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HLA class II histocompatibility antigen, DRB1-15 beta chain (DW2.2/DR2.2) (MHC class II antigen DRB1*15)

 2B1F_HUMAN              Reviewed;         266 AA.
P01911; Q29790; Q29975; Q30142; Q30166; Q32MY7; Q56FN9; Q5Y7B0;
Q5Y7B9;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
15-JAN-2008, sequence version 2.
27-SEP-2017, entry version 148.
RecName: Full=HLA class II histocompatibility antigen, DRB1-15 beta chain;
AltName: Full=DW2.2/DR2.2;
AltName: Full=MHC class II antigen DRB1*15;
Flags: Precursor;
Name=HLA-DRB1; Synonyms=HLA-DRB2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*15:01).
TISSUE=B-cell;
PubMed=3259543; DOI=10.1007/BF00364432;
Lock C.B., So A.K., Welsh K.I., Parkes J.D., Trowsdale J.;
"MHC class II sequences of an HLA-DR2 narcoleptic.";
Immunogenetics 27:449-455(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES DRB1*15:01; DRB1*15:02 AND
DRB1*15:03).
PubMed=16140993; DOI=10.1101/gr.3554305;
Raymond C.K., Kas A., Paddock M., Qiu R., Zhou Y., Subramanian S.,
Chang J., Palmieri A., Haugen E., Kaul R., Olson M.V.;
"Ancient haplotypes of the HLA Class II region.";
Genome Res. 15:1250-1257(2005).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELES DRB1*15:03 AND DRB1*15:04).
TISSUE=Blood;
PubMed=17174751; DOI=10.1016/j.humimm.2006.09.002;
Balas A., Vilches C., Rodriguez M.A., Fernandez B., Martinez M.P.,
de Pablo R., Garcia-Sanchez F., Vicario J.L.;
"Group-specific amplification of cDNA from DRB1 genes. Complete coding
sequences of partially defined alleles and identification of the new
alleles DRB1*040602, DRB1*111102, DRB1*080103, and DRB1*0113.";
Hum. Immunol. 67:1008-1016(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELE DRB1*15:01).
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELES DRB1*15:01 AND
DRB1*15:02).
TISSUE=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]
NUCLEOTIDE SEQUENCE [MRNA] OF 11-266 (ALLELE DRB1*15:02).
TISSUE=Lymphoblast;
PubMed=3571980;
Wu S.K., Yabe T., Madden M., Saunders T.L., Bach F.H.;
"cDNA cloning and sequencing reveals that the electrophoretically
constant DR beta 2 molecules, as well as the variable DR beta 1
molecules, from HLA-DR2 subtypes have different amino acid sequences
including a hypervariable region for a functionally important
epitope.";
J. Immunol. 138:2953-2959(1987).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 30-266 (ALLELE DRB1*15:01).
TISSUE=Lymphoblast;
PubMed=2885840; DOI=10.1073/pnas.84.13.4591;
Lee B.S.M., Rust N.A., McMichael A.J., McDevitt H.O.;
"HLA-DR2 subtypes form an additional supertypic family of DR beta
alleles.";
Proc. Natl. Acad. Sci. U.S.A. 84:4591-4595(1987).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 30-266 (ALLELE DRB1*15:01).
TISSUE=Lymphoblast;
PubMed=3476943; DOI=10.1073/pnas.84.17.6234;
Bell J.I., Denney D. Jr., Foster L., Belt T.K., Todd J.A.,
McDevitt H.O.;
"Allelic variation in the DR subregion of the human major
histocompatibility complex.";
Proc. Natl. Acad. Sci. U.S.A. 84:6234-6238(1987).
[9]
PROTEIN SEQUENCE OF 30-228.
TISSUE=Lymphoblast;
PubMed=6947956;
Kratzin H., Yang C.-Y., Gotz H., Pauly E., Kolbel S., Egert G.,
Thinnes F.P., Wernet P., Altevogt P., Hilschmann N.;
"Primary structure of class II human histocompatibility antigens. 1st
communication. Amino acid sequence of the N-terminal 198 residues of
the beta chain of a HLA-Dw2,2;DR2,2-alloantigen.";
Hoppe-Seyler's Z. Physiol. Chem. 362:1665-1669(1981).
