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HLA class I histocompatibility antigen, A-68 alpha chain (Aw-68) (HLA class I histocompatibility antigen, A-28 alpha chain) (MHC class I antigen A*68)

 1A68_HUMAN              Reviewed;         365 AA.
P01891; O19673; O19695; O19794; O19795; O43907; O77938; O98010;
P10315; P79505; Q9MYA5; Q9MYC4; Q9TQG7; Q9TQN5; Q9UIN2;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-FEB-2001, sequence version 4.
23-MAY-2018, entry version 177.
RecName: Full=HLA class I histocompatibility antigen, A-68 alpha chain;
AltName: Full=Aw-68;
AltName: Full=HLA class I histocompatibility antigen, A-28 alpha chain;
AltName: Full=MHC class I antigen A*68;
Flags: Precursor;
Name=HLA-A; Synonyms=HLAA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE (ALLELE A*68:02).
PubMed=3496393;
Holmes N., Ennis P., Wan A.M., Denney D.W., Parham P.;
"Multiple genetic mechanisms have contributed to the generation of the
HLA-A2/A28 family of class I MHC molecules.";
J. Immunol. 139:936-941(1987).
[2]
NUCLEOTIDE SEQUENCE (ALLELE A*68:02).
Domena J.D.;
Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*68:03).
PubMed=8881043; DOI=10.1007/s002510050172;
Ellexson M., Lau M., Terasaki P., Hildebrand W.H.;
"Molecular characterization of HLA-A*6803.";
Immunogenetics 45:78-79(1996).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*68:08).
PubMed=10395114; DOI=10.1034/j.1399-0039.1999.530614.x;
Cox S.T., Arguello J.R., Marsh S.G.E., Boham E., Lau M., Kwan P.L.,
Madrigal J.A., Little A.-M.;
"Sequence of HLA-A*6808.";
Tissue Antigens 53:597-600(1999).
[5]
NUCLEOTIDE SEQUENCE (ALLELE A*68:011).
TISSUE=Blood;
Cox S.T.;
"Confirmation of HLA-A*68011.";
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*68:17).
PubMed=10885567; DOI=10.1034/j.1399-0039.2000.550509.x;
Ramon D., Scott I., Cox S.T., Pesoa S., Vullo C., Little A.-M.,
Madrigal J.A.;
"HLA-A*6817, identified in the Kolla Amerindians of north-west
Argentina possesses a novel nucleotide substitution.";
Tissue Antigens 55:453-454(2000).
[7]
NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*68:06).
Bei M., Hurley C.K.;
Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELE A*68:03).
TISSUE=Blood;
PubMed=9271640; DOI=10.1007/s002510050304;
Vargas-Alarcon G., Martinez-Laso J., Gomez-Casado E., Perez-Blas M.,
Granados J., Alegre R., Alvarez M., Zuniga J., Arnaiz-Villena A.;
"Description of HLA-A*6803 and A*68N in Mazatecan Indians from
Mexico.";
Immunogenetics 46:446-447(1997).
[9]
NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*68:03).
TISSUE=Blood;
Blasczyk R.;
Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*68:02).
Edson S.M., Hurley C.K.;
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE OF 26-206 (ALLELES A*68:09 AND A*68:10).
PubMed=10852390; DOI=10.1034/j.1399-0039.2000.550412.x;
Ellis J., Steiner N.K., Kosman C., Henson V., Mitton W., Koester R.,
Ng J., Hartzman R.J., Hurley C.K.;
"Seventeen more novel HLA-A locus alleles.";
Tissue Antigens 55:369-373(2000).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-206 (ALLELE A*68:16).
PubMed=10803837; DOI=10.1007/s002510050618;
Gomez-Casado E., Martinez-Laso J., Gonzalez-Hevilla M., Longas J.,
Rubio I., Silvera-Redondo C., Garcia-Gomez A., Lowy E.,
Arnaiz-Villena A.;
"A novel HLA-A*6816 allele possible generated by a point mutation in a
Chilean from Punta Arenas (Magellan Strait).";
Immunogenetics 51:257-260(2000).
[13]
NUCLEOTIDE SEQUENCE OF 26-206 (ALLELES A*68:07 AND A*68:17).
PubMed=11260503; DOI=10.1034/j.1399-0039.2001.057002095.x;
Hickman H.D., Cavett J.W., Ellexson-Turner M.E., Sparkman J.N.,
Bennett T.T., Turner S., Sidebottom D.A., Trachtenberg E.A.,
Confer D.L., Hildebrand W.H.;
"Non-conservative substitutions distinguish previously uncharacterized
HLA-A molecules.";
Tissue Antigens 57:95-102(2001).
[14]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-297 (ALLELE A*68:01).
