ID BTLA_HUMAN Reviewed; 289 AA. AC Q7Z6A9; Q3B831; Q3HS85; Q6ZNH9; DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 3. DT 24-JAN-2024, entry version 163. DE RecName: Full=B- and T-lymphocyte attenuator {ECO:0000303|PubMed:14652006, ECO:0000303|PubMed:15568026}; DE AltName: Full=B- and T-lymphocyte-associated protein; DE AltName: CD_antigen=CD272; DE Flags: Precursor; GN Name=BTLA {ECO:0000303|PubMed:12796776, ECO:0000312|HGNC:HGNC:21087}; 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), MUTAGENESIS OF TYR-226; TYR-257 AND RP TYR-282, GLYCOSYLATION, FUNCTION, INTERACTION WITH PTPN6 AND PTPN11, RP VARIANTS SER-157 AND LEU-267, AND SUBCELLULAR LOCATION. RX PubMed=12796776; DOI=10.1038/ni944; RA Watanabe N., Gavrieli M., Sedy J.R., Yang J., Fallarino F., Loftin S.K., RA Hurchla M.A., Zimmerman N., Sim J., Zang X., Murphy T.L., Russell J.H., RA Allison J.P., Murphy K.M.; RT "BTLA is a lymphocyte inhibitory receptor with similarities to CTLA-4 and RT PD-1."; RL Nat. Immunol. 4:670-679(2003). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT LEU-267. RA Mao Y., Wang X., Wu H., Chen Y., Ge Y., Chen J., Zhang X.; RT "Point mutations in the BTLA gene in multiple myeloma and other hematologic RT malignancies."; RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT LEU-267. RC TISSUE=Peripheral blood; RA Oaks M.K., Tector M.F., Mewissen G.; RT "Human BTLA mRNA alternate splice transcript lacking transmembrane encoding RT region."; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 2-289 (ISOFORM 1), AND VARIANTS SER-157 AND LEU-267. 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 [LARGE SCALE MRNA] OF 4-289 (ISOFORM 1), AND VARIANTS RP SER-157 AND LEU-267. RC TISSUE=Trachea; 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 FUNCTION, MUTAGENESIS OF TYR-226; TYR-257 AND TYR-282, AND INTERACTION WITH RP PTPN6 AND PTPN11. RX PubMed=14652006; DOI=10.1016/j.bbrc.2003.11.070; RA Gavrieli M., Watanabe N., Loftin S.K., Murphy T.L., Murphy K.M.; RT "Characterization of phosphotyrosine binding motifs in the cytoplasmic RT domain of B and T lymphocyte attenuator required for association with RT protein tyrosine phosphatases SHP-1 and SHP-2."; RL Biochem. Biophys. Res. Commun. 312:1236-1243(2003). RN [8] RP FUNCTION, INTERACTION WITH TNFRSF14, AND PHOSPHORYLATION. RX PubMed=15568026; DOI=10.1038/ni1144; RA Sedy J.R., Gavrieli M., Potter K.G., Hurchla M.A., Lindsley R.C., RA Hildner K., Scheu S., Pfeffer K., Ware C.F., Murphy T.L., Murphy K.M.; RT "B and T lymphocyte attenuator regulates T cell activation through RT interaction with herpesvirus entry mediator."; RL Nat. Immunol. 6:90-98(2005). RN [9] RP FUNCTION, SUBUNIT, AND INTERACTION WITH TNFRSF14. RX PubMed=18193050; DOI=10.1038/ni1554; RA Cai G., Anumanthan A., Brown J.A., Greenfield E.A., Zhu B., Freeman G.J.; RT "CD160 inhibits activation of human CD4+ T cells through interaction with RT herpesvirus entry mediator."; RL Nat. Immunol. 9:176-185(2008). RN [10] RP FUNCTION, SUBUNIT, AND INTERACTION WITH TNFRSF14. RX PubMed=19915044; DOI=10.4049/jimmunol.0902490; RA Cheung T.C., Oborne L.M., Steinberg M.W., Macauley M.G., Fukuyama S., RA Sanjo H., D'Souza C., Norris P.S., Pfeffer K., Murphy K.M., Kronenberg M., RA Spear P.G., Ware C.F.; RT "T cell intrinsic heterodimeric complexes between HVEM and BTLA determine RT receptivity to the surrounding microenvironment."; RL J. Immunol. 