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HLA class I histocompatibility antigen, alpha chain G (HLA G antigen) (MHC class I antigen G)

 HLAG_HUMAN              Reviewed;         338 AA.
P17693;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
01-AUG-1990, sequence version 1.
22-NOV-2017, entry version 175.
RecName: Full=HLA class I histocompatibility antigen, alpha chain G;
AltName: Full=HLA G antigen;
AltName: Full=MHC class I antigen G;
Flags: Precursor;
Name=HLA-G; Synonyms=HLA-6.0, HLAG;
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 1), AND TISSUE SPECIFICITY.
TISSUE=Fetal eye;
PubMed=2336406; DOI=10.1093/nar/18.8.2189;
Shukla H., Swaroop A., Srivastava R., Weissman S.M.;
"The mRNA of a human class I gene HLA G/HLA 6.0 exhibits a restricted
pattern of expression.";
Nucleic Acids Res. 18:2189-2189(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3480534; DOI=10.1073/pnas.84.24.9145;
Geraghty D.E., Koller B.H., Orr H.T.;
"A human major histocompatibility complex class I gene that encodes a
protein with a shortened cytoplasmic segment.";
Proc. Natl. Acad. Sci. U.S.A. 84:9145-9149(1987).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Placenta;
Ishitani A., Geraghty D.E.;
Submitted (APR-1992) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10727083; DOI=10.3109/10425179909033955;
Hampe A., Coriton O., Andrieux N., Carn G., Lepourcelet M.,
Mottier S., Dreano S., Gatius M.T., Hitte C., Soriano N., Galibert F.;
"A 356-Kb sequence of the subtelomeric part of the MHC class I
region.";
DNA Seq. 10:263-299(1999).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Shiina S., Tamiya G., Oka A., Inoko H.;
"Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
[6]
ALTERNATIVE SPLICING (ISOFORMS 1; 2 AND 3), AND TISSUE SPECIFICITY.
PubMed=1570318;
Ishitani A., Geraghty D.E.;
"Alternative splicing of HLA-G transcripts yields proteins with
primary structures resembling both class I and class II antigens.";
Proc. Natl. Acad. Sci. U.S.A. 89:3947-3951(1992).
[7]
ALTERNATIVE SPLICING (ISOFORM 4), AND TISSUE SPECIFICITY (ISOFORM
HLA-G4).
PubMed=7589701;
Moreau P., Teyssier M., Kirszenbaum M., Gluckman E., Gourand L.,
Carosella E., Dausset J.;
"HLA-G mRNA forms in human trophoblasts and peripheral blood
lymphocytes: potential use in prenatal diagnosis.";
Folia Biol. (Praha) 40:431-438(1994).
[8]
ALTERNATIVE SPLICING (ISOFORMS 5 AND 6).
PubMed=7989753;
Fujii T., Ishitani A., Geraghty D.E.;
"A soluble form of the HLA-G antigen is encoded by a messenger
ribonucleic acid containing intron 4.";
J. Immunol. 153:5516-5524(1994).
[9]
ALTERNATIVE SPLICING (ISOFORM 4).
PubMed=8183892;
Kirszenbaum M., Moreau P., Gluckman E., Dausset J., Carosella E.;
"An alternatively spliced form of HLA-G mRNA in human trophoblasts and
evidence for the presence of HLA-G transcript in adult lymphocytes.";
Proc. Natl. Acad. Sci. U.S.A. 91:4209-4213(1994).
[10]
ALTERNATIVE SPLICING (ISOFORM 5), AND SUBCELLULAR LOCATION (ISOFORM
5).
PubMed=7558941;
Moreau P., Carosella E., Teyssier M., Prost S., Gluckman E.,
Dausset J., Kirszenbaum M.;
"Soluble HLA-G molecule. An alternatively spliced HLA-G mRNA form
candidate to encode it in peripheral blood mononuclear cells and human
trophoblasts.";
Hum. Immunol. 43:231-236(1995).
