; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Interleukin-15 entry;
CC URL="https://en.wikipedia.org/wiki/Interleukin_15";
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DR EMBL; U14407; AAA21551.1; -; mRNA.
DR EMBL; X91233; CAA62616.1; -; Genomic_DNA.
DR EMBL; X94223; CAA63914.1; -; mRNA.
DR EMBL; X94222; CAA63913.1; -; mRNA.
DR EMBL; AF031167; AAB97518.1; -; mRNA.
DR EMBL; Y09908; CAA71044.1; ALT_SEQ; mRNA.
DR EMBL; AY720442; AAU21241.1; -; mRNA.
DR EMBL; AK122993; BAG53839.1; -; mRNA.
DR EMBL; AK290619; BAF83308.1; -; mRNA.
DR EMBL; CR541980; CAG46777.1; -; mRNA.
DR EMBL; CR542007; CAG46804.1; -; mRNA.
DR EMBL; CH471056; EAX05083.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX05084.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX05085.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX05086.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX05087.1; -; Genomic_DNA.
DR EMBL; BC018149; AAH18149.1; -; mRNA.
DR EMBL; BC100961; AAI00962.1; -; mRNA.
DR EMBL; BC100962; AAI00963.1; -; mRNA.
DR EMBL; BC100963; AAI00964.1; -; mRNA.
DR EMBL; Z38000; CAA86100.1; -; mRNA.
DR CCDS; CCDS3755.1; -. [P40933-1]
DR CCDS; CCDS3756.1; -. [P40933-2]
DR RefSeq; NP_000576.1; NM_000585.4. [P40933-1]
DR RefSeq; NP_751915.1; NM_172175.2. [P40933-2]
DR PDB; 2XQB; X-ray; 2.60 A; A=49-162.
DR PDB; 2Z3Q; X-ray; 1.85 A; A/C=49-162.
DR PDB; 2Z3R; X-ray; 2.00 A; A/C/E/G/I/K/M/O=49-162.
DR PDB; 4GS7; X-ray; 2.35 A; A=49-162.
DR PDBsum; 2XQB; -.
DR PDBsum; 2Z3Q; -.
DR PDBsum; 2Z3R; -.
DR PDBsum; 4GS7; -.
DR AlphaFoldDB; P40933; -.
DR SMR; P40933; -.
DR BioGRID; 109813; 8.
DR CORUM; P40933; -.
DR DIP; DIP-3046N; -.
DR IntAct; P40933; 5.
DR STRING; 9606.ENSP00000296545; -.
DR BindingDB; P40933; -.
DR ChEMBL; CHEMBL3712954; -.
DR DrugBank; DB01327; Cefazolin.
DR GlyGen; P40933; 1 site.
DR iPTMnet; P40933; -.
DR PhosphoSitePlus; P40933; -.
DR BioMuta; IL15; -.
DR MassIVE; P40933; -.
DR PaxDb; P40933; -.
DR PeptideAtlas; P40933; -.
DR PRIDE; P40933; -.
DR ProteomicsDB; 55387; -. [P40933-1]
DR ProteomicsDB; 55388; -. [P40933-2]
DR ABCD; P40933; 1 sequenced antibody.
DR Antibodypedia; 3844; 1019 antibodies from 43 providers.
DR DNASU; 3600; -.
DR Ensembl; ENST00000296545.11; ENSP00000296545.7; ENSG00000164136.17. [P40933-1]
DR Ensembl; ENST00000320650.9; ENSP00000323505.4; ENSG00000164136.17. [P40933-1]
DR Ensembl; ENST00000394159.2; ENSP00000377714.1; ENSG00000164136.17. [P40933-2]
DR Ensembl; ENST00000477265.5; ENSP00000436914.1; ENSG00000164136.17. [P40933-2]
DR Ensembl; ENST00000514653.5; ENSP00000422271.1; ENSG00000164136.17. [P40933-2]
DR Ensembl; ENST00000529613.5; ENSP00000435462.1; ENSG00000164136.17. [P40933-1]
DR GeneID; 3600; -.
DR KEGG; hsa:3600; -.
DR MANE-Select; ENST00000320650.9; ENSP00000323505.4; NM_000585.5; NP_000576.1.
DR UCSC; uc003iis.4; human. [P40933-1]
DR CTD; 3600; -.
DR DisGeNET; 3600; -.
DR GeneCards; IL15; -.
DR HGNC; HGNC:5977; IL15.
DR HPA; ENSG00000164136; Low tissue specificity.
DR MIM; 600554; gene.
DR neXtProt; NX_P40933; -.
DR OpenTargets; ENSG00000164136; -.
DR PharmGKB; PA29790; -.
DR VEuPathDB; HostDB:ENSG00000164136; -.
DR eggNOG; ENOG502SCMF; Eukaryota.
DR GeneTree; ENSGT00390000016264; -.
DR HOGENOM; CLU_135111_0_0_1; -.
DR InParanoid; P40933; -.
DR OMA; ANWQDVI; -.
DR OrthoDB; 1521691at2759; -.
DR PhylomeDB; P40933; -.
DR TreeFam; TF336199; -.
DR PathwayCommons; P40933; -.
DR Reactome; R-HSA-8983432; Interleukin-15 signaling.
