CD1B_HUMAN
ID CD1B_HUMAN Reviewed; 333 AA.
AC P29016; Q5TDK9; Q5TDL0; Q9UMM2;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=T-cell surface glycoprotein CD1b;
DE AltName: CD_antigen=CD1b;
DE Flags: Precursor;
GN Name=CD1B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2447586; DOI=10.1073/pnas.84.24.9189;
RA Martin L.H., Calabi F., Lefebvre F.-A., Bilsland C.A.G., Milstein C.;
RT "Structure and expression of the human thymocyte antigens CD1a, CD1b, and
RT CD1c.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:9189-9193(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2701945;
RA Aruffo A., Seed B.;
RT "Expression of cDNA clones encoding the thymocyte antigens CD1a, b, c
RT demonstrates a hierarchy of exclusion in fibroblasts.";
RL J. Immunol. 143:1723-1730(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 203-295.
RX PubMed=3097645; DOI=10.1073/pnas.83.23.9154;
RA Martin L.H., Calabi F., Milstein C.;
RT "Isolation of CD1 genes: a family of major histocompatibility complex-
RT related differentiation antigens.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:9154-9158(1986).
RN [6]
RP FUNCTION, MUTAGENESIS OF 329-TYR-GLN-330, AND SUBCELLULAR LOCATION.
RX PubMed=10981968; DOI=10.1016/s1074-7613(00)00025-x;
RA Shamshiev A., Donda A., Prigozy T.I., Mori L., Chigorno V., Benedict C.A.,
RA Kappos L., Sonnino S., Kronenberg M., De Libero G.;
RT "The alphabeta T cell response to self-glycolipids shows a novel mechanism
RT of CD1b loading and a requirement for complex oligosaccharides.";
RL Immunity 13:255-264(2000).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=10899914; DOI=10.1084/jem.192.2.281;
RA Briken V., Jackman R.M., Watts G.F.M., Rogers R.A., Porcelli S.A.;
RT "Human CD1b and CD1c isoforms survey different intracellular compartments
RT for the presentation of microbial lipid antigens.";
RL J. Exp. Med. 192:281-288(2000).
RN [8]
RP FUNCTION, INTERACTION WITH SAPOSIN C, AND SUBCELLULAR LOCATION.
RX PubMed=14716313; DOI=10.1038/ni1035;
RA Winau F., Schwierzeck V., Hurwitz R., Remmel N., Sieling P.A., Modlin R.L.,
RA Porcelli S.A., Brinkmann V., Sugita M., Sandhoff K., Kaufmann S.H.E.,
RA Schaible U.E.;
RT "Saposin C is required for lipid presentation by human CD1b.";
RL Nat. Immunol. 5:169-174(2004).
RN [9]
RP ERRATUM OF PUBMED:14716313.
RA Winau F., Schwierzeck V., Hurwitz R., Remmel N., Sieling P.A., Modlin R.L.,
RA Porcelli S.A., Brinkmann V., Sugita M., Sandhoff K., Kaufmann S.H.E.,
RA Schaible U.E.;
RL Nat. Immunol. 5:344-344(2004).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-75.
RC TISSUE=Leukemic T-cell;
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 18-295 IN COMPLEXES WITH B2M;
RP GANGLIOSIDE GM2 AND PHOSPHATIDYLINOSITOL, AND DISULFIDE BONDS.
RX PubMed=12118248; DOI=10.1038/ni821;
RA Gadola S.D., Zaccai N.R., Harlos K., Shepherd D., Castro-Palomino J.C.,
RA Ritter G., Schmidt R.R., Jones E.Y., Cerundolo V.;
RT "Structure of human CD1b with bound ligands at 2.3 A, a maze for alkyl
RT chains.";
RL Nat. Immunol. 3:721-726(2002).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 18-295 IN COMPLEX WITH B2M AND
RP GLUCOSE MONOMYCOLATE, AND DISULFIDE BONDS.
RX PubMed=14764708; DOI=10.4049/jimmunol.172.4.2382;
RA Batuwangala T., Shepherd D., Gadola S.D., Gibson K.J.C., Zaccai N.R.,
RA Fersht A.R., Besra G.S., Cerundolo V., Jones E.Y.;
RT "The crystal structure of human CD1b with a bound bacterial glycolipid.";
RL J. Immunol. 172:2382-2388(2004).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 19-298 IN COMPLEX WITH B2M;
RP PHOSPHATIDYLCHOLINE AND SPACER LIGAND, GLYCOSYLATION AT ASN-38 AND ASN-75,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND DISULFIDE BONDS.