[11]
ALTERNATIVE SPLICING (ISOFORM 7), SUBCELLULAR LOCATION (ISOFORM 5),
AND TISSUE SPECIFICITY (ISOFORM 7).
PubMed=11137219;
Paul P., Cabestre F.A., Ibrahim E.C., Lefebvre S., Khalil-Daher I.,
Vazeux G., Quiles R.M., Bermond F., Dausset J., Carosella E.D.;
"Identification of HLA-G7 as a new splice variant of the HLA-G mRNA
and expression of soluble HLA-G5, -G6, and -G7 transcripts in human
transfected cells.";
Hum. Immunol. 61:1138-1149(2000).
[12]
SUBUNIT, MUTAGENESIS OF CYS-66, AND DISULFIDE BOND AT CYS-66.
PubMed=12454284; DOI=10.1073/pnas.212643199;
Boyson J.E., Erskine R., Whitman M.C., Chiu M., Lau J.M.,
Koopman L.A., Valter M.M., Angelisova P., Horejsi V., Strominger J.L.;
"Disulfide bond-mediated dimerization of HLA-G on the cell surface.";
Proc. Natl. Acad. Sci. U.S.A. 99:16180-16185(2002).
[13]
SUBUNIT (ISOFORM 2), INTERACTION WITH LILRB2 (ISOFORM 2), AND
MUTAGENESIS OF CYS-66.
PubMed=28348268; DOI=10.4049/jimmunol.1601296;
Kuroki K., Mio K., Takahashi A., Matsubara H., Kasai Y., Manaka S.,
Kikkawa M., Hamada D., Sato C., Maenaka K.;
"Class II-like structural features and strong receptor binding of the
nonclassical HLA-G2 isoform homodimer.";
J. Immunol. 198:3399-3403(2017).
[14]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 26-300.
PubMed=15718280; DOI=10.1073/pnas.0409676102;
Clements C.S., Kjer-Nielsen L., Kostenko L., Hoare H.L.,
Dunstone M.A., Moses E., Freed K., Brooks A.G., Rossjohn J.,
McCluskey J.;
"Crystal structure of HLA-G: a nonclassical MHC class I molecule
expressed at the fetal-maternal interface.";
Proc. Natl. Acad. Sci. U.S.A. 102:3360-3365(2005).
[15]
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 25-300, DISULFIDE BONDS, AND
INTERACTION WITH LILRB1 AND LILRB2.
PubMed=16455647; DOI=10.1074/jbc.M512305200;
Shiroishi M., Kuroki K., Ose T., Rasubala L., Shiratori I., Arase H.,
Tsumoto K., Kumagai I., Kohda D., Maenaka K.;
"Efficient leukocyte Ig-like receptor signaling and crystal structure
of disulfide-linked HLA-G dimer.";
J. Biol. Chem. 281:10439-10447(2006).
-!- FUNCTION: Involved in the presentation of foreign antigens to the
immune system. Plays a role in maternal tolerance of the fetus by
mediating protection from the deleterious effects of natural
killer cells, cytotoxic T-lymphocytes, macrophages and mononuclear
cells.
-!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2-
microglobulin). Homodimer; disulfide-linked (PubMed:12454284,
PubMed:16455647). Binds to LILRB1 and LILRB2 (PubMed:16455647).
Isoform 2: Forms a non-disulfide-linked homodimer and interacts
with LILRB2 (PubMed:28348268). {ECO:0000269|PubMed:12454284,
ECO:0000269|PubMed:16455647, ECO:0000269|PubMed:28348268}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-1043063, EBI-1043063;
Q8N423:LILRB2; NbExp=3; IntAct=EBI-1043063, EBI-2816428;
-!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane {ECO:0000305};
Single-pass type I membrane protein {ECO:0000255}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cell membrane {ECO:0000305};
Single-pass type I membrane protein {ECO:0000255}.
-!- SUBCELLULAR LOCATION: Isoform 3: Cell membrane {ECO:0000305};
Single-pass type I membrane protein {ECO:0000255}.