[10]
PROTEIN SEQUENCE OF 30-64.
TISSUE=B-cell;
PubMed=6600932; DOI=10.1021/bi00270a027;
Walker L.E., Hewick R., Hunkapiller M.W., Hood L.E., Dreyer W.J.,
Reisfeld R.A.;
"N-terminal amino acid sequences of the alpha and beta chains of HLA-
DR1 and HLA-DR2 antigens.";
Biochemistry 22:185-188(1983).
[11]
REVIEW.
PubMed=8598037; DOI=10.1016/S0092-8674(00)81025-9;
Cresswell P.;
"Invariant chain structure and MHC class II function.";
Cell 84:505-507(1996).
[12]
REVIEW.
PubMed=11684289; DOI=10.1016/S0161-5890(01)00069-4;
Villadangos J.A.;
"Presentation of antigens by MHC class II molecules: getting the most
out of them.";
Mol. Immunol. 38:329-346(2001).
[13]
REVIEW.
PubMed=17241953; DOI=10.1016/j.immuni.2007.01.005;
Menendez-Benito V., Neefjes J.;
"Autophagy in MHC class II presentation: sampling from within.";
Immunity 26:1-3(2007).
[14]
REVIEW.
PubMed=18046453; DOI=10.1038/sj.emboj.7601945;
Rocha N., Neefjes J.;
"MHC class II molecules on the move for successful antigen
presentation.";
EMBO J. 27:1-5(2008).
[15]
UBIQUITINATION BY MARCH1, AND SUBCELLULAR LOCATION.
PubMed=18305173; DOI=10.1073/pnas.0708874105;
De Gassart A., Camosseto V., Thibodeau J., Ceppi M., Catalan N.,
Pierre P., Gatti E.;
"MHC class II stabilization at the surface of human dendritic cells is
the result of maturation-dependent MARCH I down-regulation.";
Proc. Natl. Acad. Sci. U.S.A. 105:3491-3496(2008).
[16]
REVIEW.
PubMed=19092054; DOI=10.1242/jcs.035089;
Berger A.C., Roche P.A.;
"MHC class II transport at a glance.";
J. Cell Sci. 122:1-4(2009).
[17]
REVIEW.
PubMed=19533806; DOI=10.3748/wjg.15.2855;
Beswick E.J., Reyes V.E.;
"CD74 in antigen presentation, inflammation, and cancers of the
gastrointestinal tract.";
World J. Gastroenterol. 15:2855-2861(2009).
[18]
X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 30-227.
PubMed=15821740; DOI=10.1038/ni1187;
Hahn M., Nicholson M.J., Pyrdol J., Wucherpfennig K.W.;
"Unconventional topology of self peptide-major histocompatibility
complex binding by a human autoimmune T cell receptor.";
Nat. Immunol. 6:490-496(2005).
-!- FUNCTION: Binds peptides derived from antigens that access the
endocytic route of antigen presenting cells (APC) and presents
them on the cell surface for recognition by the CD4 T-cells. The
peptide binding cleft accommodates peptides of 10-30 residues. The
peptides presented by MHC class II molecules are generated mostly
by degradation of proteins that access the endocytic route, where
they are processed by lysosomal proteases and other hydrolases.
Exogenous antigens that have been endocytosed by the APC are thus
readily available for presentation via MHC II molecules, and for
this reason this antigen presentation pathway is usually referred
to as exogenous. As membrane proteins on their way to degradation
in lysosomes as part of their normal turn-over are also contained
in the endosomal/lysosomal compartments, exogenous antigens must
compete with those derived from endogenous components. Autophagy
is also a source of endogenous peptides, autophagosomes
constitutively fuse with MHC class II loading compartments. In
addition to APCs, other cells of the gastrointestinal tract, such
as epithelial cells, express MHC class II molecules and CD74 and
act as APCs, which is an unusual trait of the GI tract. To produce
a MHC class II molecule that presents an antigen, three MHC class
II molecules (heterodimers of an alpha and a beta chain) associate
with a CD74 trimer in the ER to form a heterononamer. Soon after
the entry of this complex into the endosomal/lysosomal system
where antigen processing occurs, CD74 undergoes a sequential
degradation by various proteases, including CTSS and CTSL, leaving
a small fragment termed CLIP (class-II-associated invariant chain
peptide). The removal of CLIP is facilitated by HLA-DM via direct
binding to the alpha-beta-CLIP complex so that CLIP is released.