RX PubMed=16874306; DOI=10.1038/sj.emboj.7601244;
RA Garcia-Alles L.F., Versluis K., Maveyraud L., Vallina A.T., Sansano S.,
RA Bello N.F., Gober H.-J., Guillet V., de la Salle H., Puzo G., Mori L.,
RA Heck A.J.R., De Libero G., Mourey L.;
RT "Endogenous phosphatidylcholine and a long spacer ligand stabilize the
RT lipid-binding groove of CD1b.";
RL EMBO J. 25:3684-3692(2006).
CC -!- FUNCTION: Antigen-presenting protein that binds self and non-self lipid
CC and glycolipid antigens and presents them to T-cell receptors on
CC natural killer T-cells. {ECO:0000269|PubMed:10981968,
CC ECO:0000269|PubMed:14716313}.
CC -!- SUBUNIT: Heterodimer with B2M (beta-2-microglobulin). Interacts with
CC saposin C. {ECO:0000269|PubMed:14716313, ECO:0000269|PubMed:14764708,
CC ECO:0000269|PubMed:16874306}.
CC -!- INTERACTION:
CC P29016; P61769: B2M; NbExp=4; IntAct=EBI-1033762, EBI-714718;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10899914,
CC ECO:0000269|PubMed:10981968, ECO:0000269|PubMed:14716313}; Single-pass
CC type I membrane protein {ECO:0000255}. Endosome membrane
CC {ECO:0000269|PubMed:10899914, ECO:0000269|PubMed:14716313}; Single-pass
CC type I membrane protein {ECO:0000255}. Lysosome membrane
CC {ECO:0000269|PubMed:10899914, ECO:0000269|PubMed:10981968,
CC ECO:0000269|PubMed:14716313}; Single-pass type I membrane protein
CC {ECO:0000255}. Note=Subject to intracellular trafficking between the
CC cell membrane, endosomes and lysosomes. {ECO:0000269|PubMed:10899914,
CC ECO:0000269|PubMed:10981968, ECO:0000269|PubMed:14716313}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P29016-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P29016-2; Sequence=VSP_016911;
CC -!- TISSUE SPECIFICITY: Expressed on cortical thymocytes, on certain T-cell
CC leukemias, and in various other tissues.
CC -!- MISCELLANEOUS: During protein synthesis and maturation, CD1 family
CC members bind endogenous lipids that are replaced by lipid or glycolipid
CC antigens when the proteins are internalized and pass through endosomes
CC or lysosomes, before trafficking back to the cell surface. Interaction
CC with saposin C is required for the loading of bacterial lipid antigens
CC onto CD1B in the lysosome.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M22173; AAA51940.1; -; Genomic_DNA.
DR EMBL; M22168; AAA51940.1; JOINED; Genomic_DNA.
DR EMBL; M22169; AAA51940.1; JOINED; Genomic_DNA.
DR EMBL; M22170; AAA51940.1; JOINED; Genomic_DNA.
DR EMBL; M22171; AAA51940.1; JOINED; Genomic_DNA.
DR EMBL; M22172; AAA51940.1; JOINED; Genomic_DNA.
DR EMBL; M28826; AAA51939.1; -; mRNA.
DR EMBL; AL121986; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC069481; AAH69481.1; -; mRNA.
DR EMBL; BC074747; AAH74747.1; -; mRNA.
DR EMBL; BC104216; AAI04217.1; -; mRNA.
DR EMBL; BC104217; AAI04218.1; -; mRNA.
DR EMBL; M14665; AAA51936.1; -; Genomic_DNA.
DR CCDS; CCDS1176.1; -. [P29016-1]
DR PIR; B39957; HLHUCB.
DR RefSeq; NP_001755.1; NM_001764.2. [P29016-1]
DR RefSeq; XP_011508421.1; XM_011510119.2. [P29016-2]
DR PDB; 1GZP; X-ray; 2.80 A; A=18-295.
DR PDB; 1GZQ; X-ray; 2.26 A; A=18-295.
DR PDB; 1UQS; X-ray; 3.10 A; A=18-295.
DR PDB; 2H26; X-ray; 1.80 A; A=19-298.
DR PDB; 3OV6; X-ray; 2.50 A; A=166-295.
DR PDB; 3T8X; X-ray; 1.90 A; A/C=19-298.
DR PDB; 4ONO; X-ray; 2.70 A; A=201-295.
DR PDB; 5C9J; X-ray; 2.40 A; A=203-295.
DR PDB; 5L2J; X-ray; 1.65 A; A=20-296.
DR PDB; 5L2K; X-ray; 3.20 A; A=20-296.
