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Database: UniProt
Entry: Q15399
LinkDB: Q15399
Original site: Q15399 
ID   TLR1_HUMAN              Reviewed;         786 AA.
AC   Q15399; D1CS39; D1CS41; O15452; Q32MK3; Q32MK4; Q9UG90;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 3.
DT   26-NOV-2014, entry version 155.
DE   RecName: Full=Toll-like receptor 1;
DE   AltName: Full=Toll/interleukin-1 receptor-like protein;
DE            Short=TIL;
DE   AltName: CD_antigen=CD281;
DE   Flags: Precursor;
GN   Name=TLR1; Synonyms=KIAA0012;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS SER-248 AND ILE-602.
RC   TISSUE=Erythroleukemia;
RX   PubMed=9435236; DOI=10.1073/pnas.95.2.588;
RA   Rock F.L., Hardiman G., Timans J.C., Kastelein R.A., Bazan J.F.;
RT   "A family of human receptors structurally related to Drosophila
RT   Toll.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:588-593(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=18810425; DOI=10.1007/s00251-008-0332-0;
RA   Nakajima T., Ohtani H., Satta Y., Uno Y., Akari H., Ishida T.,
RA   Kimura A.;
RT   "Natural selection in the TLR-related genes in the course of primate
RT   evolution.";
RL   Immunogenetics 60:727-735(2008).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS THR-80 AND ILE-602.
RX   PubMed=19924287; DOI=10.1371/journal.pone.0007803;
RA   Georgel P., Macquin C., Bahram S.;
RT   "The heterogeneous allelic repertoire of human Toll-Like receptor
RT   (TLR) genes.";
RL   PLoS ONE 4:E7803-E7803(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-80.
RC   TISSUE=Bone marrow;
RX   PubMed=7584026; DOI=10.1093/dnares/1.1.27;
RA   Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y.,
RA   Sato S., Nagase T., Seki N., Ishikawa K., Tabata S.;
RT   "Prediction of the coding sequences of unidentified human genes. I.
RT   The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by
RT   analysis of randomly sampled cDNA clones from human immature myeloid
RT   cell line KG-1.";
RL   DNA Res. 1:27-35(1994).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS SER-248 AND
RP   ILE-602.
RC   TISSUE=Brain;
RX   PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA   Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA   Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA   Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA   Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA   Wambutt R., Korn B., Klein M., Poustka A.;
RT   "Towards a catalog of human genes and proteins: sequencing and
RT   analysis of 500 novel complete protein coding human cDNAs.";
RL   Genome Res. 11:422-435(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS SER-248 AND
RP   ILE-602.
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PROTEIN SEQUENCE OF 25-39.
RX   PubMed=15340161; DOI=10.1110/ps.04682504;
RA   Zhang Z., Henzel W.J.;
RT   "Signal peptide prediction based on analysis of experimentally
RT   verified cleavage sites.";
RL   Protein Sci. 13:2819-2824(2004).
RN   [8]
RP   INVOLVEMENT IN PROTECTION AGAINST LEPROSY.
RX   PubMed=17548585; DOI=10.4049/jimmunol.178.12.7520;
RA   Johnson C.M., Lyle E.A., Omueti K.O., Stepensky V.A., Yegin O.,
RA   Alpsoy E., Hamann L., Schumann R.R., Tapping R.I.;
RT   "Cutting edge: A common polymorphism impairs cell surface trafficking
RT   and functional responses of TLR1 but protects against leprosy.";
RL   J. Immunol. 178:7520-7524(2007).
RN   [9]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-163.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of
RT   multiple enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 625-785.
RX   PubMed=11081518; DOI=10.1038/35040600;
RA   Xu Y., Tao X., Shen B., Horng T., Medzhitov R., Manley J.L., Tong L.;
RT   "Structural basis for signal transduction by the Toll/interleukin-1
RT   receptor domains.";
RL   Nature 408:111-115(2000).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 25-476 IN COMPLEX WITH TLR1
RP   AND BACTERIAL LIPOPEPTIDE ANALOG, DISULFIDE BONDS, AND GLYCOSYLATION
RP   AT ASN-51; ASN-163; ASN-330 AND ASN-429.