PubMed=3877632;
Holmes N., Parham P.;
"Exon shuffling in vivo can generate novel HLA class I molecules.";
EMBO J. 4:2849-2854(1985).
[15]
PROTEIN SEQUENCE OF 25-294 (A*68:01).
PubMed=6179086; DOI=10.1073/pnas.79.12.3813;
Lopez de Castro J.A., Strominger J.L., Strong D.M., Orr H.T.;
"Structure of crossreactive human histocompatibility antigens HLA-A28
and HLA-A2: possible implications for the generation of HLA
polymorphism.";
Proc. Natl. Acad. Sci. U.S.A. 79:3813-3817(1982).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[18]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-110.
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).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356 AND SER-359, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350; SER-352; SER-356
AND SER-359, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[23]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 25-294 (A*68:01).
PubMed=1448153; DOI=10.1038/360364a0;
Guo H.-C., Jardetzky T.S., Garrett T.P.J., Lane W.S., Strominger J.L.,
Wiley D.C.;
"Different length peptides bind to HLA-Aw68 similarly at their ends
but bulge out in the middle.";
Nature 360:364-366(1992).
[24]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 25-294 (A*68:01).
PubMed=1448154; DOI=10.1038/360367a0;
Silver M.L., Guo H.-C., Strominger J.L., Wiley D.C.;
"Atomic structure of a human MHC molecule presenting an influenza
virus peptide.";
Nature 360:367-369(1992).
[25]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 25-199 (A*68:01).
PubMed=7862664; DOI=10.1073/pnas.92.4.1218;
Collins E.J., Garboczi D.N., Karpusas M.N., Wiley D.C.;
"The three-dimensional structure of a class I major histocompatibility
complex molecule missing the alpha 3 domain of the heavy chain.";
Proc. Natl. Acad. Sci. U.S.A. 92:1218-1221(1995).
-!- FUNCTION: Involved in the presentation of foreign antigens to the
immune system.
-!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2-
microglobulin). Interacts with human herpesvirus 8 MIR1 protein
(By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- PTM: Polyubiquitinated in a post ER compartment by interaction
with human herpesvirus 8 MIR1 protein. This targets the protein
for rapid degradation via the ubiquitin system (By similarity).
{ECO:0000250}.
-!- POLYMORPHISM: The following alleles of A-68 are known: A*68:01
(Aw68.1), A*68:02, A*68:03. A*68:04, A*68:05, A*68:06, A*68:07,
A*68:08, A*68:09, A*68:10, A*68:16 and A*68:17. The sequence shown
is that of A*68:01. {ECO:0000305}.
-!- SIMILARITY: Belongs to the MHC class I family. {ECO:0000305}.
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EMBL; U03861; AAA03602.1; -; mRNA.
EMBL; X03070; CAB56605.1; -; Genomic_DNA.
EMBL; X03071; CAB56606.1; -; Genomic_DNA.
EMBL; U41057; AAB41292.1; -; mRNA.
EMBL; AJ315642; CAC44382.1; -; Genomic_DNA.
EMBL; AF144013; AAF74211.1; -; Genomic_DNA.
EMBL; AJ245567; CAB59722.1; -; Genomic_DNA.
EMBL; AH005127; AAB50567.1; -; Genomic_DNA.
EMBL; U89946; AAB82079.1; -; Genomic_DNA.
EMBL; U89947; AAB82080.1; -; Genomic_DNA.
EMBL; AJ001274; CAA04647.1; -; mRNA.
EMBL; AH006296; AAC25782.1; -; Genomic_DNA.
EMBL; AH007538; AAD22270.1; -; Genomic_DNA.
EMBL; AH007605; AAD27539.1; -; Genomic_DNA.
EMBL; AJ223972; CAA11708.1; -; Genomic_DNA.
EMBL; AH007201; AAD02208.1; -; Genomic_DNA.
EMBL; AH009406; AAF73477.1; -; Genomic_DNA.
PIR; A02187; HLHU28.
PIR; A24671; HLHUAW.
PIR; I38441; I38441.
UniGene; Hs.181244; -.
UniGene; Hs.713441; -.
PDB; 1HSB; X-ray; 1.90 A; A=25-294.
PDB; 1TMC; X-ray; 2.30 A; A=25-199.
PDB; 2HLA; X-ray; 2.60 A; A=25-294.
PDB; 4HWZ; X-ray; 2.40 A; A=25-298.
PDB; 4HX1; X-ray; 1.80 A; A=25-296.
PDB; 4I48; X-ray; 2.80 A; A=25-296.
PDB; 6EI2; X-ray; 1.61 A; A=25-299.
PDBsum; 1HSB; -.
PDBsum; 1TMC; -.
PDBsum; 2HLA; -.
PDBsum; 4HWZ; -.
PDBsum; 4HX1; -.
