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T-cell surface glycoprotein CD1a (T-cell surface antigen T6/Leu-6) (hTa1 thymocyte antigen) (CD antigen CD1a)

 CD1A_HUMAN              Reviewed;         327 AA.
P06126; D3DVD7; Q13962; Q5TDJ8; Q9UMM4; Q9Y5M5;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
09-FEB-2010, sequence version 4.
27-SEP-2017, entry version 169.
RecName: Full=T-cell surface glycoprotein CD1a;
AltName: Full=T-cell surface antigen T6/Leu-6;
Short=hTa1 thymocyte antigen;
AltName: CD_antigen=CD1a;
Flags: Precursor;
Name=CD1A;
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 ILE-30 AND TRP-68.
PubMed=2701945;
Aruffo A., Seed B.;
"Expression of cDNA clones encoding the thymocyte antigens CD1a, b, c
demonstrates a hierarchy of exclusion in fibroblasts.";
J. Immunol. 143:1723-1730(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2447586; DOI=10.1073/pnas.84.24.9189;
Martin L.H., Calabi F., Lefebvre F.-A., Bilsland C.A.G., Milstein C.;
"Structure and expression of the human thymocyte antigens CD1a, CD1b,
and CD1c.";
Proc. Natl. Acad. Sci. U.S.A. 84:9189-9193(1987).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Thymus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-108.
PubMed=10488738; DOI=10.1034/j.1399-0039.1999.540202.x;
Han M., Hannick L.I., DiBrino M., Robinson M.A.;
"Polymorphism of human CD1 genes.";
Tissue Antigens 54:122-127(1999).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 21-327.
PubMed=2784820; DOI=10.1111/1523-1747.ep12712175;
Longley J., Kraus J., Alonso M., Edelson R.;
"Molecular cloning of CD1a (T6), a human epidermal dendritic cell
marker related to class I MHC molecules.";
J. Invest. Dermatol. 92:628-631(1989).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 99-327.
TISSUE=T-cell;
PubMed=3093894; DOI=10.1038/323540a0;
Calabi F., Milstein C.;
"A novel family of human major histocompatibility complex-related
genes not mapping to chromosome 6.";
Nature 323:540-543(1986).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 202-294.
PubMed=3097645; DOI=10.1073/pnas.83.23.9154;
Martin L.H., Calabi F., Milstein C.;
"Isolation of CD1 genes: a family of major histocompatibility complex-
related differentiation antigens.";
Proc. Natl. Acad. Sci. U.S.A. 83:9154-9158(1986).
[10]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=11231314; DOI=10.1046/j.1523-1747.2001.01264.x;
Salamero J., Bausinger H., Mommaas A.M., Lipsker D., Proamer F.,
Cazenave J.-P., Goud B., de la Salle H., Hanau D.;
"CD1a molecules traffic through the early recycling endosomal pathway
in human Langerhans cells.";
J. Invest. Dermatol. 116:401-408(2001).
[11]
FUNCTION.
PubMed=16272286; DOI=10.4049/jimmunol.175.10.6344;
Vincent M.S., Xiong X., Grant E.P., Peng W., Brenner M.B.;
"CD1a-, b-, and c-restricted TCRs recognize both self and foreign
antigens.";
J. Immunol. 175:6344-6351(2005).
[12]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CD47, AND TISSUE
SPECIFICITY.
PubMed=18178838; DOI=10.4049/jimmunol.180.2.980;
Sloma I., Zilber M.-T., Vasselon T., Setterblad N., Cavallari M.,
Mori L., De Libero G., Charron D., Mooney N., Gelin C.;
"Regulation of CD1a surface expression and antigen presentation by
invariant chain and lipid rafts.";
J. Immunol. 180:980-987(2008).
[13]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 18-300 IN COMPLEX WITH B2M
AND SULFATIDE SELF-ANTIGEN, IDENTIFICATION BY MASS SPECTROMETRY,
GLYCOSYLATION AT ASN-37; ASN-74 AND ASN-145, AND DISULFIDE BOND.
PubMed=12833155; DOI=10.1038/ni948;
Zajonc D.M., Elsliger M.-A., Teyton L., Wilson I.A.;
"Crystal structure of CD1a in complex with a sulfatide self antigen at
a resolution of 2.15 A.";
Nat. Immunol. 4:808-815(2003).
[14]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-294 IN COMPLEX WITH B2M
AND LIPOPEPTIDE, GLYCOSYLATION AT ASN-37; ASN-74 AND ASN-145, AND
DISULFIDE BOND.