RX   PubMed=17889651; DOI=10.1016/j.cell.2007.09.008;
RA   Jin M.S., Kim S.E., Heo J.Y., Lee M.E., Kim H.M., Paik S.-G., Lee H.,
RA   Lee J.-O.;
RT   "Crystal structure of the TLR1-TLR2 heterodimer induced by binding of
RT   a tri-acylated lipopeptide.";
RL   Cell 130:1071-1082(2007).
RN   [12]
RP   ASSOCIATION OF VARIANT SER-248 WITH SUSCEPTIBILITY TO LEPROSY.
RX   PubMed=19456232; DOI=10.1086/599121;
RA   Schuring R.P., Hamann L., Faber W.R., Pahan D., Richardus J.H.,
RA   Schumann R.R., Oskam L.;
RT   "Polymorphism N248S in the human Toll-like receptor 1 gene is related
RT   to leprosy and leprosy reactions.";
RL   J. Infect. Dis. 199:1816-1819(2009).
RN   [13]
RP   VARIANTS PRO-44; THR-75; THR-80; TYR-118; SER-248; LEU-305; LEU-315;
RP   ASN-352; VAL-460; ALA-542; CYS-554; GLY-587; ILE-602; ALA-651;
RP   ALA-674; PRO-720 AND LEU-733, AND CHARACTERIZATION OF VARIANTS
RP   LEU-315; CYS-554; ILE-602; ALA-651 AND PRO-720.
RX   PubMed=21618349; DOI=10.1002/humu.21486;
RA   Ben-Ali M., Corre B., Manry J., Barreiro L.B., Quach H., Boniotto M.,
RA   Pellegrini S., Quintana-Murci L.;
RT   "Functional characterization of naturally occurring genetic variants
RT   in the human TLR1-2-6 gene family.";
RL   Hum. Mutat. 32:643-652(2011).
CC   -!- FUNCTION: Participates in the innate immune response to microbial
CC       agents. Specifically recognizes diacylated and triacylated
CC       lipopeptides. Cooperates with TLR2 to mediate the innate immune
CC       response to bacterial lipoproteins or lipopeptides. Acts via MYD88
CC       and TRAF6, leading to NF-kappa-B activation, cytokine secretion
CC       and the inflammatory response (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Binds MYD88 (via TIR domain). Interacts with CNPY3 (By
CC       similarity). Interacts (via extracellular domain) with TLR2.
CC       Ligand binding induces the formation of a heterodimer with TLR2.
CC       {ECO:0000250, ECO:0000269|PubMed:17889651}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass
CC       type I membrane protein {ECO:0000250}. Cytoplasmic vesicle,
CC       phagosome membrane {ECO:0000250}; Single-pass type I membrane
CC       protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in spleen, ovary,
CC       peripheral blood leukocytes, thymus and small intestine.
CC   -!- POLYMORPHISM: Genetic variations in TLR1 may influence
CC       susceptibility to or protection against contracting leprosy and
CC       define the leprosy susceptibility locus 5 [MIM:613223]. Ser-602 is
CC       a common allele in Caucasians. It is associated with impaired cell
CC       surface expression and receptor function resulting in protection
CC       against leprosy.
CC   -!- SIMILARITY: Belongs to the Toll-like receptor family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Contains 19 LRR (leucine-rich) repeats. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 LRRCT domain. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 TIR domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00204}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA02801.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U88540; AAC34137.1; -; mRNA.
DR   EMBL; AB445617; BAG55014.1; -; mRNA.
DR   EMBL; DQ012259; AAY85638.1; -; mRNA.
DR   EMBL; DQ012260; AAY85639.1; -; mRNA.
DR   EMBL; DQ012261; AAY85640.1; -; mRNA.
DR   EMBL; D13637; BAA02801.2; ALT_INIT; mRNA.
DR   EMBL; AL050262; CAB43364.1; -; mRNA.
DR   EMBL; BC109093; AAI09094.1; -; mRNA.
DR   EMBL; BC109094; AAI09095.1; -; mRNA.
DR   CCDS; CCDS33973.1; -.
DR   PIR; T08664; T08664.
DR   RefSeq; NP_003254.2; NM_003263.3.
DR   RefSeq; XP_005262719.1; XM_005262662.2.
DR   RefSeq; XP_005262720.1; XM_005262663.2.
DR   RefSeq; XP_005262722.1; XM_005262665.2.
