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Leukocyte immunoglobulin-like receptor subfamily B member 2 (LIR-2) (Leukocyte immunoglobulin-like receptor 2) (CD85 antigen-like family member D) (Immunoglobulin-like transcript 4) (ILT-4) (Monocyte/macrophage immunoglobulin-like receptor 10) (MIR-10) (CD antigen CD85d)

 LIRB2_HUMAN             Reviewed;         598 AA.
Q8N423; A8MU67; C9JF29; O75017; Q8NHJ7; Q8NHJ8;
03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
02-NOV-2010, sequence version 4.
07-NOV-2018, entry version 158.
RecName: Full=Leukocyte immunoglobulin-like receptor subfamily B member 2;
Short=LIR-2;
Short=Leukocyte immunoglobulin-like receptor 2;
AltName: Full=CD85 antigen-like family member D;
AltName: Full=Immunoglobulin-like transcript 4;
Short=ILT-4;
AltName: Full=Monocyte/macrophage immunoglobulin-like receptor 10;
Short=MIR-10;
AltName: CD_antigen=CD85d;
Flags: Precursor;
Name=LILRB2; Synonyms=ILT4, LIR2, MIR10;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND VARIANTS ASP-161; TYR-300;
TRP-306 AND HIS-322.
PubMed=9382880; DOI=10.1084/jem.186.11.1809;
Colonna M., Navarro F., Bellon T., Llano M., Garcia P., Samaridis J.,
Angman L., Cella M., Lopez-Botet M.;
"A common inhibitory receptor for major histocompatibility complex
class I molecules on human lymphoid and myelomonocytic cells.";
J. Exp. Med. 186:1809-1818(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, FUNCTION,
AND VARIANTS ASP-161; TYR-300; TRP-306 AND HIS-322.
TISSUE=Dendritic cell, and Peripheral blood monocyte;
PubMed=9548455;
Borges L., Hsu M.-L., Fanger N., Kubin M., Cosman D.;
"A family of human lymphoid and myeloid Ig-like receptors, some of
which bind to MHC class I molecules.";
J. Immunol. 159:5192-5196(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANTS ASP-161;
TYR-300; TRP-306 AND HIS-322.
Canavez F.C.;
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
ASP-161; TYR-300; TRP-306 AND HIS-322.
TISSUE=Peripheral blood leukocyte;
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).
[6]
INTERACTION WITH PTPN6 AND FCGR1A, PHOSPHORYLATION, TISSUE
SPECIFICITY, AND FUNCTION.
PubMed=9842885;
DOI=10.1002/(SICI)1521-4141(199811)28:11<3423::AID-IMMU3423>3.0.CO;2-2;
Fanger N.A., Cosman D., Peterson L., Braddy S.C., Maliszewski C.R.,
Borges L.;
"The MHC class I binding proteins LIR-1 and LIR-2 inhibit Fc receptor-
mediated signaling in monocytes.";
Eur. J. Immunol. 28:3423-3434(1998).
[7]
FUNCTION.
PubMed=11875462; DOI=10.1038/ni760;
Chang C.C., Ciubotariu R., Manavalan J.S., Yuan J., Colovai A.I.,
Piazza F., Lederman S., Colonna M., Cortesini R., Dalla-Favera R.,
Suciu-Foca N.;
"Tolerization of dendritic cells by T(S) cells: the crucial role of
inhibitory receptors ILT3 and ILT4.";
Nat. Immunol. 3:237-243(2002).
[8]
INTERACTION WITH TYPE I MHC ALLELES, AND FUNCTION.
PubMed=12853576; DOI=10.1073/pnas.1431057100;
Shiroishi M., Tsumoto K., Amano K., Shirakihara Y., Colonna M.,
Braud V.M., Allan D.S.J., Makadzange A., Rowland-Jones S.,
Willcox B.E., Jones E.Y., van der Merwe P.A., Kumagai I., Maenaka K.;
"Human inhibitory receptors Ig-like transcript 2 (ILT2) and ILT4
compete with CD8 for MHC class I binding and bind preferentially to
HLA-G.";
Proc. Natl. Acad. Sci. U.S.A. 100:8856-8861(2003).
[9]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 24-219, AND DISULFIDE BONDS.
PubMed=12390682; DOI=10.1186/1472-6807-2-6;
Willcox B.E., Thomas L.M., Chapman T.L., Heikema A.P., West A.P. Jr.,
Bjorkman P.J.;
"Crystal structure of LIR-2 (ILT4) at 1.8 A: differences from LIR-1
(ILT2) in regions implicated in the binding of the human
cytomegalovirus class I MHC homolog UL18.";
BMC Struct. Biol. 2:6-6(2002).
