GenomeNet

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   16-APR-2014, entry version 148.
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;
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).
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   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein (By similarity). Cytoplasmic vesicle, phagosome membrane;
CC       Single-pass type I membrane protein (By similarity).
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   -!- SIMILARITY: Contains 19 LRR (leucine-rich) repeats.
CC   -!- SIMILARITY: Contains 1 LRRCT domain.
CC   -!- SIMILARITY: Contains 1 TIR domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA02801.2; Type=Erroneous initiation;
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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   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   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=25-476.
DR   PDBsum; 1FYV; -.
DR   PDBsum; 2Z7X; -.
DR   ProteinModelPortal; Q15399; -.
DR   SMR; Q15399; 25-567, 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   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   ArrayExpress; Q15399; -.
DR   Bgee; Q15399; -.
DR   CleanEx; HS_TLR1; -.
DR   Genevestigator; Q15399; -.
DR   GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR   GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR   GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
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:0042496; P:detection of diacyl bacterial lipopeptide; IEA:InterPro.
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:0042088; P:T-helper 1 type immune response; IEA:InterPro.
DR   GO; GO:0034150; P:toll-like receptor 6 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; IPR027187; TLR1/6.
DR   InterPro; IPR017241; Toll-like_receptor.
DR   PANTHER; PTHR24365:SF130; PTHR24365:SF130; 1.
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
FT   CHAIN        25    786       Toll-like receptor 1.
FT                                /FTId=PRO_0000034705.
FT   TOPO_DOM     25    580       Extracellular (Potential).
FT   TRANSMEM    581    601       Helical; (Potential).
FT   TOPO_DOM    602    786       Cytoplasmic (Potential).
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.
FT   REGION      313    316       Interaction with bacterial lipopeptide.
FT   CARBOHYD     51     51       N-linked (GlcNAc...).
FT   CARBOHYD    137    137       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    163    163       N-linked (GlcNAc...).
FT   CARBOHYD    330    330       N-linked (GlcNAc...).
FT   CARBOHYD    429    429       N-linked (GlcNAc...).
FT   CARBOHYD    578    578       N-linked (GlcNAc...) (Potential).
FT   DISULFID    110    132
FT   DISULFID    223    230
FT   DISULFID    343    368
FT   DISULFID    419    442
FT   VARIANT      44     44       S -> P (in dbSNP:rs76600635).
FT                                /FTId=VAR_066340.
FT   VARIANT      75     75       I -> T (in dbSNP:rs137853170).
FT                                /FTId=VAR_066341.
FT   VARIANT      80     80       R -> T (in dbSNP:rs5743611).
FT                                /FTId=VAR_031916.
FT   VARIANT     118    118       H -> Y (in dbSNP:rs5743612).
FT                                /FTId=VAR_018474.
FT   VARIANT     248    248       N -> S (may confer susceptibility to
FT                                leprosy; dbSNP:rs4833095).
FT                                /FTId=VAR_031917.
FT   VARIANT     305    305       H -> L (in dbSNP:rs3923647).
FT                                /FTId=VAR_031918.
FT   VARIANT     315    315       P -> L (severe impairment of activity;
FT                                dbSNP:rs5743613).
FT                                /FTId=VAR_031919.
FT   VARIANT     352    352       H -> N (in dbSNP:rs76796448).
FT                                /FTId=VAR_066342.
FT   VARIANT     460    460       I -> V (in dbSNP:rs137853171).
FT                                /FTId=VAR_066343.
FT   VARIANT     542    542       V -> A (in dbSNP:rs137853172).
FT                                /FTId=VAR_066344.
FT   VARIANT     554    554       Y -> C (severe impairment of activity).
FT                                /FTId=VAR_066345.
FT   VARIANT     587    587       V -> G (in dbSNP:rs5743617).
FT                                /FTId=VAR_031920.
FT   VARIANT     602    602       S -> I (severe impairment of activity;
FT                                dbSNP:rs5743618).
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                                /FTId=VAR_066346.
FT   VARIANT     674    674       V -> A.
FT                                /FTId=VAR_066347.
FT   VARIANT     720    720       H -> P (severe impairment of activity;
FT                                dbSNP:rs113706342).
FT                                /FTId=VAR_066348.
FT   VARIANT     733    733       P -> L (in dbSNP:rs5743621).
FT                                /FTId=VAR_052359.
FT   CONFLICT    182    182       E -> G (in Ref. 5; CAB43364).
FT   CONFLICT    228    228       N -> S (in Ref. 5; CAB43364).
FT   CONFLICT    276    276       F -> S (in Ref. 5; CAB43364).
FT   STRAND       28     30
FT   STRAND       48     51
FT   HELIX        62     65
FT   STRAND       73     75
FT   STRAND       83     85
FT   HELIX        86     89
FT   STRAND       97     99
FT   STRAND      107    109
FT   STRAND      117    120
FT   HELIX       133    137
FT   STRAND      143    150
FT   HELIX       153    159
FT   STRAND      164    171
FT   HELIX       181    184
FT   STRAND      189    195
FT   STRAND      198    200
FT   STRAND      214    218
FT   STRAND      221    223
FT   TURN        227    230
FT   HELIX       231    238
FT   HELIX       239    242
FT   STRAND      248    257
FT   HELIX       258    269
FT   STRAND      274    285
FT   STRAND      301    309
FT   HELIX       317    324
FT   STRAND      329    336
FT   STRAND      352    354
FT   TURN        362    367
FT   STRAND      376    378
FT   HELIX       387    394
FT   STRAND      402    404
FT   HELIX       414    416
FT   STRAND      427    429
FT   HELIX       437    441
FT   STRAND      449    451
FT   HELIX       462    466
FT   STRAND      472    474
FT   STRAND      631    633
FT   STRAND      637    642
FT   HELIX       645    647
FT   HELIX       648    653
FT   HELIX       655    660
FT   TURN        661    663
FT   TURN        669    672
FT   HELIX       679    689
FT   STRAND      690    698
FT   HELIX       699    704
FT   HELIX       707    712
FT   STRAND      724    732
FT   HELIX       736    738
FT   HELIX       744    751
FT   HELIX       762    764
FT   HELIX       767    777
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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