DR SignaLink; P40933; -.
DR SIGNOR; P40933; -.
DR BioGRID-ORCS; 3600; 6 hits in 1037 CRISPR screens.
DR ChiTaRS; IL15; human.
DR EvolutionaryTrace; P40933; -.
DR GeneWiki; Interleukin_15; -.
DR GenomeRNAi; 3600; -.
DR Pharos; P40933; Tbio.
DR PRO; PR:P40933; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P40933; protein.
DR Bgee; ENSG00000164136; Expressed in decidua and 150 other tissues.
DR Genevisible; P40933; HS.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005768; C:endosome; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; TAS:ProtInc.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR GO; GO:0005126; F:cytokine receptor binding; IEA:InterPro.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0048469; P:cell maturation; IEA:Ensembl.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:0071305; P:cellular response to vitamin D; IEA:Ensembl.
DR GO; GO:0045062; P:extrathymic T cell selection; IEA:Ensembl.
DR GO; GO:0030212; P:hyaluronan metabolic process; IEA:Ensembl.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR GO; GO:0035723; P:interleukin-15-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0048535; P:lymph node development; IEA:Ensembl.
DR GO; GO:0030225; P:macrophage differentiation; IDA:ARUK-UCL.
DR GO; GO:0001779; P:natural killer cell differentiation; IEA:Ensembl.
DR GO; GO:0001787; P:natural killer cell proliferation; IEA:Ensembl.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0042119; P:neutrophil activation; IDA:UniProtKB.
DR GO; GO:0001866; P:NK T cell proliferation; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:0001819; P:positive regulation of cytokine production; IBA:GO_Central.
DR GO; GO:0050778; P:positive regulation of immune response; IBA:GO_Central.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IC:BHF-UCL.
DR GO; GO:0032740; P:positive regulation of interleukin-17 production; IDA:BHF-UCL.
DR GO; GO:0032825; P:positive regulation of natural killer cell differentiation; IEA:Ensembl.
DR GO; GO:0032819; P:positive regulation of natural killer cell proliferation; IEA:Ensembl.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IDA:UniProtKB.
DR GO; GO:1904100; P:positive regulation of protein O-linked glycosylation; IEA:Ensembl.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IBA:GO_Central.
DR GO; GO:0034105; P:positive regulation of tissue remodeling; IC:BHF-UCL.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IBA:GO_Central.
DR GO; GO:0050691; P:regulation of defense response to virus by host; IEA:Ensembl.
DR GO; GO:0045580; P:regulation of T cell differentiation; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0014732; P:skeletal muscle atrophy; IEA:Ensembl.
DR GO; GO:0007260; P:tyrosine phosphorylation of STAT protein; IDA:CACAO.
DR Gene3D; 1.20.1250.70; -; 1.
DR InterPro; IPR009079; 4_helix_cytokine-like_core.
DR InterPro; IPR020439; IL-15.
DR InterPro; IPR003443; IL-15/IL-21_fam.
DR InterPro; IPR020466; IL-15_mml.
DR PANTHER; PTHR14356; PTHR14356; 1.
DR Pfam; PF02372; IL15; 1.
DR PRINTS; PR01947; INTLKN15MAML.
DR PRINTS; PR01930; INTRLEUKIN15.
DR SUPFAM; SSF47266; SSF47266; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytokine; Cytoplasm; Disulfide bond;
KW Glycoprotein; Nucleus; Reference proteome; Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT PROPEP 30..48
FT /evidence="ECO:0000255"
FT /id="PRO_0000015393"
FT CHAIN 49..162
FT /note="Interleukin-15"
FT /id="PRO_0000015394"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 83..133
FT /evidence="ECO:0000269|PubMed:21167836"
FT DISULFID 90..136
FT /evidence="ECO:0000269|PubMed:21167836"
FT VAR_SEQ 1..37
FT /note="MRISKPHLRSISIQCYLCLLLNSHFLTEAGIHVFILG -> MVLGTIDLCS
FT (in isoform IL15-S21AA)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8668345,
FT ECO:0000303|PubMed:9405632, ECO:0000303|Ref.6,
FT ECO:0000303|Ref.8"
FT /id="VSP_002660"
FT CONFLICT 141
FT /note="E -> K (in Ref. 4; AAB97518)"
FT /evidence="ECO:0000305"
FT HELIX 49..64
FT /evidence="ECO:0007829|PDB:2Z3Q"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:2Z3Q"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:2Z3Q"
FT HELIX 84..102
FT /evidence="ECO:0007829|PDB:2Z3Q"
FT HELIX 105..119
FT /evidence="ECO:0007829|PDB:2Z3Q"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:2Z3Q"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:2Z3Q"
FT HELIX 144..158
FT /evidence="ECO:0007829|PDB:2Z3Q"
SQ SEQUENCE 162 AA; 18086 MW; 0CE0520C1D8379E2 CRC64;
MRISKPHLRS ISIQCYLCLL LNSHFLTEAG IHVFILGCFS AGLPKTEANW VNVISDLKKI
EDLIQSMHID ATLYTESDVH PSCKVTAMKC FLLELQVISL ESGDASIHDT VENLIILANN
SLSSNGNVTE SGCKECEELE EKNIKEFLQS FVHIVQMFIN TS