-!- FUNCTION: Receptor for class I MHC antigens. Recognizes a broad
spectrum of HLA-A, HLA-B, HLA-C and HLA-G alleles. Involved in the
down-regulation of the immune response and the development of
tolerance. Competes with CD8A for binding to class I MHC antigens.
Inhibits FCGR1A-mediated phosphorylation of cellular proteins and
mobilization of intracellular calcium ions.
{ECO:0000269|PubMed:11875462, ECO:0000269|PubMed:12853576,
ECO:0000269|PubMed:9548455, ECO:0000269|PubMed:9842885}.
-!- SUBUNIT: Binds PTPN6 when phosphorylated. Binds FCGR1A.
-!- INTERACTION:
Q9UKU9:ANGPTL2; NbExp=5; IntAct=EBI-2816428, EBI-15485893;
Q86XS5:ANGPTL5; NbExp=5; IntAct=EBI-2816428, EBI-15485927;
P05067:APP; NbExp=7; IntAct=EBI-2816428, EBI-821758;
P03989:HLA-B; NbExp=2; IntAct=EBI-2816428, EBI-8532782;
P18465:HLA-B; NbExp=2; IntAct=EBI-2816428, EBI-6163561;
P17693:HLA-G; NbExp=7; IntAct=EBI-2816428, EBI-1043063;
P17693-2:HLA-G; NbExp=4; IntAct=EBI-2816428, EBI-16586375;
P17693-5:HLA-G; NbExp=2; IntAct=EBI-2816428, EBI-16586455;
P17693-6:HLA-G; NbExp=3; IntAct=EBI-2816428, EBI-16586550;
P46531:NOTCH1; NbExp=8; IntAct=EBI-2816428, EBI-636374;
P29350:PTPN6; NbExp=3; IntAct=EBI-2816428, EBI-78260;
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q8N423-1; Sequence=Displayed;
Name=2;
IsoId=Q8N423-2; Sequence=VSP_008458;
Note=Alternative use of an acceptor site. No experimental
confirmation available.;
Name=3;
IsoId=Q8N423-3; Sequence=VSP_055719, VSP_055720;
Name=4;
IsoId=Q8N423-4; Sequence=VSP_055718;
Note=Gene prediction based on cDNA data.;
-!- TISSUE SPECIFICITY: Expressed on monocytes and B-cells, and at
lower levels on dendritic cells. Detected at low levels in natural
killer (NK) cells. {ECO:0000269|PubMed:9548455,
ECO:0000269|PubMed:9842885}.
-!- DOMAIN: Contains 3 copies of a cytoplasmic motif that is referred
to as the immunoreceptor tyrosine-based inhibitor motif (ITIM).
This motif is involved in modulation of cellular responses. The
phosphorylated ITIM motif can bind the SH2 domain of several SH2-
containing phosphatases.
-!- PTM: Phosphorylated on tyrosine residues. Dephosphorylated by
PTPN6. {ECO:0000269|PubMed:9842885}.
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EMBL; AF025528; AAB87662.1; -; mRNA.
EMBL; AF283986; AAL36990.1; -; mRNA.
EMBL; AF283987; AAL36991.1; -; mRNA.
EMBL; AC010518; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC036827; AAH36827.1; -; mRNA.
CCDS; CCDS12886.1; -. [Q8N423-1]
CCDS; CCDS42612.1; -. [Q8N423-2]
CCDS; CCDS62791.1; -. [Q8N423-4]
CCDS; CCDS62792.1; -. [Q8N423-3]
UniGene; Hs.655652; -.
PDB; 2DYP; X-ray; 2.50 A; D=24-219.
PDB; 2GW5; X-ray; 1.80 A; A=24-219.
PDB; 4LLA; X-ray; 2.50 A; A/B/C=222-419.
PDBsum; 2DYP; -.
PDBsum; 2GW5; -.
PDBsum; 4LLA; -.
ProteinModelPortal; Q8N423; -.
SMR; Q8N423; -.
DIP; DIP-59888N; -.
IntAct; Q8N423; 23.
STRING; 9606.ENSP00000375629; -.
iPTMnet; Q8N423; -.
PhosphoSitePlus; Q8N423; -.
BioMuta; LILRB2; -.
DMDM; 311033485; -.
PaxDb; Q8N423; -.
