ICOSL_HUMAN
ID ICOSL_HUMAN Reviewed; 302 AA.
AC O75144; A8MUZ1; Q9HD18; Q9NRQ1;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=ICOS ligand;
DE AltName: Full=B7 homolog 2;
DE Short=B7-H2;
DE AltName: Full=B7-like protein Gl50;
DE AltName: Full=B7-related protein 1;
DE Short=B7RP-1;
DE AltName: CD_antigen=CD275;
DE Flags: Precursor;
GN Name=ICOSLG; Synonyms=B7H2, B7RP1, ICOSL, KIAA0653;
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 1).
RC TISSUE=Dendritic cell;
RX PubMed=11023515;
RA Wang S., Zhu G., Chapoval A.I., Dong H., Tamada K., Ni J., Chen L.;
RT "Costimulation of T cells by B7-H2, a B7-like molecule that binds ICOS.";
RL Blood 96:2808-2813(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Peripheral blood lymphocyte;
RX PubMed=11007762; DOI=10.1093/intimm/12.10.1439;
RA Yoshinaga S.K., Zhang M., Pistillo J., Horan T., Khare S.D., Miner K.,
RA Sonnenberg M., Boone T., Brankow D., Dai T., Delaney J., Han H., Hui A.,
RA Kohno T., Manoukian R., Whoriskey J.S., Coccia M.A.;
RT "Characterization of a new human B7-related protein: B7RP-1 is the ligand
RT to the co-stimulatory protein ICOS.";
RL Int. Immunol. 12:1439-1447(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Leukocyte;
RX PubMed=10657606; DOI=10.4049/jimmunol.164.4.1653;
RA Ling V., Wu P.W., Finnerty H.F., Bean K.M., Spaulding V., Fouser L.A.,
RA Leonard J.P., Hunter S.E., Zollner R., Thomas J.L., Miyashiro J.S.,
RA Jacobs K.A., Collins M.;
RT "Identification of GL50, a novel B7-like protein that functionally binds to
RT ICOS receptor.";
RL J. Immunol. 164:1653-1657(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Ling V., Dunussi-Joannopolulos K.;
RT "GL50 molecules and uses therefor.";
RL Patent number WO0121796, 29-MAR-2001.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [8]
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [10]
RP TISSUE SPECIFICITY.
RX PubMed=10779774; DOI=10.4049/jimmunol.164.9.4689;
RA Aicher A., Hayden-Ledbetter M., Brady W.A., Pezzutto A., Richter G.,
RA Magaletti D., Buckwalter S., Ledbetter J.A., Clark E.A.;
RT "Characterization of human inducible costimulator ligand expression and
RT function.";
RL J. Immunol. 164:4689-4696(2000).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70 AND ASN-186.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [12]
RP INTERACTION WITH CTLA4.
RX PubMed=28484017; DOI=10.1073/pnas.1617941114;
RA Ramagopal U.A., Liu W., Garrett-Thomson S.C., Bonanno J.B., Yan Q.,
RA Srinivasan M., Wong S.C., Bell A., Mankikar S., Rangan V.S., Deshpande S.,
RA Korman A.J., Almo S.C.;
RT "Structural basis for cancer immunotherapy by the first-in-class checkpoint
RT inhibitor ipilimumab.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E4223-E4232(2017).
CC -!- FUNCTION: Ligand for the T-cell-specific cell surface receptor ICOS.
CC Acts as a costimulatory signal for T-cell proliferation and cytokine
CC secretion; induces also B-cell proliferation and differentiation into
CC plasma cells. Could play an important role in mediating local tissue
CC responses to inflammatory conditions, as well as in modulating the
CC secondary immune response by co-stimulating memory T-cell function (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CTLA4 (in vitro).
CC {ECO:0000269|PubMed:28484017}.
CC -!- INTERACTION:
CC O75144; Q9Y6W8: ICOS; NbExp=8; IntAct=EBI-12923856, EBI-3922712;
CC O75144; O75144: ICOSLG; NbExp=7; IntAct=EBI-12923856, EBI-12923856;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11007762};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=O75144-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75144-2; Sequence=VSP_002520;
CC Name=3;
CC IsoId=O75144-3; Sequence=VSP_054718;
CC -!- TISSUE SPECIFICITY: Isoform 1 is widely expressed (brain, heart,
CC kidney, liver, lung, pancreas, placenta, skeletal muscle, bone marrow,
CC colon, ovary, prostate, testis, lymph nodes, leukocytes, spleen, thymus
CC and tonsil), while isoform 2 is detected only in lymph nodes,
CC leukocytes and spleen. Expressed on activated monocytes and dendritic
CC cells. {ECO:0000269|PubMed:10779774}.