DR   RefSeq; XP_005262723.1; XM_005262666.2.
DR   RefSeq; XP_006714091.1; XM_006714028.1.
DR   UniGene; Hs.621817; -.
DR   UniGene; Hs.654532; -.
DR   PDB; 1FYV; X-ray; 2.90 A; A=625-785.
DR   PDB; 2Z7X; X-ray; 2.10 A; B=25-475.
DR   PDBsum; 1FYV; -.
DR   PDBsum; 2Z7X; -.
DR   ProteinModelPortal; Q15399; -.
DR   SMR; Q15399; 25-578, 625-785.
DR   BioGrid; 112951; 2.
DR   STRING; 9606.ENSP00000354932; -.
DR   PhosphoSite; Q15399; -.
DR   DMDM; 146291086; -.
DR   PaxDb; Q15399; -.
DR   PRIDE; Q15399; -.
DR   Ensembl; ENST00000308979; ENSP00000354932; ENSG00000174125.
DR   Ensembl; ENST00000502213; ENSP00000421259; ENSG00000174125.
DR   GeneID; 7096; -.
DR   KEGG; hsa:7096; -.
DR   UCSC; uc003gtl.3; human.
DR   CTD; 7096; -.
DR   GeneCards; GC04M038797; -.
DR   HGNC; HGNC:11847; TLR1.
DR   MIM; 601194; gene.
DR   MIM; 613223; phenotype.
DR   neXtProt; NX_Q15399; -.
DR   PharmGKB; PA36549; -.
DR   eggNOG; NOG272762; -.
DR   GeneTree; ENSGT00760000119006; -.
DR   HOGENOM; HOG000008676; -.
DR   HOVERGEN; HBG023180; -.
DR   InParanoid; Q15399; -.
DR   KO; K05398; -.
DR   OMA; KEFGNMS; -.
DR   OrthoDB; EOG7GN2M5; -.
DR   PhylomeDB; Q15399; -.
DR   TreeFam; TF351113; -.
DR   EvolutionaryTrace; Q15399; -.
DR   GeneWiki; TLR_1; -.
DR   GenomeRNAi; 7096; -.
DR   NextBio; 27759; -.
DR   PRO; PR:Q15399; -.
DR   Bgee; Q15399; -.
DR   CleanEx; HS_TLR1; -.
DR   ExpressionAtlas; Q15399; baseline and differential.
DR   Genevestigator; Q15399; -.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR   GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; TAS:ProtInc.
DR   GO; GO:0035354; C:Toll-like receptor 1-Toll-like receptor 2 protein complex; IDA:MGI.
DR   GO; GO:0046982; F:protein heterodimerization activity; IDA:MGI.
DR   GO; GO:0004872; F:receptor activity; TAS:ProtInc.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; NAS:UniProtKB.
DR   GO; GO:0071727; P:cellular response to triacyl bacterial lipopeptide; IDA:MGI.
DR   GO; GO:0042495; P:detection of triacyl bacterial lipopeptide; IDA:MGI.
DR   GO; GO:0006955; P:immune response; TAS:ProtInc.
DR   GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0042116; P:macrophage activation; NAS:UniProtKB.
DR   GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0045410; P:positive regulation of interleukin-6 biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0042535; P:positive regulation of tumor necrosis factor biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0050707; P:regulation of cytokine secretion; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   GO; GO:0034130; P:toll-like receptor 1 signaling pathway; IEA:InterPro.
DR   Gene3D; 3.40.50.10140; -; 1.
DR   InterPro; IPR000483; Cys-rich_flank_reg_C.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR000157; TIR_dom.
DR   InterPro; IPR027190; TLR1.
DR   InterPro; IPR017241; Toll-like_receptor.
DR   PANTHER; PTHR24365:SF261; PTHR24365:SF261; 1.
DR   Pfam; PF13855; LRR_8; 2.
DR   Pfam; PF01582; TIR; 1.
DR   PIRSF; PIRSF037595; Toll-like_receptor; 1.
DR   SMART; SM00082; LRRCT; 1.
DR   SMART; SM00255; TIR; 1.
DR   SUPFAM; SSF52200; SSF52200; 1.
DR   PROSITE; PS51450; LRR; 10.