PeptideAtlas; Q8N423; -.
PRIDE; Q8N423; -.
ProteomicsDB; 71866; -.
ProteomicsDB; 71867; -. [Q8N423-2]
DNASU; 10288; -.
Ensembl; ENST00000314446; ENSP00000319960; ENSG00000131042.
Ensembl; ENST00000391746; ENSP00000375626; ENSG00000131042.
Ensembl; ENST00000391748; ENSP00000375628; ENSG00000131042.
Ensembl; ENST00000391749; ENSP00000375629; ENSG00000131042.
Ensembl; ENST00000434421; ENSP00000410117; ENSG00000131042.
Ensembl; ENST00000610886; ENSP00000482933; ENSG00000276146.
Ensembl; ENST00000614225; ENSP00000480841; ENSG00000275463. [Q8N423-4]
Ensembl; ENST00000617341; ENSP00000484373; ENSG00000276146.
Ensembl; ENST00000617886; ENSP00000483553; ENSG00000276146.
Ensembl; ENST00000618392; ENSP00000480302; ENSG00000274513.
Ensembl; ENST00000618705; ENSP00000481208; ENSG00000275463. [Q8N423-1]
Ensembl; ENST00000619122; ENSP00000483478; ENSG00000275463. [Q8N423-3]
Ensembl; ENST00000621020; ENSP00000483014; ENSG00000275463. [Q8N423-2]
UCSC; uc010eri.4; human. [Q8N423-1]
DisGeNET; 10288; -.
EuPathDB; HostDB:ENSG00000131042.13; -.
GeneCards; LILRB2; -.
HGNC; HGNC:6606; LILRB2.
MIM; 604815; gene.
neXtProt; NX_Q8N423; -.
PharmGKB; PA30380; -.
eggNOG; ENOG410IKJD; Eukaryota.
eggNOG; ENOG41116BR; LUCA.
HOGENOM; HOG000234395; -.
HOVERGEN; HBG074353; -.
InParanoid; Q8N423; -.
OrthoDB; EOG091G0D6W; -.
PhylomeDB; Q8N423; -.
TreeFam; TF336644; -.
Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-HSA-6798695; Neutrophil degranulation.
SIGNOR; Q8N423; -.
ChiTaRS; LILRB2; human.
EvolutionaryTrace; Q8N423; -.
PRO; PR:Q8N423; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000131042; Expressed in 139 organ(s), highest expression level in blood.
CleanEx; HS_LILRB2; -.
ExpressionAtlas; Q8N423; baseline and differential.
Genevisible; Q8N423; HS.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0016020; C:membrane; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
GO; GO:0001540; F:amyloid-beta binding; IMP:ARUK-UCL.
GO; GO:0050839; F:cell adhesion molecule binding; IPI:BHF-UCL.
GO; GO:0032396; F:inhibitory MHC class I receptor activity; IDA:BHF-UCL.
GO; GO:0042288; F:MHC class I protein binding; IDA:UniProtKB.
GO; GO:0023029; F:MHC class Ib protein binding; IPI:BHF-UCL.
GO; GO:0042803; F:protein homodimerization activity; IDA:ARUK-UCL.
GO; GO:0008157; F:protein phosphatase 1 binding; IPI:UniProtKB.
GO; GO:0044877; F:protein-containing complex binding; IPI:ARUK-UCL.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
GO; GO:0006968; P:cellular defense response; TAS:ProtInc.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:BHF-UCL.
GO; GO:0002774; P:Fc receptor mediated inhibitory signaling pathway; IDA:UniProtKB.
GO; GO:0034113; P:heterotypic cell-cell adhesion; IDA:BHF-UCL.
GO; GO:0006955; P:immune response; TAS:ProtInc.
GO; GO:0002767; P:immune response-inhibiting cell surface receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0007611; P:learning or memory; ISS:ARUK-UCL.
GO; GO:0002578; P:negative regulation of antigen processing and presentation; IDA:BHF-UCL.
GO; GO:0051926; P:negative regulation of calcium ion transport; IDA:UniProtKB.
GO; GO:1905875; P:negative regulation of postsynaptic density organization; IC:ARUK-UCL.
GO; GO:0051248; P:negative regulation of protein metabolic process; ISS:ARUK-UCL.
GO; GO:0042130; P:negative regulation of T cell proliferation; IDA:BHF-UCL.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0032755; P:positive regulation of interleukin-6 production; NAS:BHF-UCL.