PubMed=15723809; DOI=10.1016/j.immuni.2004.12.009;
Zajonc D.M., Crispin M.D., Bowden T.A., Young D.C., Cheng T.-Y.,
Hu J., Costello C.E., Rudd P.M., Dwek R.A., Miller M.J., Brenner M.B.,
Moody D.B., Wilson I.A.;
"Molecular mechanism of lipopeptide presentation by CD1a.";
Immunity 22:209-219(2005).
[15]
X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 21-295, DISULFIDE BONDS, AND
GLYCOSYLATION AT ASN-74 AND ASN-145.
PubMed=25642819; DOI=10.1038/ni.3098;
Birkinshaw R.W., Pellicci D.G., Cheng T.Y., Keller A.N.,
Sandoval-Romero M., Gras S., de Jong A., Uldrich A.P., Moody D.B.,
Godfrey D.I., Rossjohn J.;
"alphabeta T cell antigen receptor recognition of CD1a presenting self
lipid ligands.";
Nat. Immunol. 16:258-266(2015).
[16]
VARIANTS ILE-30 AND TRP-68, AND SUBCELLULAR LOCATION.
PubMed=11600221; DOI=10.1016/S0198-8859(01)00314-7;
Oteo M., Arribas P., Setien F., Parra J.F., Mirones I.,
Gomez del Moral M., Martinez-Naves E.;
"Structural characterization of two CD1A allelic variants.";
Hum. Immunol. 62:1137-1141(2001).
-!- FUNCTION: Antigen-presenting protein that binds self and non-self
lipid and glycolipid antigens and presents them to T-cell
receptors on natural killer T-cells. {ECO:0000269|PubMed:11231314,
ECO:0000269|PubMed:16272286, ECO:0000269|PubMed:18178838}.
-!- SUBUNIT: Heterodimer with B2M (beta-2-microglobulin). Interacts
with CD74. {ECO:0000269|PubMed:12833155,
ECO:0000269|PubMed:15723809, ECO:0000269|PubMed:18178838}.
-!- INTERACTION:
P61769:B2M; NbExp=2; IntAct=EBI-1036766, EBI-714718;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11231314,
ECO:0000269|PubMed:11600221, ECO:0000269|PubMed:18178838}; Single-
pass type I membrane protein {ECO:0000255}. Membrane raft
{ECO:0000269|PubMed:18178838}; Single-pass type I membrane protein
{ECO:0000255}. Endosome membrane {ECO:0000269|PubMed:11231314};
Single-pass type I membrane protein {ECO:0000255}. Note=Subject to
intracellular trafficking between the cell membrane and endosomes
(PubMed:11231314). Localizes to cell surface lipid rafts
(PubMed:18178838). {ECO:0000269|PubMed:11231314,
ECO:0000269|PubMed:18178838}.
-!- TISSUE SPECIFICITY: Expressed on cortical thymocytes, epidermal
Langerhans cells, dendritic cells, on certain T-cell leukemias,
and in various other tissues. {ECO:0000269|PubMed:11231314,
ECO:0000269|PubMed:18178838}.
-!- MISCELLANEOUS: During protein synthesis and maturation, CD1 family
members bind endogenous lipids that are replaced by lipid or
glycolipid antigens when the proteins are internalized and pass
through endosomes, before trafficking back to the cell surface.
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EMBL; M28825; AAA51931.1; -; mRNA.
EMBL; M22167; AAA51932.1; -; Genomic_DNA.
EMBL; M22080; AAA51932.1; JOINED; Genomic_DNA.
EMBL; M22163; AAA51932.1; JOINED; Genomic_DNA.
EMBL; M22164; AAA51932.1; JOINED; Genomic_DNA.
EMBL; M22165; AAA51932.1; JOINED; Genomic_DNA.
EMBL; M22166; AAA51932.1; JOINED; Genomic_DNA.
EMBL; AK312945; BAG35786.1; -; mRNA.
EMBL; AL121986; CAI10848.1; -; Genomic_DNA.
EMBL; CH471121; EAW52843.1; -; Genomic_DNA.
EMBL; CH471121; EAW52844.1; -; Genomic_DNA.
EMBL; AF142665; AAD37578.1; -; Genomic_DNA.
EMBL; M27735; AAA51933.1; -; mRNA.
EMBL; X04450; CAA28049.1; -; mRNA.
EMBL; M14663; AAA51934.1; -; Genomic_DNA.
CCDS; CCDS1174.1; -.
PIR; A39957; HLHUCD.
RefSeq; NP_001307581.1; NM_001320652.1.
RefSeq; NP_001754.2; NM_001763.2.
UniGene; Hs.1309; -.