DR   PROSITE; PS50104; TIR; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Complete proteome; Cytoplasmic vesicle;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Immunity;
KW   Inflammatory response; Innate immunity; Leucine-rich repeat; Membrane;
KW   Polymorphism; Receptor; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     24       {ECO:0000269|PubMed:15340161}.
FT   CHAIN        25    786       Toll-like receptor 1.
FT                                /FTId=PRO_0000034705.
FT   TOPO_DOM     25    580       Extracellular. {ECO:0000255}.
FT   TRANSMEM    581    601       Helical. {ECO:0000255}.
FT   TOPO_DOM    602    786       Cytoplasmic. {ECO:0000255}.
FT   REPEAT       54     77       LRR 1.
FT   REPEAT       78    101       LRR 2.
FT   REPEAT      102    125       LRR 3.
FT   REPEAT      126    150       LRR 4.
FT   REPEAT      151    175       LRR 5.
FT   REPEAT      176    199       LRR 6.
FT   REPEAT      200    223       LRR 7.
FT   REPEAT      224    250       LRR 8.
FT   REPEAT      251    278       LRR 9.
FT   REPEAT      279    308       LRR 10.
FT   REPEAT      309    337       LRR 11.
FT   REPEAT      338    361       LRR 12.
FT   REPEAT      362    388       LRR 13.
FT   REPEAT      389    414       LRR 14.
FT   REPEAT      415    437       LRR 15.
FT   REPEAT      438    457       LRR 16.
FT   REPEAT      458    478       LRR 17.
FT   REPEAT      479    500       LRR 18.
FT   REPEAT      501    524       LRR 19.
FT   DOMAIN      525    579       LRRCT.
FT   DOMAIN      635    779       TIR. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00204}.
FT   REGION      313    316       Interaction with bacterial lipopeptide.
FT   CARBOHYD     51     51       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:17889651}.
FT   CARBOHYD    137    137       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    163    163       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:17889651,
FT                                ECO:0000269|PubMed:19159218}.
FT   CARBOHYD    330    330       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:17889651}.
FT   CARBOHYD    429    429       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:17889651}.
FT   CARBOHYD    578    578       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID    110    132       {ECO:0000269|PubMed:17889651}.
FT   DISULFID    223    230       {ECO:0000269|PubMed:17889651}.
FT   DISULFID    343    368       {ECO:0000269|PubMed:17889651}.
FT   DISULFID    419    442       {ECO:0000269|PubMed:17889651}.
FT   VARIANT      44     44       S -> P (in dbSNP:rs76600635).
FT                                {ECO:0000269|PubMed:21618349}.
FT                                /FTId=VAR_066340.
FT   VARIANT      75     75       I -> T (in dbSNP:rs137853170).
FT                                {ECO:0000269|PubMed:21618349}.
FT                                /FTId=VAR_066341.
FT   VARIANT      80     80       R -> T (in dbSNP:rs5743611).
FT                                {ECO:0000269|PubMed:19924287,
FT                                ECO:0000269|PubMed:21618349,
FT                                ECO:0000269|PubMed:7584026}.
FT                                /FTId=VAR_031916.
FT   VARIANT     118    118       H -> Y (in dbSNP:rs5743612).
FT                                {ECO:0000269|PubMed:21618349}.
FT                                /FTId=VAR_018474.
FT   VARIANT     248    248       N -> S (may confer susceptibility to
FT                                leprosy; dbSNP:rs4833095).
FT                                {ECO:0000269|PubMed:11230166,
FT                                ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:21618349,
FT                                ECO:0000269|PubMed:9435236}.
FT                                /FTId=VAR_031917.
FT   VARIANT     305    305       H -> L (in dbSNP:rs3923647).
FT                                {ECO:0000269|PubMed:21618349}.
FT                                /FTId=VAR_031918.
FT   VARIANT     315    315       P -> L (severe impairment of activity;
FT                                dbSNP:rs5743613).
FT                                {ECO:0000269|PubMed:21618349}.
FT                                /FTId=VAR_031919.
FT   VARIANT     352    352       H -> N (in dbSNP:rs76796448).
FT                                {ECO:0000269|PubMed:21618349}.
FT                                /FTId=VAR_066342.
FT   VARIANT     460    460       I -> V (in dbSNP:rs137853171).
FT                                {ECO:0000269|PubMed:21618349}.
FT                                /FTId=VAR_066343.
