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Toll-like receptor 1 (Toll/interleukin-1 receptor-like protein) (TIL) (CD antigen CD281)

 TLR1_HUMAN              Reviewed;         786 AA.
Q15399; D1CS39; D1CS41; O15452; Q32MK3; Q32MK4; Q9UG90;
31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
01-MAY-2007, sequence version 3.
18-JUL-2018, entry version 186.
RecName: Full=Toll-like receptor 1;
AltName: Full=Toll/interleukin-1 receptor-like protein;
Short=TIL;
AltName: CD_antigen=CD281;
Flags: Precursor;
Name=TLR1; Synonyms=KIAA0012;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS SER-248 AND ILE-602.
TISSUE=Erythroleukemia;
PubMed=9435236; DOI=10.1073/pnas.95.2.588;
Rock F.L., Hardiman G., Timans J.C., Kastelein R.A., Bazan J.F.;
"A family of human receptors structurally related to Drosophila
Toll.";
Proc. Natl. Acad. Sci. U.S.A. 95:588-593(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=18810425; DOI=10.1007/s00251-008-0332-0;
Nakajima T., Ohtani H., Satta Y., Uno Y., Akari H., Ishida T.,
Kimura A.;
"Natural selection in the TLR-related genes in the course of primate
evolution.";
Immunogenetics 60:727-735(2008).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS THR-80 AND ILE-602.
PubMed=19924287; DOI=10.1371/journal.pone.0007803;
Georgel P., Macquin C., Bahram S.;
"The heterogeneous allelic repertoire of human Toll-Like receptor
(TLR) genes.";
PLoS ONE 4:E7803-E7803(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-80.
TISSUE=Bone marrow;
PubMed=7584026; DOI=10.1093/dnares/1.1.27;
Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y.,
Sato S., Nagase T., Seki N., Ishikawa K., Tabata S.;
"Prediction of the coding sequences of unidentified human genes. I.
The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by
analysis of randomly sampled cDNA clones from human immature myeloid
cell line KG-1.";
DNA Res. 1:27-35(1994).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS SER-248 AND
ILE-602.
TISSUE=Brain;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS SER-248 AND
ILE-602.
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 25-39.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally
verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[8]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TLR2 AND CD14.
PubMed=16880211; DOI=10.1074/jbc.M602794200;
Triantafilou M., Gamper F.G., Haston R.M., Mouratis M.A., Morath S.,
Hartung T., Triantafilou K.;
"Membrane sorting of toll-like receptor (TLR)-2/6 and TLR2/1
heterodimers at the cell surface determines heterotypic associations
with CD36 and intracellular targeting.";
J. Biol. Chem. 281:31002-31011(2006).
[9]
INVOLVEMENT IN PROTECTION AGAINST LEPROSY.
PubMed=17548585; DOI=10.4049/jimmunol.178.12.7520;
Johnson C.M., Lyle E.A., Omueti K.O., Stepensky V.A., Yegin O.,
Alpsoy E., Hamann L., Schumann R.R., Tapping R.I.;
"Cutting edge: A common polymorphism impairs cell surface trafficking
and functional responses of TLR1 but protects against leprosy.";
J. Immunol. 178:7520-7524(2007).
[10]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-163.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[11]
FUNCTION.
TISSUE=T-cell;
PubMed=21078852; DOI=10.1128/IAI.00806-10;
Lancioni C.L., Li Q., Thomas J.J., Ding X., Thiel B., Drage M.G.,
Pecora N.D., Ziady A.G., Shank S., Harding C.V., Boom W.H.,
Rojas R.E.;
"Mycobacterium tuberculosis lipoproteins directly regulate human
memory CD4(+) T cell activation via Toll-like receptors 1 and 2.";
Infect. Immun. 79:663-673(2011).
[12]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 625-785.
PubMed=11081518; DOI=10.1038/35040600;
Xu Y., Tao X., Shen B., Horng T., Medzhitov R., Manley J.L., Tong L.;
"Structural basis for signal transduction by the Toll/interleukin-1
receptor domains.";
Nature 408:111-115(2000).
[13]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 25-476 IN COMPLEX WITH TLR2
AND BACTERIAL LIPOPEPTIDE ANALOG, DISULFIDE BONDS, AND GLYCOSYLATION
AT ASN-51; ASN-163; ASN-330 AND ASN-429.