GO; GO:1900454; P:positive regulation of long-term synaptic depression; ISS:ARUK-UCL.
GO; GO:0035307; P:positive regulation of protein dephosphorylation; ISS:ARUK-UCL.
GO; GO:0045591; P:positive regulation of regulatory T cell differentiation; IMP:BHF-UCL.
GO; GO:0042102; P:positive regulation of T cell proliferation; IDA:BHF-UCL.
GO; GO:0002666; P:positive regulation of T cell tolerance induction; IMP:BHF-UCL.
GO; GO:0002645; P:positive regulation of tolerance induction; IMP:UniProtKB.
GO; GO:2001198; P:regulation of dendritic cell differentiation; IC:BHF-UCL.
GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
GO; GO:1900271; P:regulation of long-term synaptic potentiation; ISS:ARUK-UCL.
GO; GO:0007165; P:signal transduction; IDA:BHF-UCL.
Gene3D; 2.60.40.10; -; 4.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
Pfam; PF13895; Ig_2; 1.
SMART; SM00409; IG; 3.
SMART; SM00408; IGc2; 3.
SUPFAM; SSF48726; SSF48726; 4.
PROSITE; PS50835; IG_LIKE; 2.
1: Evidence at protein level;
3D-structure; Adaptive immunity; Alternative splicing;
Complete proteome; Disulfide bond; Glycoprotein; Immunity;
Immunoglobulin domain; Membrane; Phosphoprotein; Polymorphism;
Receptor; Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 598 Leukocyte immunoglobulin-like receptor
subfamily B member 2.
/FTId=PRO_0000014821.
TOPO_DOM 22 461 Extracellular. {ECO:0000255}.
TRANSMEM 462 482 Helical. {ECO:0000255}.
TOPO_DOM 483 598 Cytoplasmic. {ECO:0000255}.
DOMAIN 27 110 Ig-like C2-type 1.
DOMAIN 111 229 Ig-like C2-type 2.
DOMAIN 230 318 Ig-like C2-type 3.
DOMAIN 330 419 Ig-like C2-type 4.
MOTIF 531 536 ITIM motif 1.
MOTIF 560 565 ITIM motif 2.
MOTIF 590 595 ITIM motif 3.
CARBOHYD 280 280 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 301 301 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 340 340 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 49 98 {ECO:0000244|PDB:2GW5,
ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:12390682}.
DISULFID 144 196 {ECO:0000244|PDB:2GW5,
ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:12390682}.
DISULFID 156 166 {ECO:0000244|PDB:2GW5,
ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:12390682}.
DISULFID 245 296 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 345 396 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 1 116 Missing (in isoform 4). {ECO:0000305}.
/FTId=VSP_055718.
VAR_SEQ 437 437 Missing (in isoform 2).
{ECO:0000303|Ref.3}.
/FTId=VSP_008458.
VAR_SEQ 495 510 TQRKADFQHPAGAVGP -> SPAQLPTPRKKTSMLP (in
isoform 3). {ECO:0000303|PubMed:9382880}.
/FTId=VSP_055719.
VAR_SEQ 511 598 Missing (in isoform 3).
{ECO:0000303|PubMed:9382880}.
/FTId=VSP_055720.
VARIANT 20 20 H -> R (in dbSNP:rs383369).
/FTId=VAR_016997.
VARIANT 161 161 E -> D (in dbSNP:rs373032).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9382880,
ECO:0000269|PubMed:9548455,
ECO:0000269|Ref.3}.
/FTId=VAR_016998.
VARIANT 235 235 V -> M (in dbSNP:rs386056).
/FTId=VAR_047432.
VARIANT 300 300 H -> Y (in dbSNP:rs7247538).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9382880,
ECO:0000269|PubMed:9548455,
ECO:0000269|Ref.3}.
/FTId=VAR_016999.
VARIANT 306 306 C -> W (in dbSNP:rs7247451).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9382880,
ECO:0000269|PubMed:9548455,
ECO:0000269|Ref.3}.
/FTId=VAR_017000.
VARIANT 322 322 R -> H (in dbSNP:rs1128646).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9382880,
ECO:0000269|PubMed:9548455,
ECO:0000269|Ref.3}.
/FTId=VAR_061314.
VARIANT 324 324 T -> R (in dbSNP:rs7247055).
/FTId=VAR_047433.
VARIANT 326 326 F -> S (in dbSNP:rs7246737).
/FTId=VAR_047434.
VARIANT 349 349 R -> G (in dbSNP:rs7247025).
/FTId=VAR_047435.