HLA-DM stabilizes MHC class II molecules until primary high
affinity antigenic peptides are bound. The MHC II molecule bound
to a peptide is then transported to the cell membrane surface. In
B-cells, the interaction between HLA-DM and MHC class II molecules
is regulated by HLA-DO. Primary dendritic cells (DCs) also to
express HLA-DO. Lysosomal microenvironment has been implicated in
the regulation of antigen loading into MHC II molecules, increased
acidification produces increased proteolysis and efficient peptide
loading.
-!- SUBUNIT: Heterodimer of an alpha and a beta subunit; also referred
as MHC class II molecule. In the endoplasmic reticulum (ER) it
forms a heterononamer; 3 MHC class II molecules bind to a CD74
homotrimer (also known as invariant chain or HLA class II
histocompatibility antigen gamma chain). In the
endosomal/lysosomal system; CD74 undergoes sequential degradation
by various proteases; leaving a small fragment termed CLIP on each
MHC class II molecule. MHC class II molecule interacts with
HLA_DM, and HLA_DO in B-cells, in order to release CLIP and
facilitate the binding of antigenic peptides.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18305173};
Single-pass type I membrane protein {ECO:0000269|PubMed:18305173}.
Endoplasmic reticulum membrane {ECO:0000269|PubMed:18305173};
Single-pass type I membrane protein {ECO:0000269|PubMed:18305173}.
Golgi apparatus, trans-Golgi network membrane
{ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein
{ECO:0000269|PubMed:18305173}. Endosome membrane
{ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein
{ECO:0000269|PubMed:18305173}. Lysosome membrane
{ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein
{ECO:0000269|PubMed:18305173}. Late endosome membrane
{ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein
{ECO:0000269|PubMed:18305173}. Note=The MHC class II complex
transits through a number of intracellular compartments in the
endocytic pathway until it reaches the cell membrane for antigen
presentation.
-!- PTM: Ubiquitinated by MARCH1 and MARCH8 at Lys-254 leading to
sorting into the endosome system and down-regulation of MHC class
II. {ECO:0000305|PubMed:18305173}.
-!- POLYMORPHISM: The following alleles of DRB1-15 are known:
DRB1*15:01, DRB1*15:02, DRB1*15:03, DRB1*15:04, DRB1*15:05,
DRB1*15:06, DRB1*15:07, DRB1*15:08, DRB1*15:09, DRB1*15:10,
DRB1*15:11, DRB1*15:12, DRB1*15:13, DRB1*15:14, DRB1*15:15,
DRB1*15:16, DRB1*15:18, DRB1*15:19, DRB1*15:20, DRB1*15:21,
DRB1*15:22, DRB1*15:23, DRB1*15:24, DRB1*15:25, DRB1*15:26,
DRB1*15:27, DRB1*15:28, DRB1*15:29, DRB1*15:30, DRB1*15:31 and
DRB1*15:32. The sequence shown is that of DRB1*15:01.
-!- MISCELLANEOUS: The chain shown constituted about 70% of a pool of
at least seven similar beta chains.
-!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}.
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EMBL; M20430; AAA59831.1; -; mRNA.
EMBL; AY663395; AAU87979.1; -; Genomic_DNA.
EMBL; AY663406; AAU88008.1; -; Genomic_DNA.
EMBL; AY663411; AAU88023.1; -; Genomic_DNA.
EMBL; AY663414; AAU88033.1; -; Genomic_DNA.
EMBL; AY961072; AAX63460.1; -; mRNA.
EMBL; AY961073; AAX63461.1; -; mRNA.
EMBL; AL713966; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC033827; AAH33827.1; -; mRNA.
EMBL; BC108922; AAI08923.1; -; mRNA.
EMBL; M28584; AAA59681.1; -; mRNA.
EMBL; M16957; AAA36279.1; -; mRNA.
EMBL; M17378; AAA59801.1; -; mRNA.
CCDS; CCDS47409.1; -.
PIR; I68734; HLHUWB.
RefSeq; NP_002115.2; NM_002124.3.
UniGene; Hs.534322; -.
UniGene; Hs.696211; -.