183:7286-7296(2009). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 26-137 IN COMPLEX WITH TNFRSF14, RP AND DISULFIDE BONDS. RX PubMed=16169851; DOI=10.1074/jbc.m507629200; RA Compaan D.M., Gonzalez L.C., Tom I., Loyet K.M., Eaton D., Hymowitz S.G.; RT "Attenuating lymphocyte activity: the crystal structure of the BTLA-HVEM RT complex."; RL J. Biol. Chem. 280:39553-39561(2005). CC -!- FUNCTION: Inhibitory receptor on lymphocytes that negatively regulates CC antigen receptor signaling via PTPN6/SHP-1 and PTPN11/SHP-2 CC (PubMed:12796776, PubMed:14652006, PubMed:15568026, PubMed:18193050). CC May interact in cis (on the same cell) or in trans (on other cells) CC with TNFRSF14 (PubMed:19915044). In cis interactions, appears to play CC an immune regulatory role inhibiting in trans interactions in naive T CC cells to maintain a resting state. In trans interactions, can CC predominate during adaptive immune response to provide survival signals CC to effector T cells (PubMed:19915044). {ECO:0000269|PubMed:12796776, CC ECO:0000269|PubMed:14652006, ECO:0000269|PubMed:15568026, CC ECO:0000269|PubMed:18193050, ECO:0000269|PubMed:19915044}. CC -!- SUBUNIT: Interacts with tyrosine phosphatases PTPN6/SHP-1 and CC PTPN11/SHP-2 (PubMed:12796776, PubMed:14652006). Interacts with CC TNFRSF14/HVEM (via cysteine-rich domain 1) (PubMed:15568026, CC PubMed:18193050, PubMed:19915044). {ECO:0000269|PubMed:12796776, CC ECO:0000269|PubMed:14652006, ECO:0000269|PubMed:15568026, CC ECO:0000269|PubMed:16169851, ECO:0000269|PubMed:18193050, CC ECO:0000269|PubMed:19915044}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12796776}; CC Single-pass type I membrane protein {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q7Z6A9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q7Z6A9-2; Sequence=VSP_040305; CC -!- PTM: Phosphorylated on Tyr residues by TNFRSF14 and by antigen CC receptors cross-linking, both inducing association with PTPN6 and CC PTPN11. {ECO:0000269|PubMed:15568026}. CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12796776}. CC -!- SEQUENCE CAUTION: CC Sequence=BAD18396.1; Type=Erroneous initiation; Note=Truncated N-terminus.; 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; AY293286; AAP44003.1; -; mRNA. DR EMBL; AY599411; AAT44901.1; -; mRNA. DR EMBL; DQ198368; ABA54407.1; -; mRNA. DR EMBL; AC092894; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC107091; AAI07092.1; -; mRNA. DR EMBL; BC107092; AAI07093.1; -; mRNA. DR EMBL; AK131204; BAD18396.1; ALT_INIT; mRNA. DR CCDS; CCDS33819.1; -. [Q7Z6A9-1] DR CCDS; CCDS43130.1; -. [Q7Z6A9-2] DR RefSeq; NP_001078826.1; NM_001085357.1. [Q7Z6A9-2] DR RefSeq; NP_861445.3; NM_181780.3. [Q7Z6A9-1] DR RefSeq; XP_016861237.1; XM_017005748.1. [Q7Z6A9-1] DR PDB; 2AW2; X-ray; 2.80 A; A/X=26-137. DR PDB; 6NYP; X-ray; 2.70 A; A/B/C/D=31-137. DR PDB; 8F60; X-ray; 1.64 A; C=31-150. DR PDB; 8F6L; X-ray; 1.85 A; C=31-150. DR PDB; 8F6O; X-ray; 2.31 A; C=31-150. DR PDBsum; 2AW2; -. DR PDBsum; 6NYP; -. DR PDBsum; 8F60; -. DR PDBsum; 8F6L; -. DR PDBsum; 8F6O; -. DR AlphaFoldDB; Q7Z6A9; -. DR SMR; Q7Z6A9; -. DR BioGRID; 127411; 39. DR DIP; DIP-48795N; -. DR IntAct; Q7Z6A9; 3. DR MINT; Q7Z6A9; -. DR STRING; 9606.ENSP00000333919; -. DR GlyCosmos; Q7Z6A9; 