PubMed=17889651; DOI=10.1016/j.cell.2007.09.008;
Jin M.S., Kim S.E., Heo J.Y., Lee M.E., Kim H.M., Paik S.-G., Lee H.,
Lee J.-O.;
"Crystal structure of the TLR1-TLR2 heterodimer induced by binding of
a tri-acylated lipopeptide.";
Cell 130:1071-1082(2007).
[14]
ASSOCIATION OF VARIANT SER-248 WITH SUSCEPTIBILITY TO LEPROSY.
PubMed=19456232; DOI=10.1086/599121;
Schuring R.P., Hamann L., Faber W.R., Pahan D., Richardus J.H.,
Schumann R.R., Oskam L.;
"Polymorphism N248S in the human Toll-like receptor 1 gene is related
to leprosy and leprosy reactions.";
J. Infect. Dis. 199:1816-1819(2009).
[15]
VARIANTS PRO-44; THR-75; THR-80; TYR-118; SER-248; LEU-305; LEU-315;
ASN-352; VAL-460; ALA-542; CYS-554; GLY-587; ILE-602; ALA-651;
ALA-674; PRO-720 AND LEU-733, AND CHARACTERIZATION OF VARIANTS
LEU-315; CYS-554; ILE-602; ALA-651 AND PRO-720.
PubMed=21618349; DOI=10.1002/humu.21486;
Ben-Ali M., Corre B., Manry J., Barreiro L.B., Quach H., Boniotto M.,
Pellegrini S., Quintana-Murci L.;
"Functional characterization of naturally occurring genetic variants
in the human TLR1-2-6 gene family.";
Hum. Mutat. 32:643-652(2011).
-!- FUNCTION: Participates in the innate immune response to microbial
agents. Specifically recognizes diacylated and triacylated
lipopeptides. Cooperates with TLR2 to mediate the innate immune
response to bacterial lipoproteins or lipopeptides
(PubMed:21078852). Forms the activation cluster TLR2:TLR1:CD14 in
response to triacylated lipopeptides, this cluster triggers
signaling from the cell surface and subsequently is targeted to
the Golgi in a lipid-raft dependent pathway (PubMed:16880211).
Acts via MYD88 and TRAF6, leading to NF-kappa-B activation,
cytokine secretion and the inflammatory response.
{ECO:0000269|PubMed:16880211, ECO:0000269|PubMed:21078852}.
-!- SUBUNIT: Interacts (via extracellular domain) with TLR2. TLR2
seems to exist in heterodimers with either TLR1 or TLR6 before
stimulation by the ligand. The heterodimers form bigger oligomers
in response to their corresponding ligands as well as further
heterotypic associations with other receptors such as CD14 and/or
CD36 (PubMed:16880211, PubMed:17889651). The activation cluster
TLR2:TLR1:CD14 forms in response to triacylated lipopeptides
(PubMed:16880211). Binds MYD88 (via TIR domain). Interacts with
CNPY3 (By similarity). {ECO:0000250|UniProtKB:Q9EPQ1,
ECO:0000269|PubMed:16880211, ECO:0000269|PubMed:17889651}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-9009517, EBI-9009517;
O60603:TLR2; NbExp=3; IntAct=EBI-9009517, EBI-973722;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16880211};
Single-pass type I membrane protein {ECO:0000255}. Cytoplasmic
vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q9EPQ1};
Single-pass type I membrane protein {ECO:0000255}. Membrane raft
{ECO:0000269|PubMed:16880211}. Golgi apparatus
{ECO:0000269|PubMed:16880211}. Note=Does not reside in lipid rafts
before stimulation but accumulates increasingly in the raft upon
the presence of the microbial ligand. In response to triacylated
lipoproteins, TLR2:TLR1 heterodimers are recruited in lipid rafts,
this recruitment determine the intracellular targeting to the
Golgi apparatus. {ECO:0000269|PubMed:16880211}.
-!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in spleen, ovary,
peripheral blood leukocytes, thymus and small intestine.