DR PDB; 5WKE; X-ray; 1.69 A; A=20-296.
DR PDB; 5WKG; X-ray; 2.06 A; A=20-296.
DR PDB; 5WKI; X-ray; 2.75 A; A=20-296.
DR PDB; 5WL1; X-ray; 1.38 A; A=20-296.
DR PDB; 6CUG; X-ray; 2.40 A; A=20-296.
DR PDB; 6D64; X-ray; 1.70 A; A=20-296.
DR PDBsum; 1GZP; -.
DR PDBsum; 1GZQ; -.
DR PDBsum; 1UQS; -.
DR PDBsum; 2H26; -.
DR PDBsum; 3OV6; -.
DR PDBsum; 3T8X; -.
DR PDBsum; 4ONO; -.
DR PDBsum; 5C9J; -.
DR PDBsum; 5L2J; -.
DR PDBsum; 5L2K; -.
DR PDBsum; 5WKE; -.
DR PDBsum; 5WKG; -.
DR PDBsum; 5WKI; -.
DR PDBsum; 5WL1; -.
DR PDBsum; 6CUG; -.
DR PDBsum; 6D64; -.
DR AlphaFoldDB; P29016; -.
DR SMR; P29016; -.
DR BioGRID; 107348; 89.
DR IntAct; P29016; 34.
DR MINT; P29016; -.
DR STRING; 9606.ENSP00000357150; -.
DR GlyGen; P29016; 4 sites.
DR iPTMnet; P29016; -.
DR PhosphoSitePlus; P29016; -.
DR BioMuta; CD1B; -.
DR DMDM; 115962; -.
DR MassIVE; P29016; -.
DR MaxQB; P29016; -.
DR PaxDb; P29016; -.
DR PeptideAtlas; P29016; -.
DR PRIDE; P29016; -.
DR ProteomicsDB; 54511; -. [P29016-1]
DR ProteomicsDB; 54512; -. [P29016-2]
DR ABCD; P29016; 1 sequenced antibody.
DR Antibodypedia; 20455; 668 antibodies from 38 providers.
DR DNASU; 910; -.
DR Ensembl; ENST00000368168.4; ENSP00000357150.3; ENSG00000158485.11. [P29016-1]
DR GeneID; 910; -.
DR KEGG; hsa:910; -.
DR MANE-Select; ENST00000368168.4; ENSP00000357150.3; NM_001764.3; NP_001755.1.
DR UCSC; uc001frx.4; human. [P29016-1]
DR CTD; 910; -.
DR DisGeNET; 910; -.
DR GeneCards; CD1B; -.
DR HGNC; HGNC:1635; CD1B.
DR HPA; ENSG00000158485; Tissue enriched (lymphoid).
DR MIM; 188360; gene.
DR neXtProt; NX_P29016; -.
DR OpenTargets; ENSG00000158485; -.
DR PharmGKB; PA26194; -.
DR VEuPathDB; HostDB:ENSG00000158485; -.
DR eggNOG; ENOG502SJH6; Eukaryota.
DR GeneTree; ENSGT01040000240396; -.
DR HOGENOM; CLU_047501_9_2_1; -.
DR InParanoid; P29016; -.
DR OMA; FAGDFQI; -.
DR OrthoDB; 827472at2759; -.
DR PhylomeDB; P29016; -.
DR TreeFam; TF336723; -.
DR PathwayCommons; P29016; -.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR SignaLink; P29016; -.
DR BioGRID-ORCS; 910; 6 hits in 1070 CRISPR screens.
DR EvolutionaryTrace; P29016; -.
DR GenomeRNAi; 910; -.
DR Pharos; P29016; Tbio.
DR PRO; PR:P29016; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P29016; protein.
DR Bgee; ENSG00000158485; Expressed in thymus and 70 other tissues.
DR ExpressionAtlas; P29016; baseline and differential.
DR Genevisible; P29016; HS.
DR GO; GO:0009986; C:cell surface; HDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0030883; F:endogenous lipid antigen binding; IBA:GO_Central.
DR GO; GO:0030884; F:exogenous lipid antigen binding; IBA:GO_Central.
DR GO; GO:0071723; F:lipopeptide binding; IBA:GO_Central.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0048006; P:antigen processing and presentation, endogenous lipid antigen via MHC class Ib; IBA:GO_Central.
DR GO; GO:0048007; P:antigen processing and presentation, exogenous lipid antigen via MHC class Ib; IBA:GO_Central.
DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.30.500.10; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003597; Ig_C1-set.
DR InterPro; IPR011161; MHC_I-like_Ag-recog.