-!- SUBCELLULAR LOCATION: Isoform 4: Cell membrane {ECO:0000305};
Single-pass type I membrane protein {ECO:0000255}.
-!- SUBCELLULAR LOCATION: Isoform 5: Secreted
{ECO:0000269|PubMed:11137219, ECO:0000269|PubMed:7558941}.
-!- SUBCELLULAR LOCATION: Isoform 6: Secreted {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Isoform 7: Secreted {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Name=1; Synonyms=HLA-G1 {ECO:0000303|PubMed:1570318};
IsoId=P17693-1; Sequence=Displayed;
Name=2; Synonyms=HLA-G2 {ECO:0000303|PubMed:1570318};
IsoId=P17693-2; Sequence=VSP_059192, VSP_059195;
Name=3; Synonyms=HLA-G3 {ECO:0000303|PubMed:1570318};
IsoId=P17693-3; Sequence=VSP_059191;
Name=4; Synonyms=HLA-G.3-5 {ECO:0000303|PubMed:8183892}, HLA-G4
{ECO:0000303|PubMed:7589701};
IsoId=P17693-4; Sequence=VSP_059196;
Name=5; Synonyms=HLA-G1sol {ECO:0000303|PubMed:7989753}, HLA-G5
{ECO:0000303|PubMed:7558941};
IsoId=P17693-5; Sequence=VSP_059197;
Name=6; Synonyms=HLA-G2sol {ECO:0000303|PubMed:7989753}, HLA-G6
{ECO:0000303|PubMed:11137219};
IsoId=P17693-6; Sequence=VSP_059192, VSP_059195, VSP_059197;
Name=7; Synonyms=HLA-G7 {ECO:0000303|PubMed:11137219};
IsoId=P17693-7; Sequence=VSP_059193, VSP_059194;
-!- TISSUE SPECIFICITY: Expressed in trophoblasts. Expressed in fetal
eye and thymus (PubMed:2336406). Also expressed in adult eye
(PubMed:1570318). Isoform 4: Expressed in fetal first trimester
trophoblasts (PubMed:7589701). Isoform 7: Expressed in first
trimester, second trimester and term placenta, fetal liver,
amniotic membrane, skin, cord blood and peripheral blood
mononuclear cells (PubMed:11137219). {ECO:0000269|PubMed:11137219,
ECO:0000269|PubMed:1570318, ECO:0000269|PubMed:2336406,
ECO:0000269|PubMed:7589701}.
-!- SIMILARITY: Belongs to the MHC class I family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/HLAGID43744ch6p22.html";
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EMBL; X17273; CAA35174.1; -; mRNA.
EMBL; J03027; AAA98745.1; -; Genomic_DNA.
EMBL; M90683; AAA52673.1; -; mRNA.
EMBL; AF055066; AAC24826.1; -; Genomic_DNA.
EMBL; BA000025; BAB63336.1; -; Genomic_DNA.
CCDS; CCDS4668.1; -. [P17693-1]
PIR; A39953; A39953.
RefSeq; NP_002118.1; NM_002127.5.
UniGene; Hs.512152; -.
PDB; 1YDP; X-ray; 1.90 A; A=26-300.
PDB; 2D31; X-ray; 3.20 A; A/D=25-300.
PDB; 2DYP; X-ray; 2.50 A; A=25-300.
PDB; 3BZE; X-ray; 2.50 A; P/Q/R/S=3-11.
PDB; 3CDG; X-ray; 3.40 A; P/Q=3-11.
PDB; 3CII; X-ray; 4.41 A; C/F=3-11.
PDB; 3KYN; X-ray; 2.40 A; A=26-299.
PDB; 3KYO; X-ray; 1.70 A; A/C=26-298.
PDBsum; 1YDP; -.
PDBsum; 2D31; -.
PDBsum; 2DYP; -.
PDBsum; 3BZE; -.
PDBsum; 3CDG; -.
PDBsum; 3CII; -.
PDBsum; 3KYN; -.
