BTLA_HUMAN
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 03-AUG-2022, entry version 155.
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};
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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 PDBsum; 2AW2; -.
DR PDBsum; 6NYP; -.
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 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; Q7Z6A9; -.
DR PeptideAtlas; Q7Z6A9; -.
DR PRIDE; 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; 917 antibodies from 43 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 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; 1342267at2759; -.
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; 11 hits in 1070 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 99 other tissues.
DR Genevisible; Q7Z6A9; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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 Gene3D; 2.60.40.10; -; 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; PTHR37996; 1.
DR Pfam; PF00047; ig; 1.
DR SMART; SM00409; IG; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
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 45..49
FT /evidence="ECO:0007829|PDB:6NYP"
FT STRAND 54..61
FT /evidence="ECO:0007829|PDB:6NYP"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:6NYP"
FT STRAND 68..75
FT /evidence="ECO:0007829|PDB:6NYP"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:6NYP"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:6NYP"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:6NYP"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:6NYP"
FT STRAND 111..119
FT /evidence="ECO:0007829|PDB:6NYP"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:6NYP"
FT STRAND 129..134
FT /evidence="ECO:0007829|PDB:6NYP"
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