PDBsum; 4I48; -.
PDBsum; 6EI2; -.
ProteinModelPortal; P01891; -.
SMR; P01891; -.
IntAct; P01891; 7.
MINT; P01891; -.
iPTMnet; P01891; -.
SwissPalm; P01891; -.
DMDM; 13124681; -.
EPD; P01891; -.
MaxQB; P01891; -.
PeptideAtlas; P01891; -.
PRIDE; P01891; -.
Ensembl; ENST00000457879; ENSP00000403575; ENSG00000235657.
DisGeNET; 3105; -.
GeneCards; HLA-A; -.
HGNC; HGNC:4931; HLA-A.
MalaCards; HLA-A; -.
MIM; 142800; gene.
neXtProt; NX_P01891; -.
HOVERGEN; HBG016709; -.
InParanoid; P01891; -.
PhylomeDB; P01891; -.
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.
ChiTaRS; HLA-A; human.
EvolutionaryTrace; P01891; -.
Proteomes; UP000005640; Chromosome 6.
CleanEx; HS_HLA-A; -.
GO; GO:0009986; C:cell surface; ISS:UniProtKB.
GO; GO:0031901; C:early endosome membrane; TAS:Reactome.
GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome.
GO; GO:0005794; C:Golgi apparatus; ISS: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:0042612; C:MHC class I protein complex; ISS:UniProtKB.
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:0030881; F:beta-2-microglobulin binding; IMP:UniProtKB.
GO; GO:0042605; F:peptide antigen binding; IMP:UniProtKB.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
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:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
GO; GO:0060337; P:type I interferon signaling pathway; TAS:Reactome.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
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.
InterPro; IPR010579; MHC_I_a_C.
Pfam; PF07654; C1-set; 1.
Pfam; PF00129; MHC_I; 1.
Pfam; PF06623; MHC_I_C; 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; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycoprotein; Host-virus interaction; Immunity;
Membrane; MHC I; Phosphoprotein; Polymorphism; Reference proteome;
Signal; Transmembrane; Transmembrane helix; Ubl conjugation.
SIGNAL 1 24 {ECO:0000269|PubMed:6179086}.
CHAIN 25 365 HLA class I histocompatibility antigen,
A-68 alpha chain.
/FTId=PRO_0000018830.
TOPO_DOM 25 308 Extracellular. {ECO:0000255}.
TRANSMEM 309 332 Helical. {ECO:0000255}.
TOPO_DOM 333 365 Cytoplasmic. {ECO:0000255}.
DOMAIN 209 295 Ig-like C1-type.
REGION 25 114 Alpha-1.
REGION 115 206 Alpha-2.
REGION 207 298 Alpha-3.
REGION 299 308 Connecting peptide.
MOD_RES 343 343 Phosphoserine.
{ECO:0000250|UniProtKB:P18462}.
MOD_RES 344 344 Phosphotyrosine.
{ECO:0000250|UniProtKB:P18462}.
MOD_RES 345 345 Phosphoserine.
{ECO:0000250|UniProtKB:P18462}.
MOD_RES 349 349 Phosphoserine.
{ECO:0000250|UniProtKB:P18462}.
MOD_RES 350 350 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 352 352 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 356 356 Phosphoserine.
{ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 359 359 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
CARBOHYD 110 110 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
DISULFID 125 188
DISULFID 227 283
VARIANT 36 36 V -> M (in allele A*68:02).
{ECO:0000269|PubMed:3496393,
ECO:0000269|Ref.10, ECO:0000269|Ref.2}.
/FTId=VAR_004389.
VARIANT 86 87 RN -> EE (in allele A*68:10).
{ECO:0000269|PubMed:10852390}.
/FTId=VAR_010362.
VARIANT 89 89 R -> G (in dbSNP:rs199474430).
/FTId=VAR_056304.
VARIANT 94 94 Q -> H (in allele A*68:03, allele A*68:04
and allele A*68:05; dbSNP:rs78306866).
{ECO:0000269|PubMed:8881043,
ECO:0000269|PubMed:9271640,
ECO:0000269|Ref.9}.
/FTId=VAR_010363.
VARIANT 97 97 T -> I (in allele A*68:04).
/FTId=VAR_010364.
VARIANT 98 98 D -> H (in allele A*68:05).
/FTId=VAR_010365.
VARIANT 101 101 D -> N (in dbSNP:rs1136688).
/FTId=VAR_056305.
VARIANT 121 121 M -> R (in allele A*68:02).
{ECO:0000269|PubMed:3496393,
ECO:0000269|Ref.10, ECO:0000269|Ref.2}.
/FTId=VAR_004390.
VARIANT 129 129 S -> P (in allele A*68:02;
dbSNP:rs1136700).