CC -!- INDUCTION: Constitutive expression is further enhanced by treatment
CC with TNF in peripheral blood B-cells and monocytes, while it is
CC decreased in dendritic cells.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. BTN/MOG family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA31628.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA31628.1; Type=Miscellaneous discrepancy; Note=The sequence differs from that shown in position 300 onward for unknown reason.; Evidence={ECO:0000305};
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DR EMBL; AF199028; AAF34739.1; -; mRNA.
DR EMBL; AF289028; AAG01176.1; -; mRNA.
DR EMBL; AF216749; AAK16241.1; -; mRNA.
DR EMBL; AX100595; CAC36465.1; -; mRNA.
DR EMBL; AB014553; BAA31628.1; ALT_SEQ; mRNA.
DR EMBL; AK090492; BAG52170.1; -; mRNA.
DR EMBL; AP001058; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP001059; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471079; EAX09446.1; -; Genomic_DNA.
DR EMBL; BC064637; AAH64637.1; -; mRNA.
DR CCDS; CCDS42952.1; -. [O75144-1]
DR CCDS; CCDS63377.1; -. [O75144-3]
DR CCDS; CCDS63379.1; -. [O75144-2]
DR RefSeq; NP_001269979.1; NM_001283050.1. [O75144-2]
DR RefSeq; NP_001269980.1; NM_001283051.1. [O75144-3]
DR RefSeq; NP_056074.1; NM_015259.5. [O75144-1]
DR RefSeq; XP_006723963.1; XM_006723900.2.
DR PDB; 6X4G; X-ray; 3.50 A; C=19-248.
DR PDB; 6X4T; X-ray; 3.15 A; A/C=19-248.
DR PDBsum; 6X4G; -.
DR PDBsum; 6X4T; -.
DR AlphaFoldDB; O75144; -.
DR SMR; O75144; -.
DR BioGRID; 116900; 21.
DR IntAct; O75144; 7.
DR ChEMBL; CHEMBL3712949; -.
DR GlyConnect; 740; 5 N-Linked glycans (3 sites).
DR GlyGen; O75144; 6 sites, 7 N-linked glycans (3 sites).
DR iPTMnet; O75144; -.
DR PhosphoSitePlus; O75144; -.
DR SwissPalm; O75144; -.
DR BioMuta; ICOSLG; -.
DR CPTAC; CPTAC-2600; -.
DR EPD; O75144; -.
DR jPOST; O75144; -.
DR MassIVE; O75144; -.
DR MaxQB; O75144; -.
DR PaxDb; O75144; -.
DR PeptideAtlas; O75144; -.
DR PRIDE; O75144; -.
DR ProteomicsDB; 2140; -.
DR ProteomicsDB; 49806; -. [O75144-1]
DR ProteomicsDB; 49807; -. [O75144-2]
DR TopDownProteomics; O75144-2; -. [O75144-2]
DR ABCD; O75144; 8 sequenced antibodies.
DR Antibodypedia; 24158; 813 antibodies from 44 providers.
DR CPTC; O75144; 1 antibody.
DR DNASU; 23308; -.
DR Ensembl; ENST00000344330.8; ENSP00000339477.4; ENSG00000160223.17. [O75144-2]
DR Ensembl; ENST00000400377.3; ENSP00000383228.3; ENSG00000160223.17. [O75144-3]
DR Ensembl; ENST00000407780.7; ENSP00000384432.3; ENSG00000160223.17. [O75144-1]
DR GeneID; 23308; -.
DR KEGG; hsa:23308; -.
DR MANE-Select; ENST00000407780.8; ENSP00000384432.3; NM_015259.6; NP_056074.1.
DR UCSC; uc002zee.5; human. [O75144-1]
DR CTD; 23308; -.
DR DisGeNET; 23308; -.
DR GeneCards; ICOSLG; -.
DR HGNC; HGNC:17087; ICOSLG.
DR HPA; ENSG00000160223; Tissue enhanced (bone marrow, brain).
DR MIM; 605717; gene.
DR neXtProt; NX_O75144; -.
DR OpenTargets; ENSG00000160223; -.
DR OpenTargets; ENSG00000277117; -.
DR PharmGKB; PA134977297; -.
DR VEuPathDB; HostDB:ENSG00000160223; -.