VARIANT 403 403 D -> N (in dbSNP:rs4993133).
/FTId=VAR_061315.
CONFLICT 583 583 R -> G (in Ref. 5; AAH36827).
{ECO:0000305}.
STRAND 30 35 {ECO:0000244|PDB:2GW5}.
STRAND 37 40 {ECO:0000244|PDB:2GW5}.
STRAND 45 50 {ECO:0000244|PDB:2GW5}.
STRAND 57 63 {ECO:0000244|PDB:2GW5}.
STRAND 71 73 {ECO:0000244|PDB:2DYP}.
HELIX 75 77 {ECO:0000244|PDB:2GW5}.
HELIX 78 80 {ECO:0000244|PDB:2DYP}.
STRAND 82 87 {ECO:0000244|PDB:2GW5}.
TURN 90 92 {ECO:0000244|PDB:2GW5}.
STRAND 94 102 {ECO:0000244|PDB:2GW5}.
STRAND 113 118 {ECO:0000244|PDB:2GW5}.
STRAND 125 130 {ECO:0000244|PDB:2GW5}.
STRAND 140 158 {ECO:0000244|PDB:2GW5}.
STRAND 166 168 {ECO:0000244|PDB:2GW5}.
STRAND 176 183 {ECO:0000244|PDB:2GW5}.
STRAND 188 190 {ECO:0000244|PDB:2DYP}.
STRAND 193 199 {ECO:0000244|PDB:2GW5}.
STRAND 226 231 {ECO:0000244|PDB:4LLA}.
STRAND 233 235 {ECO:0000244|PDB:4LLA}.
STRAND 241 249 {ECO:0000244|PDB:4LLA}.
STRAND 252 258 {ECO:0000244|PDB:4LLA}.
STRAND 264 268 {ECO:0000244|PDB:4LLA}.
STRAND 277 283 {ECO:0000244|PDB:4LLA}.
HELIX 288 290 {ECO:0000244|PDB:4LLA}.
STRAND 292 299 {ECO:0000244|PDB:4LLA}.
STRAND 313 317 {ECO:0000244|PDB:4LLA}.
STRAND 326 331 {ECO:0000244|PDB:4LLA}.
STRAND 333 335 {ECO:0000244|PDB:4LLA}.
STRAND 342 349 {ECO:0000244|PDB:4LLA}.
STRAND 352 361 {ECO:0000244|PDB:4LLA}.
STRAND 366 369 {ECO:0000244|PDB:4LLA}.
STRAND 371 373 {ECO:0000244|PDB:4LLA}.
STRAND 376 382 {ECO:0000244|PDB:4LLA}.
HELIX 388 390 {ECO:0000244|PDB:4LLA}.
STRAND 392 400 {ECO:0000244|PDB:4LLA}.
STRAND 403 407 {ECO:0000244|PDB:4LLA}.
STRAND 414 418 {ECO:0000244|PDB:4LLA}.
SEQUENCE 598 AA; 65039 MW; 33E9737AFCAFCE2D CRC64;
MTPIVTVLIC LGLSLGPRTH VQTGTIPKPT LWAEPDSVIT QGSPVTLSCQ GSLEAQEYRL
YREKKSASWI TRIRPELVKN GQFHIPSITW EHTGRYGCQY YSRARWSELS DPLVLVMTGA
YPKPTLSAQP SPVVTSGGRV TLQCESQVAF GGFILCKEGE EEHPQCLNSQ PHARGSSRAI
FSVGPVSPNR RWSHRCYGYD LNSPYVWSSP SDLLELLVPG VSKKPSLSVQ PGPVVAPGES
LTLQCVSDVG YDRFVLYKEG ERDLRQLPGR QPQAGLSQAN FTLGPVSRSY GGQYRCYGAH
NLSSECSAPS DPLDILITGQ IRGTPFISVQ PGPTVASGEN VTLLCQSWRQ FHTFLLTKAG
AADAPLRLRS IHEYPKYQAE FPMSPVTSAH AGTYRCYGSL NSDPYLLSHP SEPLELVVSG
PSMGSSPPPT GPISTPAGPE DQPLTPTGSD PQSGLGRHLG VVIGILVAVV LLLLLLLLLF
LILRHRRQGK HWTSTQRKAD FQHPAGAVGP EPTDRGLQWR SSPAADAQEE NLYAAVKDTQ
PEDGVEMDTR AAASEAPQDV TYAQLHSLTL RRKATEPPPS QEREPPAEPS IYATLAIH


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