{ECO:0000269|PubMed:3496393,
ECO:0000269|Ref.10, ECO:0000269|Ref.2}.
/FTId=VAR_004391.
VARIANT 133 133 F -> L (in dbSNP:rs1059488).
/FTId=VAR_056306.
VARIANT 138 138 R -> E (in allele A*68:06; requires 2
nucleotide substitutions).
{ECO:0000269|PubMed:10852390}.
/FTId=VAR_010366.
VARIANT 138 138 R -> H (in allele A*68:02).
{ECO:0000269|PubMed:3496393,
ECO:0000269|Ref.10, ECO:0000269|Ref.2}.
/FTId=VAR_004392.
VARIANT 140 140 D -> H (in allele A*68:06 and allele
A*68:07). {ECO:0000269|PubMed:10885567}.
/FTId=VAR_010367.
VARIANT 140 140 D -> V (in allele A*68:17).
{ECO:0000269|PubMed:10885567,
ECO:0000269|PubMed:11260503}.
/FTId=VAR_010368.
VARIANT 140 140 D -> Y (in allele A*68:02).
{ECO:0000269|PubMed:3496393,
ECO:0000269|Ref.10, ECO:0000269|Ref.2}.
/FTId=VAR_004393.
VARIANT 175 175 H -> L (in allele A*68:16).
{ECO:0000269|PubMed:10803837}.
/FTId=VAR_010369.
VARIANT 180 180 W -> L (in allele A*68:08).
{ECO:0000269|PubMed:10395114}.
/FTId=VAR_010370.
VARIANT 180 180 W -> Q (in allele A*68:09; requires 2
nucleotide substitutions).
/FTId=VAR_010371.
CONFLICT 206 206 T -> A (in Ref. 12; AAF74211).
{ECO:0000305}.
CONFLICT 231 231 S -> G (in Ref. 15; AA sequence).
{ECO:0000305}.
STRAND 27 36 {ECO:0000244|PDB:6EI2}.
STRAND 41 43 {ECO:0000244|PDB:4HX1}.
STRAND 45 52 {ECO:0000244|PDB:6EI2}.
STRAND 55 61 {ECO:0000244|PDB:6EI2}.
STRAND 64 66 {ECO:0000244|PDB:6EI2}.
HELIX 74 76 {ECO:0000244|PDB:6EI2}.
HELIX 81 108 {ECO:0000244|PDB:6EI2}.
STRAND 113 115 {ECO:0000244|PDB:1TMC}.
STRAND 118 127 {ECO:0000244|PDB:6EI2}.
STRAND 133 142 {ECO:0000244|PDB:6EI2}.
STRAND 145 150 {ECO:0000244|PDB:6EI2}.
STRAND 157 159 {ECO:0000244|PDB:6EI2}.
HELIX 162 173 {ECO:0000244|PDB:6EI2}.
HELIX 176 185 {ECO:0000244|PDB:6EI2}.
HELIX 187 198 {ECO:0000244|PDB:6EI2}.
HELIX 200 203 {ECO:0000244|PDB:6EI2}.
STRAND 210 235 {ECO:0000244|PDB:6EI2}.
STRAND 238 243 {ECO:0000244|PDB:6EI2}.
STRAND 246 248 {ECO:0000244|PDB:6EI2}.
STRAND 252 254 {ECO:0000244|PDB:6EI2}.
STRAND 261 263 {ECO:0000244|PDB:6EI2}.
STRAND 265 274 {ECO:0000244|PDB:6EI2}.
HELIX 278 280 {ECO:0000244|PDB:6EI2}.
STRAND 281 286 {ECO:0000244|PDB:6EI2}.
STRAND 290 292 {ECO:0000244|PDB:1HSB}.
STRAND 294 296 {ECO:0000244|PDB:6EI2}.
SEQUENCE 365 AA; 40909 MW; 78539C59DB8B1DFC CRC64;
MAVMAPRTLV LLLSGALALT QTWAGSHSMR YFYTSVSRPG RGEPRFIAVG YVDDTQFVRF
DSDAASQRME PRAPWIEQEG PEYWDRNTRN VKAQSQTDRV DLGTLRGYYN QSEAGSHTIQ
MMYGCDVGSD GRFLRGYRQD AYDGKDYIAL KEDLRSWTAA DMAAQTTKHK WEAAHVAEQW
RAYLEGTCVE WLRRYLENGK ETLQRTDAPK THMTHHAVSD HEATLRCWAL SFYPAEITLT
WQRDGEDQTQ DTELVETRPA GDGTFQKWVA VVVPSGQEQR YTCHVQHEGL PKPLTLRWEP
SSQPTIPIVG IIAGLVLFGA VITGAVVAAV MWRRKSSDRK GGSYSQAASS DSAQGSDVSL
TACKV


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