-!- POLYMORPHISM: Genetic variations in TLR1 may influence
susceptibility to or protection against contracting leprosy and
define the leprosy susceptibility locus 5 [MIM:613223]. Ser-602 is
a common allele in Caucasians. It is associated with impaired cell
surface expression and receptor function resulting in protection
against leprosy.
-!- SIMILARITY: Belongs to the Toll-like receptor family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA02801.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; U88540; AAC34137.1; -; mRNA.
EMBL; AB445617; BAG55014.1; -; mRNA.
EMBL; DQ012259; AAY85638.1; -; mRNA.
EMBL; DQ012260; AAY85639.1; -; mRNA.
EMBL; DQ012261; AAY85640.1; -; mRNA.
EMBL; D13637; BAA02801.2; ALT_INIT; mRNA.
EMBL; AL050262; CAB43364.1; -; mRNA.
EMBL; BC109093; AAI09094.1; -; mRNA.
EMBL; BC109094; AAI09095.1; -; mRNA.
CCDS; CCDS33973.1; -.
PIR; T08664; T08664.
RefSeq; NP_003254.2; NM_003263.3.
RefSeq; XP_005262719.1; XM_005262662.4.
RefSeq; XP_011512044.1; XM_011513742.2.
RefSeq; XP_011512045.1; XM_011513743.2.
RefSeq; XP_011512046.1; XM_011513744.2.
RefSeq; XP_011512047.1; XM_011513745.2.
RefSeq; XP_016864060.1; XM_017008571.1.
RefSeq; XP_016864061.1; XM_017008572.1.
UniGene; Hs.621817; -.
UniGene; Hs.654532; -.
PDB; 1FYV; X-ray; 2.90 A; A=625-785.
PDB; 2Z7X; X-ray; 2.10 A; B=25-475.
PDBsum; 1FYV; -.
PDBsum; 2Z7X; -.
ProteinModelPortal; Q15399; -.
SMR; Q15399; -.
BioGrid; 112951; 13.
IntAct; Q15399; 6.
STRING; 9606.ENSP00000354932; -.
ChEMBL; CHEMBL3885643; -.
iPTMnet; Q15399; -.
PhosphoSitePlus; Q15399; -.
BioMuta; TLR1; -.
DMDM; 146291086; -.
EPD; Q15399; -.
PaxDb; Q15399; -.
PeptideAtlas; Q15399; -.
PRIDE; Q15399; -.
ProteomicsDB; 60569; -.
Ensembl; ENST00000308979; ENSP00000354932; ENSG00000174125.
Ensembl; ENST00000502213; ENSP00000421259; ENSG00000174125.
GeneID; 7096; -.
KEGG; hsa:7096; -.
UCSC; uc003gtl.4; human.
CTD; 7096; -.
DisGeNET; 7096; -.
EuPathDB; HostDB:ENSG00000174125.7; -.
GeneCards; TLR1; -.
HGNC; HGNC:11847; TLR1.
MalaCards; TLR1; -.
MIM; 601194; gene.
MIM; 613223; phenotype.
neXtProt; NX_Q15399; -.
OpenTargets; ENSG00000174125; -.
PharmGKB; PA36549; -.
eggNOG; KOG4641; Eukaryota.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00760000119006; -.
HOGENOM; HOG000008676; -.
HOVERGEN; HBG023180; -.
InParanoid; Q15399; -.
KO; K05398; -.
OMA; NNIETTW; -.
OrthoDB; EOG091G0356; -.
PhylomeDB; Q15399; -.
TreeFam; TF351113; -.
Reactome; R-HSA-1236974; ER-Phagosome pathway.
Reactome; R-HSA-1461957; Beta defensins.
Reactome; R-HSA-166058; MyD88:Mal cascade initiated on plasma membrane.
Reactome; R-HSA-168179; Toll Like Receptor TLR1:TLR2 Cascade.
Reactome; R-HSA-5602498; MyD88 deficiency (TLR2/4).
Reactome; R-HSA-5603041; IRAK4 deficiency (TLR2/4).
Reactome; R-HSA-5686938; Regulation of TLR by endogenous ligand.
EvolutionaryTrace; Q15399; -.
GeneWiki; TLR_1; -.
GenomeRNAi; 7096; -.
PRO; PR:Q15399; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000174125; -.
CleanEx; HS_TLR1; -.