3 sites, No reported glycans. DR GlyGen; Q7Z6A9; 3 sites. DR iPTMnet; Q7Z6A9; -. DR PhosphoSitePlus; Q7Z6A9; -. DR SwissPalm; Q7Z6A9; -. DR BioMuta; BTLA; -. DR DMDM; 296439425; -. DR jPOST; Q7Z6A9; -. DR MassIVE; Q7Z6A9; -. DR PaxDb; 9606-ENSP00000333919; -. DR PeptideAtlas; Q7Z6A9; -. DR ProteomicsDB; 69387; -. [Q7Z6A9-1] DR ProteomicsDB; 69388; -. [Q7Z6A9-2] DR TopDownProteomics; Q7Z6A9-1; -. [Q7Z6A9-1] DR TopDownProteomics; Q7Z6A9-2; -. [Q7Z6A9-2] DR ABCD; Q7Z6A9; 2 sequenced antibodies. DR Antibodypedia; 16304; 1031 antibodies from 44 providers. DR CPTC; Q7Z6A9; 3 antibodies. DR DNASU; 151888; -. DR Ensembl; ENST00000334529.10; ENSP00000333919.5; ENSG00000186265.10. [Q7Z6A9-1] DR Ensembl; ENST00000383680.4; ENSP00000373178.4; ENSG00000186265.10. [Q7Z6A9-2] DR GeneID; 151888; -. DR KEGG; hsa:151888; -. DR MANE-Select; ENST00000334529.10; ENSP00000333919.5; NM_181780.4; NP_861445.4. DR UCSC; uc003dza.5; human. [Q7Z6A9-1] DR AGR; HGNC:21087; -. DR CTD; 151888; -. DR DisGeNET; 151888; -. DR GeneCards; BTLA; -. DR HGNC; HGNC:21087; BTLA. DR HPA; ENSG00000186265; Tissue enriched (lymphoid). DR MIM; 607925; gene. DR neXtProt; NX_Q7Z6A9; -. DR OpenTargets; ENSG00000186265; -. DR PharmGKB; PA134968341; -. DR VEuPathDB; HostDB:ENSG00000186265; -. DR eggNOG; ENOG502S8FS; Eukaryota. DR GeneTree; ENSGT00390000017390; -. DR HOGENOM; CLU_085244_0_0_1; -. DR InParanoid; Q7Z6A9; -. DR OMA; NVTWCKF; -. DR OrthoDB; 5359457at2759; -. DR PhylomeDB; Q7Z6A9; -. DR TreeFam; TF337694; -. DR PathwayCommons; Q7Z6A9; -. DR Reactome; R-HSA-388841; Costimulation by the CD28 family. DR SignaLink; Q7Z6A9; -. DR BioGRID-ORCS; 151888; 15 hits in 1154 CRISPR screens. DR EvolutionaryTrace; Q7Z6A9; -. DR GeneWiki; BTLA; -. DR GenomeRNAi; 151888; -. DR Pharos; Q7Z6A9; Tbio. DR PRO; PR:Q7Z6A9; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q7Z6A9; Protein. DR Bgee; ENSG00000186265; Expressed in lymph node and 101 other cell types or tissues. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central. DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW. DR GO; GO:0002768; P:immune response-regulating cell surface receptor signaling pathway; IBA:GO_Central. DR CDD; cd20928; IgI_BTLA; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 1. DR InterPro; IPR039257; BTLA. 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; IPR013151; Immunoglobulin. DR PANTHER; PTHR37996; B- AND T-LYMPHOCYTE ATTENUATOR; 1. DR PANTHER; PTHR37996:SF1; B- AND T-LYMPHOCYTE ATTENUATOR; 1. DR Pfam; PF00047; ig; 1. DR SMART; SM00409; IG; 1. DR SUPFAM; SSF48726; Immunoglobulin; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR Genevisible; Q7Z6A9; HS. PE 1: Evidence at protein level; KW 3D-structure; Adaptive immunity; Alternative splicing; Cell membrane; KW Disulfide bond; Glycoprotein; Immunity; Immunoglobulin domain; Membrane; KW Phosphoprotein; Receptor; Reference proteome; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1..30 FT /evidence="ECO:0000255" FT CHAIN 31..289 FT /note="B- and T-lymphocyte attenuator" FT /id="PRO_0000014523" FT TOPO_DOM 31..157 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 158..178 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 179..289 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 31..132 FT /note="Ig-like V-type" FT CARBOHYD 75 