DR eggNOG; ENOG502SQ2A; Eukaryota.
DR GeneTree; ENSGT00940000161590; -.
DR HOGENOM; CLU_013137_8_2_1; -.
DR InParanoid; O75144; -.
DR OMA; VYWQIAD; -.
DR OrthoDB; 1537230at2759; -.
DR PhylomeDB; O75144; -.
DR TreeFam; TF331083; -.
DR PathwayCommons; O75144; -.
DR Reactome; R-HSA-388841; Costimulation by the CD28 family.
DR SignaLink; O75144; -.
DR BioGRID-ORCS; 102723996; 0 hits in 4 CRISPR screens.
DR BioGRID-ORCS; 23308; 8 hits in 1067 CRISPR screens.
DR ChiTaRS; ICOSLG; human.
DR GeneWiki; ICOSLG; -.
DR Pharos; O75144; Tbio.
DR PRO; PR:O75144; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; O75144; protein.
DR Bgee; ENSG00000160223; Expressed in cartilage tissue and 106 other tissues.
DR ExpressionAtlas; O75144; baseline and differential.
DR Genevisible; O75144; HS.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:HPA.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0042113; P:B cell activation; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; NAS:UniProtKB.
DR GO; GO:0006972; P:hyperosmotic response; NAS:UniProtKB.
DR GO; GO:0042104; P:positive regulation of activated T cell proliferation; TAS:UniProtKB.
DR GO; GO:0001817; P:regulation of cytokine production; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
DR GO; GO:0042110; P:T cell activation; NAS:UniProtKB.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Alternative splicing; B-cell activation;
KW Cell membrane; Disulfide bond; Glycoprotein; Immunity;
KW Immunoglobulin domain; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..302
FT /note="ICOS ligand"
FT /id="PRO_0000014803"
FT TOPO_DOM 19..256
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 278..302
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 19..129
FT /note="Ig-like V-type"
FT DOMAIN 141..227
FT /note="Ig-like C2-type"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 37..113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 158..216
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 18..134
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054718"
FT VAR_SEQ 300..302
FT /note="GHV -> ESWNLLLLLS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10657606, ECO:0000303|Ref.4"
FT /id="VSP_002520"
FT VARIANT 128
FT /note="V -> I (in dbSNP:rs11558819)"
FT /id="VAR_049880"
FT STRAND 20..28
FT /evidence="ECO:0007829|PDB:6X4T"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:6X4T"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:6X4T"
FT STRAND 50..59
FT /evidence="ECO:0007829|PDB:6X4T"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:6X4T"
FT TURN 78..83
FT /evidence="ECO:0007829|PDB:6X4T"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:6X4G"
FT HELIX 88..92
FT /evidence="ECO:0007829|PDB:6X4T"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:6X4T"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:6X4T"
FT STRAND 109..117
FT /evidence="ECO:0007829|PDB:6X4T"
FT TURN 118..121
FT /evidence="ECO:0007829|PDB:6X4T"
FT STRAND 122..136
FT /evidence="ECO:0007829|PDB:6X4T"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:6X4T"
FT STRAND 155..165
FT /evidence="ECO:0007829|PDB:6X4T"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:6X4T"
FT TURN 174..177
FT /evidence="ECO:0007829|PDB:6X4T"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:6X4T"
FT STRAND 185..191
FT /evidence="ECO:0007829|PDB:6X4T"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:6X4T"
FT STRAND 197..204
FT /evidence="ECO:0007829|PDB:6X4T"
FT STRAND 213..219
FT /evidence="ECO:0007829|PDB:6X4T"
FT TURN 220..223
FT /evidence="ECO:0007829|PDB:6X4T"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:6X4T"
SQ SEQUENCE 302 AA; 33349 MW; 647934E21B55E34A CRC64;
MRLGSPGLLF LLFSSLRADT QEKEVRAMVG SDVELSCACP EGSRFDLNDV YVYWQTSESK
TVVTYHIPQN SSLENVDSRY RNRALMSPAG MLRGDFSLRL FNVTPQDEQK FHCLVLSQSL
GFQEVLSVEV TLHVAANFSV PVVSAPHSPS QDELTFTCTS INGYPRPNVY WINKTDNSLL
DQALQNDTVF LNMRGLYDVV SVLRIARTPS VNIGCCIENV LLQQNLTVGS QTGNDIGERD
KITENPVSTG EKNAATWSIL AVLCLLVVVA VAIGWVCRDR CLQHSYAGAW AVSPETELTG
HV