FT   VARIANT     542    542       V -> A (in dbSNP:rs137853172).
FT                                {ECO:0000269|PubMed:21618349}.
FT                                /FTId=VAR_066344.
FT   VARIANT     554    554       Y -> C (severe impairment of activity).
FT                                {ECO:0000269|PubMed:21618349}.
FT                                /FTId=VAR_066345.
FT   VARIANT     587    587       V -> G (in dbSNP:rs5743617).
FT                                {ECO:0000269|PubMed:21618349}.
FT                                /FTId=VAR_031920.
FT   VARIANT     602    602       S -> I (severe impairment of activity;
FT                                dbSNP:rs5743618).
FT                                {ECO:0000269|PubMed:11230166,
FT                                ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:19924287,
FT                                ECO:0000269|PubMed:21618349,
FT                                ECO:0000269|PubMed:9435236}.
FT                                /FTId=VAR_031921.
FT   VARIANT     631    631       L -> R (in dbSNP:rs5743619).
FT                                /FTId=VAR_052358.
FT   VARIANT     651    651       V -> A (severe impairment of activity).
FT                                {ECO:0000269|PubMed:21618349}.
FT                                /FTId=VAR_066346.
FT   VARIANT     674    674       V -> A. {ECO:0000269|PubMed:21618349}.
FT                                /FTId=VAR_066347.
FT   VARIANT     720    720       H -> P (severe impairment of activity;
FT                                dbSNP:rs113706342).
FT                                {ECO:0000269|PubMed:21618349}.
FT                                /FTId=VAR_066348.
FT   VARIANT     733    733       P -> L (in dbSNP:rs5743621).
FT                                {ECO:0000269|PubMed:21618349}.
FT                                /FTId=VAR_052359.
FT   CONFLICT    182    182       E -> G (in Ref. 5; CAB43364).
FT                                {ECO:0000305}.
FT   CONFLICT    228    228       N -> S (in Ref. 5; CAB43364).
FT                                {ECO:0000305}.
FT   CONFLICT    276    276       F -> S (in Ref. 5; CAB43364).
FT                                {ECO:0000305}.
FT   STRAND       28     30       {ECO:0000244|PDB:2Z7X}.
FT   STRAND       48     51       {ECO:0000244|PDB:2Z7X}.
FT   HELIX        62     65       {ECO:0000244|PDB:2Z7X}.
FT   STRAND       73     75       {ECO:0000244|PDB:2Z7X}.
FT   STRAND       83     85       {ECO:0000244|PDB:2Z7X}.
FT   HELIX        86     89       {ECO:0000244|PDB:2Z7X}.
FT   STRAND       97     99       {ECO:0000244|PDB:2Z7X}.
FT   STRAND      107    109       {ECO:0000244|PDB:2Z7X}.
FT   STRAND      117    120       {ECO:0000244|PDB:2Z7X}.
FT   HELIX       133    137       {ECO:0000244|PDB:2Z7X}.
FT   STRAND      143    150       {ECO:0000244|PDB:2Z7X}.
FT   HELIX       153    159       {ECO:0000244|PDB:2Z7X}.
FT   STRAND      164    171       {ECO:0000244|PDB:2Z7X}.
FT   HELIX       181    184       {ECO:0000244|PDB:2Z7X}.
FT   STRAND      189    195       {ECO:0000244|PDB:2Z7X}.
FT   STRAND      198    200       {ECO:0000244|PDB:2Z7X}.
FT   STRAND      214    218       {ECO:0000244|PDB:2Z7X}.
FT   STRAND      221    223       {ECO:0000244|PDB:2Z7X}.
FT   TURN        227    230       {ECO:0000244|PDB:2Z7X}.
FT   HELIX       231    238       {ECO:0000244|PDB:2Z7X}.
FT   HELIX       239    242       {ECO:0000244|PDB:2Z7X}.
FT   STRAND      248    257       {ECO:0000244|PDB:2Z7X}.
FT   HELIX       258    269       {ECO:0000244|PDB:2Z7X}.
FT   STRAND      274    285       {ECO:0000244|PDB:2Z7X}.
FT   STRAND      301    309       {ECO:0000244|PDB:2Z7X}.
FT   HELIX       317    324       {ECO:0000244|PDB:2Z7X}.
FT   STRAND      329    336       {ECO:0000244|PDB:2Z7X}.