PDB; 1ONQ; X-ray; 2.15 A; A/C=18-294.
PDB; 1XZ0; X-ray; 2.80 A; A/C=18-294.
PDB; 4X6C; X-ray; 2.80 A; A/C=21-295.
PDB; 4X6D; X-ray; 2.98 A; A/C=21-295.
PDB; 4X6E; X-ray; 2.10 A; A=21-295.
PDB; 4X6F; X-ray; 1.91 A; A=21-295.
PDB; 5J1A; X-ray; 1.86 A; A=1-295.
PDBsum; 1ONQ; -.
PDBsum; 1XZ0; -.
PDBsum; 4X6C; -.
PDBsum; 4X6D; -.
PDBsum; 4X6E; -.
PDBsum; 4X6F; -.
PDBsum; 5J1A; -.
ProteinModelPortal; P06126; -.
SMR; P06126; -.
BioGrid; 107347; 42.
IntAct; P06126; 4.
MINT; MINT-4655994; -.
STRING; 9606.ENSP00000289429; -.
DrugBank; DB00098; Anti-thymocyte Globulin (Rabbit).
iPTMnet; P06126; -.
PhosphoSitePlus; P06126; -.
SwissPalm; P06126; -.
BioMuta; CD1A; -.
DMDM; 288558852; -.
MaxQB; P06126; -.
PaxDb; P06126; -.
PeptideAtlas; P06126; -.
PRIDE; P06126; -.
DNASU; 909; -.
Ensembl; ENST00000289429; ENSP00000289429; ENSG00000158477.
GeneID; 909; -.
KEGG; hsa:909; -.
UCSC; uc001frt.4; human.
CTD; 909; -.
DisGeNET; 909; -.
EuPathDB; HostDB:ENSG00000158477.6; -.
GeneCards; CD1A; -.
H-InvDB; HIX0001190; -.
HGNC; HGNC:1634; CD1A.
HPA; CAB000009; -.
HPA; HPA010734; -.
MIM; 188370; gene.
neXtProt; NX_P06126; -.
OpenTargets; ENSG00000158477; -.
PharmGKB; PA26193; -.
eggNOG; ENOG410JACG; Eukaryota.
eggNOG; ENOG41113WA; LUCA.
GeneTree; ENSGT00480000042665; -.
HOGENOM; HOG000111666; -.
HOVERGEN; HBG004453; -.
InParanoid; P06126; -.
KO; K06448; -.
OMA; NDITHNL; -.
OrthoDB; EOG091G0DB3; -.
PhylomeDB; P06126; -.
TreeFam; TF336723; -.
Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
EvolutionaryTrace; P06126; -.
GeneWiki; CD1A; -.
GenomeRNAi; 909; -.
PRO; PR:P06126; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000158477; -.
CleanEx; HS_CD1A; -.
Genevisible; P06126; HS.
GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0030881; F:beta-2-microglobulin binding; IBA:GO_Central.
GO; GO:0030883; F:endogenous lipid antigen binding; IBA:GO_Central.
GO; GO:0030884; F:exogenous lipid antigen binding; IBA:GO_Central.
GO; GO:0071723; F:lipopeptide binding; IBA:GO_Central.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0048007; P:antigen processing and presentation, exogenous lipid antigen via MHC class Ib; IBA:GO_Central.
GO; GO:0006955; P:immune response; NAS:UniProtKB.
GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 3.30.500.10; -; 1.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003597; Ig_C1-set.
InterPro; IPR011161; MHC_I-like_Ag-recog.
InterPro; IPR011162; MHC_I/II-like_Ag-recog.
Pfam; PF07654; C1-set; 1.
Pfam; PF16497; MHC_I_3; 1.
SMART; SM00407; IGc1; 1.
SUPFAM; SSF48726; SSF48726; 1.
SUPFAM; SSF54452; SSF54452; 1.
PROSITE; PS50835; IG_LIKE; 1.
1: Evidence at protein level;
3D-structure; Adaptive immunity; Cell membrane; Complete proteome;
Disulfide bond; Endosome; Glycoprotein; Immunity;
Immunoglobulin domain; Membrane; Polymorphism; Reference proteome;
Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 16
CHAIN 17 327 T-cell surface glycoprotein CD1a.
/FTId=PRO_0000014578.
TOPO_DOM 17 300 Extracellular. {ECO:0000255}.
TRANSMEM 301 321 Helical. {ECO:0000255}.
TOPO_DOM 322 327 Cytoplasmic. {ECO:0000255}.
DOMAIN 184 291 Ig-like.
REGION 90 94 Glycolipid binding.
{ECO:0000244|PDB:1ONQ,
ECO:0000269|PubMed:12833155}.