UniGene; Hs.736560; -.
PDB; 1BX2; X-ray; 2.60 A; B/E=32-222.
PDB; 1YMM; X-ray; 3.50 A; B=30-227.
PDB; 2WBJ; X-ray; 3.00 A; B/F=30-227.
PDBsum; 1BX2; -.
PDBsum; 1YMM; -.
PDBsum; 2WBJ; -.
ProteinModelPortal; P01911; -.
SMR; P01911; -.
BioGrid; 109368; 39.
IntAct; P01911; 1.
STRING; 9606.ENSP00000353099; -.
ChEMBL; CHEMBL3831291; -.
iPTMnet; P01911; -.
BioMuta; ATXN1; -.
DMDM; 166214928; -.
PaxDb; P01911; -.
PeptideAtlas; P01911; -.
PRIDE; P01911; -.
DNASU; 3123; -.
Ensembl; ENST00000360004; ENSP00000353099; ENSG00000196126.
GeneID; 3123; -.
CTD; 3123; -.
DisGeNET; 3123; -.
EuPathDB; HostDB:ENSG00000196126.10; -.
GeneCards; HLA-DRB1; -.
HGNC; HGNC:4948; HLA-DRB1.
HPA; CAB015400; -.
HPA; CAB034021; -.
MalaCards; HLA-DRB1; -.
MIM; 142857; gene.
neXtProt; NX_P01911; -.
OpenTargets; ENSG00000196126; -.
PharmGKB; PA35072; -.
eggNOG; ENOG410IWG3; Eukaryota.
eggNOG; ENOG410YI0S; LUCA.
GeneTree; ENSGT00760000118970; -.
HOVERGEN; HBG012730; -.
InParanoid; P01911; -.
PhylomeDB; P01911; -.
Reactome; R-HSA-202424; Downstream TCR signaling.
Reactome; R-HSA-202427; Phosphorylation of CD3 and TCR zeta chains.
Reactome; R-HSA-202430; Translocation of ZAP-70 to Immunological synapse.
Reactome; R-HSA-202433; Generation of second messenger molecules.
Reactome; R-HSA-2132295; MHC class II antigen presentation.
Reactome; R-HSA-389948; PD-1 signaling.
Reactome; R-HSA-877300; Interferon gamma signaling.
ChiTaRS; HLA-DRB1; human.
EvolutionaryTrace; P01911; -.
GeneWiki; HLA-DRB1; -.
GenomeRNAi; 3123; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000196126; -.
CleanEx; HS_HLA-DRB1; -.
ExpressionAtlas; P01911; baseline and differential.
Genevisible; P01911; HS.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
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:0031902; C:late endosome membrane; IDA:UniProtKB.
GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0042613; C:MHC class II protein complex; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome.
GO; GO:0023026; F:MHC class II protein complex binding; IDA:UniProtKB.
GO; GO:0042605; F:peptide antigen binding; IDA:UniProtKB.
GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
GO; GO:0002506; P:polysaccharide assembly with MHC class II protein complex; IDA:UniProtKB.
GO; GO:0031295; P:T cell costimulation; TAS:Reactome.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 3.10.320.10; -; 1.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003006; Ig/MHC_CS.
InterPro; IPR003597; Ig_C1-set.
InterPro; IPR011162; MHC_I/II-like_Ag-recog.
InterPro; IPR014745; MHC_II_a/b_N.
InterPro; IPR000353; MHC_II_b_N.
Pfam; PF07654; C1-set; 1.
Pfam; PF00969; MHC_II_beta; 1.
ProDom; PD000328; MHC_II_b_N; 1.
SMART; SM00407; IGc1; 1.
SMART; SM00921; MHC_II_beta; 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; Cell membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
Endosome; Glycoprotein; Golgi apparatus; Immunity; Isopeptide bond;
Lysosome; Membrane; MHC II; Polymorphism; Reference proteome; Signal;
Transmembrane; Transmembrane helix; Ubl conjugation.
SIGNAL 1 29 {ECO:0000269|PubMed:6600932,
ECO:0000269|PubMed:6947956}.
CHAIN 30 266 HLA class II histocompatibility antigen,
DRB1-15 beta chain.
/FTId=PRO_0000080744.
TOPO_DOM 30 227 Extracellular. {ECO:0000255}.