ExpressionAtlas; Q15399; baseline and differential.
Genevisible; Q15399; HS.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0016020; C:membrane; NAS:UniProtKB.
GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0035354; C:Toll-like receptor 1-Toll-like receptor 2 protein complex; IDA:MGI.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0071723; F:lipopeptide binding; IBA:GO_Central.
GO; GO:0046982; F:protein heterodimerization activity; IDA:MGI.
GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
GO; GO:0035663; F:Toll-like receptor 2 binding; IPI:UniProtKB.
GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
GO; GO:0001775; P:cell activation; IDA:AgBase.
GO; GO:0071727; P:cellular response to triacyl bacterial lipopeptide; IDA:UniProtKB.
GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
GO; GO:0042495; P:detection of triacyl bacterial lipopeptide; IDA:MGI.
GO; GO:0006955; P:immune response; TAS:ProtInc.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0042116; P:macrophage activation; NAS:UniProtKB.
GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; TAS:Reactome.
GO; GO:0045410; P:positive regulation of interleukin-6 biosynthetic process; ISS:UniProtKB.
GO; GO:2000484; P:positive regulation of interleukin-8 secretion; IGI:ARUK-UCL.
GO; GO:0034137; P:positive regulation of toll-like receptor 2 signaling pathway; IGI:ARUK-UCL.
GO; GO:0042535; P:positive regulation of tumor necrosis factor biosynthetic process; ISS:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0034130; P:toll-like receptor 1 signaling pathway; IEA:InterPro.
GO; GO:0002224; P:toll-like receptor signaling pathway; IBA:GO_Central.
GO; GO:0038123; P:toll-like receptor TLR1:TLR2 signaling pathway; TAS:Reactome.
Gene3D; 3.40.50.10140; -; 1.
Gene3D; 3.80.10.10; -; 1.
InterPro; IPR000483; Cys-rich_flank_reg_C.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR000157; TIR_dom.
InterPro; IPR027190; TLR1.
InterPro; IPR035897; Toll_tir_struct_dom_sf.
PANTHER; PTHR24365:SF261; PTHR24365:SF261; 1.
Pfam; PF13855; LRR_8; 2.
Pfam; PF01463; LRRCT; 1.
Pfam; PF01582; TIR; 1.
SMART; SM00369; LRR_TYP; 4.
SMART; SM00082; LRRCT; 1.
SMART; SM00255; TIR; 1.
SUPFAM; SSF52200; SSF52200; 1.
PROSITE; PS51450; LRR; 10.
PROSITE; PS50104; TIR; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome; Cytoplasmic vesicle;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Golgi apparatus; Immunity; Inflammatory response; Innate immunity;
Leucine-rich repeat; Membrane; Polymorphism; Receptor;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 24 {ECO:0000269|PubMed:15340161}.
CHAIN 25 786 Toll-like receptor 1.
/FTId=PRO_0000034705.
TOPO_DOM 25 580 Extracellular. {ECO:0000255}.
TRANSMEM 581 601 Helical. {ECO:0000255}.
TOPO_DOM 602 786 Cytoplasmic. {ECO:0000255}.
REPEAT 54 77 LRR 1.
REPEAT 78 101 LRR 2.
REPEAT 102 125 LRR 3.
REPEAT 126 150 LRR 4.
REPEAT 151 175 LRR 5.
REPEAT 176 199 LRR 6.
REPEAT 200 223 LRR 7.
REPEAT 224 250 LRR 8.
REPEAT 251 278 LRR 9.
REPEAT 279 308 LRR 10.
REPEAT 309 337 LRR 11.
REPEAT 338 361 LRR 12.
REPEAT 362 388 LRR 13.
REPEAT 389 414 LRR 14.
REPEAT 415 437 LRR 15.
REPEAT 438 457 LRR 16.
REPEAT 458 478 LRR 17.
REPEAT 479 500 LRR 18.
REPEAT 501 524 LRR 19.
DOMAIN 525 579 LRRCT.
DOMAIN 635 779 TIR. {ECO:0000255|PROSITE-
ProRule:PRU00204}.
REGION 313 316 Interaction with bacterial lipopeptide.
CARBOHYD 51 51 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17889651}.