PDBsum; 3KYO; -.
ProteinModelPortal; P17693; -.
SMR; P17693; -.
BioGrid; 109380; 18.
DIP; DIP-46121N; -.
IntAct; P17693; 5.
STRING; 9606.ENSP00000353472; -.
iPTMnet; P17693; -.
PhosphoSitePlus; P17693; -.
SwissPalm; P17693; -.
BioMuta; HLA-G; -.
DMDM; 122132; -.
EPD; P17693; -.
PaxDb; P17693; -.
PeptideAtlas; P17693; -.
PRIDE; P17693; -.
DNASU; 3135; -.
Ensembl; ENST00000360323; ENSP00000353472; ENSG00000204632. [P17693-1]
Ensembl; ENST00000376815; ENSP00000366011; ENSG00000204632. [P17693-3]
Ensembl; ENST00000383621; ENSP00000373116; ENSG00000206506. [P17693-1]
Ensembl; ENST00000383622; ENSP00000373117; ENSG00000206506. [P17693-3]
Ensembl; ENST00000415687; ENSP00000389969; ENSG00000237216. [P17693-3]
Ensembl; ENST00000423011; ENSP00000389522; ENSG00000233095. [P17693-1]
Ensembl; ENST00000423373; ENSP00000405238; ENSG00000235346. [P17693-1]
Ensembl; ENST00000428701; ENSP00000412927; ENSG00000204632. [P17693-1]
Ensembl; ENST00000428952; ENSP00000388176; ENSG00000235680. [P17693-1]
Ensembl; ENST00000429890; ENSP00000401326; ENSG00000235680. [P17693-3]
Ensembl; ENST00000444098; ENSP00000398200; ENSG00000230413. [P17693-1]
Ensembl; ENST00000445373; ENSP00000416408; ENSG00000230413. [P17693-3]
Ensembl; ENST00000448306; ENSP00000413926; ENSG00000233095. [P17693-3]
Ensembl; ENST00000449127; ENSP00000408773; ENSG00000237216. [P17693-1]
Ensembl; ENST00000457132; ENSP00000410247; ENSG00000235346. [P17693-3]
Ensembl; ENST00000546545; ENSP00000447762; ENSG00000230413. [P17693-1]
Ensembl; ENST00000546634; ENSP00000447780; ENSG00000235346. [P17693-1]
Ensembl; ENST00000547241; ENSP00000448085; ENSG00000233095. [P17693-1]
Ensembl; ENST00000547931; ENSP00000448363; ENSG00000237216. [P17693-1]
Ensembl; ENST00000550897; ENSP00000449903; ENSG00000235680. [P17693-1]
Ensembl; ENST00000553052; ENSP00000449291; ENSG00000206506. [P17693-1]
Ensembl; ENST00000622601; ENSP00000479399; ENSG00000276051. [P17693-3]
GeneID; 3135; -.
KEGG; hsa:3135; -.
CTD; 3135; -.
DisGeNET; 3135; -.
EuPathDB; HostDB:ENSG00000204632.11; -.
GeneCards; HLA-G; -.
H-InvDB; HIX0166674; -.
H-InvDB; HIX0167370; -.
HGNC; HGNC:4964; HLA-G.
HPA; CAB016158; -.
MalaCards; HLA-G; -.
MIM; 142871; gene.
neXtProt; NX_P17693; -.
OpenTargets; ENSG00000204632; -.
PharmGKB; PA35083; -.
eggNOG; ENOG410II5V; Eukaryota.
eggNOG; ENOG4111K8F; LUCA.
GeneTree; ENSGT00760000118960; -.
HOVERGEN; HBG016709; -.
InParanoid; P17693; -.
KO; K06751; -.
PhylomeDB; P17693; -.
TreeFam; TF336617; -.
Reactome; R-HSA-1236974; ER-Phagosome pathway.
Reactome; R-HSA-1236977; Endosomal/Vacuolar pathway.
Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-HSA-877300; Interferon gamma signaling.