TRANSMEM 228 248 Helical. {ECO:0000255}.
TOPO_DOM 249 266 Cytoplasmic. {ECO:0000255}.
DOMAIN 126 214 Ig-like C1-type.
REGION 30 124 Beta-1.
REGION 125 227 Beta-2.
CARBOHYD 48 48 N-linked (GlcNAc...) asparagine.
DISULFID 44 108
DISULFID 146 202
CROSSLNK 254 254 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P20039}.
VARIANT 5 5 K -> R (in dbSNP:rs9270305).
/FTId=VAR_050364.
VARIANT 55 55 F -> Y (in dbSNP:rs16822516).
/FTId=VAR_050365.
VARIANT 59 59 Y -> H (in allele DRB1*15:03;
dbSNP:rs11554462).
/FTId=VAR_038162.
VARIANT 96 96 I -> F (in allele DRB1*15:04;
dbSNP:rs17886918).
/FTId=VAR_038163.
VARIANT 106 106 T -> N (in dbSNP:rs9269941).
/FTId=VAR_050366.
VARIANT 115 115 V -> G (in allele DRB1*15:02;
dbSNP:rs17885482).
/FTId=VAR_038164.
VARIANT 164 164 G -> S (in dbSNP:rs1059633).
/FTId=VAR_050367.
VARIANT 169 169 A -> T (in dbSNP:rs2308768).
/FTId=VAR_050368.
VARIANT 262 262 T -> R (in dbSNP:rs9269744).
/FTId=VAR_050370.
CONFLICT 119 119 T -> A (in Ref. 5; AAI08923).
{ECO:0000305}.
CONFLICT 154 154 G -> A (in Ref. 8; AAA59801).
{ECO:0000305}.
CONFLICT 171 171 M -> G (in Ref. 9; AA sequence).
{ECO:0000305}.
CONFLICT 179 180 NG -> D (in Ref. 9; AA sequence).
{ECO:0000305}.
STRAND 36 47 {ECO:0000244|PDB:1BX2}.
TURN 48 51 {ECO:0000244|PDB:1BX2}.
STRAND 52 61 {ECO:0000244|PDB:1BX2}.
STRAND 64 70 {ECO:0000244|PDB:1BX2}.
TURN 71 73 {ECO:0000244|PDB:1BX2}.
STRAND 75 80 {ECO:0000244|PDB:1BX2}.
HELIX 81 83 {ECO:0000244|PDB:1BX2}.
HELIX 84 92 {ECO:0000244|PDB:1BX2}.
HELIX 94 106 {ECO:0000244|PDB:1BX2}.
HELIX 108 115 {ECO:0000244|PDB:1BX2}.
TURN 116 121 {ECO:0000244|PDB:1BX2}.
STRAND 127 134 {ECO:0000244|PDB:1BX2}.
STRAND 142 154 {ECO:0000244|PDB:1BX2}.
STRAND 157 162 {ECO:0000244|PDB:1BX2}.
STRAND 165 167 {ECO:0000244|PDB:1BX2}.
STRAND 169 173 {ECO:0000244|PDB:1BX2}.
STRAND 180 182 {ECO:0000244|PDB:1BX2}.
STRAND 184 192 {ECO:0000244|PDB:1BX2}.
STRAND 199 205 {ECO:0000244|PDB:1BX2}.
STRAND 209 211 {ECO:0000244|PDB:2WBJ}.
STRAND 213 218 {ECO:0000244|PDB:1BX2}.
SEQUENCE 266 AA; 29966 MW; 3B5912820A4654BE CRC64;
MVCLKLPGGS CMTALTVTLM VLSSPLALSG DTRPRFLWQP KRECHFFNGT ERVRFLDRYF
YNQEESVRFD SDVGEFRAVT ELGRPDAEYW NSQKDILEQA RAAVDTYCRH NYGVVESFTV
QRRVQPKVTV YPSKTQPLQH HNLLVCSVSG FYPGSIEVRW FLNGQEEKAG MVSTGLIQNG
DWTFQTLVML ETVPRSGEVY TCQVEHPSVT SPLTVEWRAR SESAQSKMLS GVGGFVLGLL
FLGAGLFIYF RNQKGHSGLQ PTGFLS


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