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 94 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 110 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 34..63 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:16169851" FT DISULFID 58..115 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:16169851" FT DISULFID 72..79 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:16169851" FT VAR_SEQ 135..182 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2, FT ECO:0000303|Ref.3" FT /id="VSP_040305" FT VARIANT 124 FT /note="I -> V (in dbSNP:rs16859633)" FT /id="VAR_056027" FT VARIANT 157 FT /note="R -> S (in dbSNP:rs2931761)" FT /evidence="ECO:0000269|PubMed:12796776, FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334" FT /id="VAR_027607" FT VARIANT 267 FT /note="P -> L (in dbSNP:rs9288952)" FT /evidence="ECO:0000269|PubMed:12796776, FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334, FT ECO:0000269|Ref.2, ECO:0000269|Ref.3" FT /id="VAR_027608" FT MUTAGEN 226 FT /note="Y->F: No change of phosphorylation implicated in FT interaction with PTPN6 and PTPN11. Severe reduction of FT phosphorylation; when associated with F-257 and/or F-282." FT /evidence="ECO:0000269|PubMed:12796776, FT ECO:0000269|PubMed:14652006" FT MUTAGEN 257 FT /note="Y->F: No change of phosphorylation implicated in FT interaction with PTPN6 and PTPN11. Severe reduction of FT phosphorylation; when associated with F-226 and/or F-282." FT /evidence="ECO:0000269|PubMed:12796776, FT ECO:0000269|PubMed:14652006" FT MUTAGEN 282 FT /note="Y->F: No change of phosphorylation implicated in FT interaction with PTPN6 and PTPN11. Severe reduction of FT phosphorylation; when associated with F-226 and/or F-257." FT /evidence="ECO:0000269|PubMed:12796776, FT ECO:0000269|PubMed:14652006" FT CONFLICT 105 FT /note="V -> M (in Ref. 1; AAP44003)" FT /evidence="ECO:0000305" FT CONFLICT 138 FT /note="S -> G (in Ref. 1; AAP44003)" FT /evidence="ECO:0000305" FT CONFLICT 148 FT /note="M -> V (in Ref. 1; AAP44003)" FT /evidence="ECO:0000305" FT CONFLICT 171 FT /note="C -> W (in Ref. 1; AAP44003)" FT /evidence="ECO:0000305" FT CONFLICT 219 FT /note="L -> P (in Ref. 6; BAD18396)" FT /evidence="ECO:0000305" FT CONFLICT 223 FT /note="T -> A (in Ref. 1; AAP44003)" FT /evidence="ECO:0000305" FT CONFLICT 243 FT /note="Y -> C (in Ref. 1; AAP44003)" FT /evidence="ECO:0000305" FT STRAND 44..49 FT /evidence="ECO:0007829|PDB:8F60" FT STRAND 54..61 FT /evidence="ECO:0007829|PDB:8F60" FT STRAND 63..65 FT /evidence="ECO:0007829|PDB:8F60" FT STRAND 70..75 FT /evidence="ECO:0007829|PDB:8F60" FT STRAND 78..81 FT /evidence="ECO:0007829|PDB:8F60" FT STRAND 87..92 FT /evidence="ECO:0007829|PDB:8F60" FT STRAND 95..102 FT /evidence="ECO:0007829|PDB:8F60" FT HELIX 107..109 FT /evidence="ECO:0007829|PDB:8F60" FT STRAND 111..119 FT /evidence="ECO:0007829|PDB:8F60" FT STRAND 122..125 FT /evidence="ECO:0007829|PDB:8F60" FT STRAND 129..134 FT /evidence="ECO:0007829|PDB:8F60" SQ SEQUENCE 289 AA; 32834 MW; F4D1FF775D7D33F3 CRC64; MKTLPAMLGT GKLFWVFFLI PYLDIWNIHG KESCDVQLYI KRQSEHSILA GDPFELECPV KYCANRPHVT WCKLNGTTCV KLEDRQTSWK EEKNISFFIL HFEPVLPNDN GSYRCSANFQ SNLIESHSTT LYVTDVKSAS ERPSKDEMAS RPWLLYRLLP LGGLPLLITT CFCLFCCLRR HQGKQNELSD TAGREINLVD AHLKSEQTEA STRQNSQVLL SETGIYDNDP DLCFRMQEGS EVYSNPCLEE NKPGIVYASL NHSVIGPNSR LARNVKEAPT EYASICVRS //