Reactome; R-HSA-909733; Interferon alpha/beta signaling.
Reactome; R-HSA-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
SIGNOR; P17693; -.
ChiTaRS; HLA-G; human.
EvolutionaryTrace; P17693; -.
GeneWiki; HLA-G; -.
GenomeRNAi; 3135; -.
PRO; PR:P17693; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000204632; -.
CleanEx; HS_HLA-G; -.
ExpressionAtlas; P17693; baseline and differential.
Genevisible; P17693; HS.
GO; GO:0031901; C:early endosome membrane; TAS:Reactome.
GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0042612; C:MHC class I protein complex; IEA:UniProtKB-KW.
GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0055038; C:recycling endosome membrane; TAS:Reactome.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0042605; F:peptide antigen binding; IBA:GO_Central.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0005102; F:receptor binding; IPI:UniProtKB.
GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
GO; GO:0002480; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent; TAS:Reactome.
GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; IBA:GO_Central.
GO; GO:0006968; P:cellular defense response; TAS:ProtInc.
GO; GO:0002767; P:immune response-inhibiting cell surface receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
GO; GO:2001199; P:negative regulation of dendritic cell differentiation; IDA:BHF-UCL.
GO; GO:0050777; P:negative regulation of immune response; IC:UniProtKB.
GO; GO:0042130; P:negative regulation of T cell proliferation; IDA:BHF-UCL.
GO; GO:0032735; P:positive regulation of interleukin-12 production; IDA:BHF-UCL.
GO; GO:0045591; P:positive regulation of regulatory T cell differentiation; IMP: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:0050776; P:regulation of immune response; TAS:Reactome.
GO; GO:0060337; P:type I interferon signaling pathway; TAS:Reactome.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 3.30.500.10; -; 1.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003006; Ig/MHC_CS.
InterPro; IPR003597; Ig_C1-set.
InterPro; IPR011161; MHC_I-like_Ag-recog.
InterPro; IPR037055; MHC_I-like_Ag-recog_sf.
InterPro; IPR011162; MHC_I/II-like_Ag-recog.
InterPro; IPR001039; MHC_I_a_a1/a2.
Pfam; PF07654; C1-set; 1.
Pfam; PF00129; MHC_I; 1.
PRINTS; PR01638; MHCCLASSI.
SMART; SM00407; IGc1; 1.
SUPFAM; SSF48726; SSF48726; 1.
SUPFAM; SSF54452; SSF54452; 1.
PROSITE; PS50835; IG_LIKE; 1.
PROSITE; PS00290; IG_MHC; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; Immunity; Membrane; MHC I;
Reference proteome; Secreted; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 24
CHAIN 25 338 HLA class I histocompatibility antigen,
alpha chain G.
/FTId=PRO_0000018886.
TOPO_DOM 25 308 Extracellular. {ECO:0000255}.
TRANSMEM 309 332 Helical. {ECO:0000255}.
TOPO_DOM 333 338 Cytoplasmic. {ECO:0000255}.
DOMAIN 209 299 Ig-like C1-type.
REGION 25 114 Alpha-1.
REGION 115 206 Alpha-2.
REGION 207 298 Alpha-3.
REGION 299 308 Connecting peptide.
CARBOHYD 110 110 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
DISULFID 66 66 Interchain. {ECO:0000255|PROSITE-
ProRule:PRU00114,
ECO:0000269|PubMed:12454284}.
DISULFID 125 188 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:16455647}.
DISULFID 227 283 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:16455647}.
VAR_SEQ 115 298 Missing (in isoform 3).
{ECO:0000269|PubMed:1570318}.
/FTId=VSP_059191.
VAR_SEQ 115 206 Missing (in isoform 2 and isoform 6).
{ECO:0000269|PubMed:1570318}.
/FTId=VSP_059192.
VAR_SEQ 116 116 S -> E (in isoform 7).
{ECO:0000269|PubMed:11137219}.
/FTId=VSP_059193.