CARBOHYD 137 137 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 163 163 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17889651,
ECO:0000269|PubMed:19159218}.
CARBOHYD 330 330 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17889651}.
CARBOHYD 429 429 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17889651}.
CARBOHYD 578 578 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 110 132 {ECO:0000269|PubMed:17889651}.
DISULFID 223 230 {ECO:0000269|PubMed:17889651}.
DISULFID 343 368 {ECO:0000269|PubMed:17889651}.
DISULFID 419 442 {ECO:0000269|PubMed:17889651}.
VARIANT 44 44 S -> P (in dbSNP:rs76600635).
{ECO:0000269|PubMed:21618349}.
/FTId=VAR_066340.
VARIANT 75 75 I -> T (in dbSNP:rs137853170).
{ECO:0000269|PubMed:21618349}.
/FTId=VAR_066341.
VARIANT 80 80 R -> T (in dbSNP:rs5743611).
{ECO:0000269|PubMed:19924287,
ECO:0000269|PubMed:21618349,
ECO:0000269|PubMed:7584026}.
/FTId=VAR_031916.
VARIANT 118 118 H -> Y (in dbSNP:rs5743612).
{ECO:0000269|PubMed:21618349}.
/FTId=VAR_018474.
VARIANT 248 248 N -> S (may confer susceptibility to
leprosy; dbSNP:rs4833095).
{ECO:0000269|PubMed:11230166,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:21618349,
ECO:0000269|PubMed:9435236}.
/FTId=VAR_031917.
VARIANT 305 305 H -> L (in dbSNP:rs3923647).
{ECO:0000269|PubMed:21618349}.
/FTId=VAR_031918.
VARIANT 315 315 P -> L (severe impairment of activity;
dbSNP:rs5743613).
{ECO:0000269|PubMed:21618349}.
/FTId=VAR_031919.
VARIANT 352 352 H -> N (in dbSNP:rs76796448).
{ECO:0000269|PubMed:21618349}.
/FTId=VAR_066342.
VARIANT 460 460 I -> V (in dbSNP:rs137853171).
{ECO:0000269|PubMed:21618349}.
/FTId=VAR_066343.
VARIANT 542 542 V -> A (in dbSNP:rs137853172).
{ECO:0000269|PubMed:21618349}.
/FTId=VAR_066344.
VARIANT 554 554 Y -> C (severe impairment of activity;
dbSNP:rs137853173).
{ECO:0000269|PubMed:21618349}.
/FTId=VAR_066345.
VARIANT 587 587 V -> G (in dbSNP:rs5743617).
{ECO:0000269|PubMed:21618349}.
/FTId=VAR_031920.
VARIANT 602 602 S -> I (severe impairment of activity;
dbSNP:rs5743618).
{ECO:0000269|PubMed:11230166,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:19924287,
ECO:0000269|PubMed:21618349,
ECO:0000269|PubMed:9435236}.
/FTId=VAR_031921.
VARIANT 631 631 L -> R (in dbSNP:rs5743619).
/FTId=VAR_052358.
VARIANT 651 651 V -> A (severe impairment of activity;
dbSNP:rs137853174).
{ECO:0000269|PubMed:21618349}.
/FTId=VAR_066346.
VARIANT 674 674 V -> A. {ECO:0000269|PubMed:21618349}.
/FTId=VAR_066347.
VARIANT 720 720 H -> P (severe impairment of activity;
dbSNP:rs113706342).
{ECO:0000269|PubMed:21618349}.
/FTId=VAR_066348.
VARIANT 733 733 P -> L (in dbSNP:rs5743621).
{ECO:0000269|PubMed:21618349}.
/FTId=VAR_052359.
CONFLICT 182 182 E -> G (in Ref. 5; CAB43364).
{ECO:0000305}.
CONFLICT 228 228 N -> S (in Ref. 5; CAB43364).
{ECO:0000305}.
CONFLICT 276 276 F -> S (in Ref. 5; CAB43364).
{ECO:0000305}.
STRAND 28 30 {ECO:0000244|PDB:2Z7X}.
STRAND 48 51 {ECO:0000244|PDB:2Z7X}.
HELIX 62 65 {ECO:0000244|PDB:2Z7X}.