BINDING 171 171 Glycolipid. {ECO:0000244|PDB:1ONQ,
ECO:0000269|PubMed:12833155}.
BINDING 175 175 Glycolipid. {ECO:0000244|PDB:1ONQ,
ECO:0000269|PubMed:12833155}.
CARBOHYD 37 37 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12833155,
ECO:0000269|PubMed:15723809}.
CARBOHYD 60 60 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 74 74 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12833155,
ECO:0000269|PubMed:15723809,
ECO:0000269|PubMed:25642819}.
CARBOHYD 145 145 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12833155,
ECO:0000269|PubMed:15723809,
ECO:0000269|PubMed:25642819}.
DISULFID 119 183 {ECO:0000244|PDB:4X6C,
ECO:0000269|PubMed:25642819}.
DISULFID 223 278 {ECO:0000244|PDB:1ONQ,
ECO:0000244|PDB:1XZ0,
ECO:0000244|PDB:4X6C,
ECO:0000269|PubMed:12833155,
ECO:0000269|PubMed:15723809,
ECO:0000269|PubMed:25642819}.
VARIANT 22 22 K -> N (in dbSNP:rs3087217).
/FTId=VAR_062522.
VARIANT 30 30 T -> I (in dbSNP:rs2269714).
{ECO:0000269|PubMed:11600221,
ECO:0000269|PubMed:2701945}.
/FTId=VAR_010209.
VARIANT 68 68 C -> W (in dbSNP:rs2269715).
{ECO:0000269|PubMed:11600221,
ECO:0000269|PubMed:2701945}.
/FTId=VAR_010210.
CONFLICT 70 71 WS -> V (in Ref. 7; AAA51933).
{ECO:0000305}.
STRAND 27 37 {ECO:0000244|PDB:5J1A}.
STRAND 40 49 {ECO:0000244|PDB:5J1A}.
STRAND 52 58 {ECO:0000244|PDB:5J1A}.
TURN 59 62 {ECO:0000244|PDB:5J1A}.
STRAND 63 68 {ECO:0000244|PDB:5J1A}.
HELIX 69 72 {ECO:0000244|PDB:5J1A}.
HELIX 77 101 {ECO:0000244|PDB:5J1A}.
TURN 102 106 {ECO:0000244|PDB:5J1A}.
STRAND 109 119 {ECO:0000244|PDB:5J1A}.
STRAND 129 135 {ECO:0000244|PDB:5J1A}.
STRAND 138 144 {ECO:0000244|PDB:5J1A}.
STRAND 147 150 {ECO:0000244|PDB:5J1A}.
HELIX 152 154 {ECO:0000244|PDB:5J1A}.
HELIX 155 165 {ECO:0000244|PDB:5J1A}.
HELIX 169 180 {ECO:0000244|PDB:5J1A}.
HELIX 182 191 {ECO:0000244|PDB:5J1A}.
TURN 192 194 {ECO:0000244|PDB:5J1A}.
HELIX 195 198 {ECO:0000244|PDB:5J1A}.
STRAND 205 210 {ECO:0000244|PDB:5J1A}.
STRAND 218 231 {ECO:0000244|PDB:5J1A}.
STRAND 234 239 {ECO:0000244|PDB:5J1A}.
STRAND 248 254 {ECO:0000244|PDB:4X6C}.
STRAND 260 269 {ECO:0000244|PDB:5J1A}.
HELIX 270 272 {ECO:0000244|PDB:5J1A}.
STRAND 276 281 {ECO:0000244|PDB:5J1A}.
HELIX 283 285 {ECO:0000244|PDB:5J1A}.
STRAND 290 294 {ECO:0000244|PDB:5J1A}.
SEQUENCE 327 AA; 37077 MW; C575C3C538F0AA29 CRC64;
MLFLLLPLLA VLPGDGNADG LKEPLSFHVT WIASFYNHSW KQNLVSGWLS DLQTHTWDSN
SSTIVFLCPW SRGNFSNEEW KELETLFRIR TIRSFEGIRR YAHELQFEYP FEIQVTGGCE
LHSGKVSGSF LQLAYQGSDF VSFQNNSWLP YPVAGNMAKH FCKVLNQNQH ENDITHNLLS
DTCPRFILGL LDAGKAHLQR QVKPEAWLSH GPSPGPGHLQ LVCHVSGFYP KPVWVMWMRG
EQEQQGTQRG DILPSADGTW YLRATLEVAA GEAADLSCRV KHSSLEGQDI VLYWEHHSSV
GFIILAVIVP LLLLIGLALW FRKRCFC


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