FT   STRAND      352    354       {ECO:0000244|PDB:2Z7X}.
FT   TURN        362    367       {ECO:0000244|PDB:2Z7X}.
FT   STRAND      376    378       {ECO:0000244|PDB:2Z7X}.
FT   HELIX       387    394       {ECO:0000244|PDB:2Z7X}.
FT   STRAND      402    404       {ECO:0000244|PDB:2Z7X}.
FT   HELIX       414    416       {ECO:0000244|PDB:2Z7X}.
FT   STRAND      427    429       {ECO:0000244|PDB:2Z7X}.
FT   HELIX       437    441       {ECO:0000244|PDB:2Z7X}.
FT   STRAND      449    451       {ECO:0000244|PDB:2Z7X}.
FT   HELIX       462    466       {ECO:0000244|PDB:2Z7X}.
FT   STRAND      472    474       {ECO:0000244|PDB:2Z7X}.
FT   STRAND      631    633       {ECO:0000244|PDB:1FYV}.
FT   STRAND      637    642       {ECO:0000244|PDB:1FYV}.
FT   HELIX       645    647       {ECO:0000244|PDB:1FYV}.
FT   HELIX       648    653       {ECO:0000244|PDB:1FYV}.
FT   HELIX       655    660       {ECO:0000244|PDB:1FYV}.
FT   TURN        661    663       {ECO:0000244|PDB:1FYV}.
FT   TURN        669    672       {ECO:0000244|PDB:1FYV}.
FT   HELIX       679    689       {ECO:0000244|PDB:1FYV}.
FT   STRAND      690    698       {ECO:0000244|PDB:1FYV}.
FT   HELIX       699    704       {ECO:0000244|PDB:1FYV}.
FT   HELIX       707    712       {ECO:0000244|PDB:1FYV}.
FT   STRAND      724    732       {ECO:0000244|PDB:1FYV}.
FT   HELIX       736    738       {ECO:0000244|PDB:1FYV}.
FT   HELIX       744    751       {ECO:0000244|PDB:1FYV}.
FT   HELIX       762    764       {ECO:0000244|PDB:1FYV}.
FT   HELIX       767    777       {ECO:0000244|PDB:1FYV}.
SQ   SEQUENCE   786 AA;  90291 MW;  1BFCCC5E42EA5242 CRC64;
     MTSIFHFAII FMLILQIRIQ LSEESEFLVD RSKNGLIHVP KDLSQKTTIL NISQNYISEL
     WTSDILSLSK LRILIISHNR IQYLDISVFK FNQELEYLDL SHNKLVKISC HPTVNLKHLD
     LSFNAFDALP ICKEFGNMSQ LKFLGLSTTH LEKSSVLPIA HLNISKVLLV LGETYGEKED
     PEGLQDFNTE SLHIVFPTNK EFHFILDVSV KTVANLELSN IKCVLEDNKC SYFLSILAKL
     QTNPKLSNLT LNNIETTWNS FIRILQLVWH TTVWYFSISN VKLQGQLDFR DFDYSGTSLK
     ALSIHQVVSD VFGFPQSYIY EIFSNMNIKN FTVSGTRMVH MLCPSKISPF LHLDFSNNLL
     TDTVFENCGH LTELETLILQ MNQLKELSKI AEMTTQMKSL QQLDISQNSV SYDEKKGDCS
     WTKSLLSLNM SSNILTDTIF RCLPPRIKVL DLHSNKIKSI PKQVVKLEAL QELNVAFNSL
     TDLPGCGSFS SLSVLIIDHN SVSHPSADFF QSCQKMRSIK AGDNPFQCTC ELGEFVKNID
     QVSSEVLEGW PDSYKCDYPE SYRGTLLKDF HMSELSCNIT LLIVTIVATM LVLAVTVTSL
     CSYLDLPWYL RMVCQWTQTR RRARNIPLEE LQRNLQFHAF ISYSGHDSFW VKNELLPNLE
     KEGMQICLHE RNFVPGKSIV ENIITCIEKS YKSIFVLSPN FVQSEWCHYE LYFAHHNLFH
     EGSNSLILIL LEPIPQYSIP SSYHKLKSLM ARRTYLEWPK EKSKRGLFWA NLRAAINIKL
     TEQAKK
//
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