VAR_SEQ 117 338 Missing (in isoform 7).
{ECO:0000269|PubMed:11137219}.
/FTId=VSP_059194.
VAR_SEQ 207 298 Missing (in isoform 4).
{ECO:0000269|PubMed:7589701,
ECO:0000269|PubMed:8183892}.
/FTId=VSP_059196.
VAR_SEQ 207 207 D -> K (in isoform 2 and isoform 6).
{ECO:0000269|PubMed:1570318}.
/FTId=VSP_059195.
VAR_SEQ 299 338 KQSSLPTIPIMGIVAGLVVLAAVVTGAAVAAVLWRKKSSD
-> SKEGDGGIMSVRESRSLSEDL (in isoform 5
and isoform 6).
{ECO:0000269|PubMed:7989753}.
/FTId=VSP_059197.
MUTAGEN 66 66 C->S: Abolishes homodimerization. Does
not affect binding of isoform 2 to
LILRB2. {ECO:0000269|PubMed:12454284,
ECO:0000269|PubMed:28348268}.
STRAND 27 36 {ECO:0000244|PDB:3KYO}.
STRAND 41 43 {ECO:0000244|PDB:3KYO}.
STRAND 45 52 {ECO:0000244|PDB:3KYO}.
STRAND 55 61 {ECO:0000244|PDB:3KYO}.
STRAND 64 66 {ECO:0000244|PDB:3KYO}.
STRAND 70 73 {ECO:0000244|PDB:2D31}.
HELIX 74 76 {ECO:0000244|PDB:3KYO}.
HELIX 81 108 {ECO:0000244|PDB:3KYO}.
STRAND 113 115 {ECO:0000244|PDB:2DYP}.
STRAND 118 132 {ECO:0000244|PDB:3KYO}.
STRAND 134 142 {ECO:0000244|PDB:3KYO}.
STRAND 145 150 {ECO:0000244|PDB:3KYO}.
STRAND 157 161 {ECO:0000244|PDB:3KYO}.
HELIX 162 173 {ECO:0000244|PDB:3KYO}.
HELIX 176 185 {ECO:0000244|PDB:3KYO}.
HELIX 187 198 {ECO:0000244|PDB:3KYO}.
HELIX 200 203 {ECO:0000244|PDB:3KYO}.
STRAND 210 218 {ECO:0000244|PDB:3KYO}.
TURN 219 221 {ECO:0000244|PDB:3KYO}.
STRAND 222 235 {ECO:0000244|PDB:3KYO}.
STRAND 238 243 {ECO:0000244|PDB:3KYO}.
STRAND 246 248 {ECO:0000244|PDB:3KYO}.
HELIX 249 251 {ECO:0000244|PDB:1YDP}.
STRAND 261 263 {ECO:0000244|PDB:3KYO}.
STRAND 265 274 {ECO:0000244|PDB:3KYO}.
HELIX 278 280 {ECO:0000244|PDB:3KYO}.
STRAND 281 286 {ECO:0000244|PDB:3KYO}.
STRAND 290 292 {ECO:0000244|PDB:3KYO}.
STRAND 294 296 {ECO:0000244|PDB:3KYO}.
SEQUENCE 338 AA; 38224 MW; 0678E263BE8962FF CRC64;
MVVMAPRTLF LLLSGALTLT ETWAGSHSMR YFSAAVSRPG RGEPRFIAMG YVDDTQFVRF
DSDSACPRME PRAPWVEQEG PEYWEEETRN TKAHAQTDRM NLQTLRGYYN QSEASSHTLQ
WMIGCDLGSD GRLLRGYEQY AYDGKDYLAL NEDLRSWTAA DTAAQISKRK CEAANVAEQR
RAYLEGTCVE WLHRYLENGK EMLQRADPPK THVTHHPVFD YEATLRCWAL GFYPAEIILT
WQRDGEDQTQ DVELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PEPLMLRWKQ
SSLPTIPIMG IVAGLVVLAA VVTGAAVAAV LWRKKSSD


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