STRAND 73 75 {ECO:0000244|PDB:2Z7X}.
STRAND 83 85 {ECO:0000244|PDB:2Z7X}.
HELIX 86 89 {ECO:0000244|PDB:2Z7X}.
STRAND 97 99 {ECO:0000244|PDB:2Z7X}.
STRAND 107 109 {ECO:0000244|PDB:2Z7X}.
STRAND 117 120 {ECO:0000244|PDB:2Z7X}.
HELIX 133 137 {ECO:0000244|PDB:2Z7X}.
STRAND 143 150 {ECO:0000244|PDB:2Z7X}.
HELIX 153 159 {ECO:0000244|PDB:2Z7X}.
STRAND 164 171 {ECO:0000244|PDB:2Z7X}.
HELIX 181 184 {ECO:0000244|PDB:2Z7X}.
STRAND 189 195 {ECO:0000244|PDB:2Z7X}.
STRAND 198 200 {ECO:0000244|PDB:2Z7X}.
STRAND 214 218 {ECO:0000244|PDB:2Z7X}.
STRAND 221 223 {ECO:0000244|PDB:2Z7X}.
TURN 227 230 {ECO:0000244|PDB:2Z7X}.
HELIX 231 238 {ECO:0000244|PDB:2Z7X}.
HELIX 239 242 {ECO:0000244|PDB:2Z7X}.
STRAND 248 257 {ECO:0000244|PDB:2Z7X}.
HELIX 258 269 {ECO:0000244|PDB:2Z7X}.
STRAND 274 285 {ECO:0000244|PDB:2Z7X}.
STRAND 301 309 {ECO:0000244|PDB:2Z7X}.
HELIX 317 324 {ECO:0000244|PDB:2Z7X}.
STRAND 329 336 {ECO:0000244|PDB:2Z7X}.
STRAND 352 354 {ECO:0000244|PDB:2Z7X}.
TURN 362 367 {ECO:0000244|PDB:2Z7X}.
STRAND 376 378 {ECO:0000244|PDB:2Z7X}.
HELIX 387 394 {ECO:0000244|PDB:2Z7X}.
STRAND 402 404 {ECO:0000244|PDB:2Z7X}.
HELIX 414 416 {ECO:0000244|PDB:2Z7X}.
STRAND 427 429 {ECO:0000244|PDB:2Z7X}.
HELIX 437 441 {ECO:0000244|PDB:2Z7X}.
STRAND 449 451 {ECO:0000244|PDB:2Z7X}.
HELIX 462 466 {ECO:0000244|PDB:2Z7X}.
STRAND 472 474 {ECO:0000244|PDB:2Z7X}.
TURN 487 491 {ECO:0000244|PDB:2Z7X}.
HELIX 504 516 {ECO:0000244|PDB:2Z7X}.
TURN 517 520 {ECO:0000244|PDB:2Z7X}.
STRAND 521 523 {ECO:0000244|PDB:2Z7X}.
TURN 529 531 {ECO:0000244|PDB:2Z7X}.
HELIX 536 538 {ECO:0000244|PDB:2Z7X}.
STRAND 631 633 {ECO:0000244|PDB:1FYV}.
STRAND 637 642 {ECO:0000244|PDB:1FYV}.
HELIX 645 647 {ECO:0000244|PDB:1FYV}.
HELIX 648 653 {ECO:0000244|PDB:1FYV}.
HELIX 655 660 {ECO:0000244|PDB:1FYV}.
TURN 661 663 {ECO:0000244|PDB:1FYV}.
TURN 669 672 {ECO:0000244|PDB:1FYV}.
HELIX 679 689 {ECO:0000244|PDB:1FYV}.
STRAND 690 698 {ECO:0000244|PDB:1FYV}.
HELIX 699 704 {ECO:0000244|PDB:1FYV}.
HELIX 707 712 {ECO:0000244|PDB:1FYV}.
STRAND 724 732 {ECO:0000244|PDB:1FYV}.
HELIX 736 738 {ECO:0000244|PDB:1FYV}.
HELIX 744 751 {ECO:0000244|PDB:1FYV}.
HELIX 762 764 {ECO:0000244|PDB:1FYV}.
HELIX 767 777 {ECO:0000244|PDB:1FYV}.
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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