DR InterPro; IPR037055; MHC_I-like_Ag-recog_sf.
DR InterPro; IPR011162; MHC_I/II-like_Ag-recog.
DR Pfam; PF07654; C1-set; 1.
DR Pfam; PF16497; MHC_I_3; 1.
DR SMART; SM00407; IGc1; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF54452; SSF54452; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Alternative splicing; Cell membrane;
KW Disulfide bond; Endosome; Glycoprotein; Immunity; Immunoglobulin domain;
KW Lysosome; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..333
FT /note="T-cell surface glycoprotein CD1b"
FT /id="PRO_0000014579"
FT TOPO_DOM 18..303
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 325..333
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 185..295
FT /note="Ig-like"
FT MOTIF 329..332
FT /note="Internalization signal"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16874306"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16874306,
FT ECO:0000269|PubMed:19349973"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 120..184
FT /evidence="ECO:0000269|PubMed:12118248,
FT ECO:0000269|PubMed:14764708, ECO:0000269|PubMed:16874306,
FT ECO:0007744|PDB:1GZP, ECO:0007744|PDB:1UQS,
FT ECO:0007744|PDB:2H26"
FT DISULFID 149..163
FT /evidence="ECO:0000269|PubMed:12118248,
FT ECO:0000269|PubMed:14764708, ECO:0000269|PubMed:16874306,
FT ECO:0007744|PDB:1GZP, ECO:0007744|PDB:1UQS,
FT ECO:0007744|PDB:2H26"
FT DISULFID 224..279
FT /evidence="ECO:0000269|PubMed:12118248,
FT ECO:0000269|PubMed:14764708, ECO:0000269|PubMed:16874306,
FT ECO:0007744|PDB:1GZP, ECO:0007744|PDB:1UQS,
FT ECO:0007744|PDB:2H26"
FT VAR_SEQ 242..296
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_016911"
FT MUTAGEN 329..330
FT /note="YQ->AA: Strongly reduced internalization and
FT trafficking to endosomes."
FT /evidence="ECO:0000269|PubMed:10981968"
FT STRAND 27..38
FT /evidence="ECO:0007829|PDB:5WL1"
FT STRAND 41..50
FT /evidence="ECO:0007829|PDB:5WL1"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:5WL1"
FT TURN 60..63
FT /evidence="ECO:0007829|PDB:5WL1"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:5WL1"
FT TURN 70..75
FT /evidence="ECO:0007829|PDB:5WL1"
FT HELIX 78..102
FT /evidence="ECO:0007829|PDB:5WL1"
FT TURN 103..107
FT /evidence="ECO:0007829|PDB:5WL1"
FT STRAND 110..122
FT /evidence="ECO:0007829|PDB:5WL1"
FT STRAND 128..136
FT /evidence="ECO:0007829|PDB:5WL1"
FT STRAND 139..145
FT /evidence="ECO:0007829|PDB:5WL1"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:5WL1"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:5WL1"
FT HELIX 156..166
FT /evidence="ECO:0007829|PDB:5WL1"
FT HELIX 172..181
FT /evidence="ECO:0007829|PDB:5WL1"
FT HELIX 183..194
FT /evidence="ECO:0007829|PDB:5WL1"
FT HELIX 196..199
FT /evidence="ECO:0007829|PDB:5WL1"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:5WL1"
FT STRAND 219..232
FT /evidence="ECO:0007829|PDB:5WL1"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:5WL1"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:6CUG"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:5WL1"
FT TURN 257..259
FT /evidence="ECO:0007829|PDB:5WL1"
FT STRAND 260..270
FT /evidence="ECO:0007829|PDB:5WL1"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:5WL1"
FT STRAND 277..282
FT /evidence="ECO:0007829|PDB:5WL1"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:5WL1"
FT STRAND 291..294
FT /evidence="ECO:0007829|PDB:5WL1"
SQ SEQUENCE 333 AA; 36939 MW; 7D02B670D4DE8CC7 CRC64;
MLLLPFQLLA VLFPGGNSEH AFQGPTSFHV IQTSSFTNST WAQTQGSGWL DDLQIHGWDS
DSGTAIFLKP WSKGNFSDKE VAELEEIFRV YIFGFAREVQ DFAGDFQMKY PFEIQGIAGC
ELHSGGAIVS FLRGALGGLD FLSVKNASCV PSPEGGSRAQ KFCALIIQYQ GIMETVRILL
YETCPRYLLG VLNAGKADLQ RQVKPEAWLS SGPSPGPGRL QLVCHVSGFY PKPVWVMWMR
GEQEQQGTQL GDILPNANWT WYLRATLDVA DGEAAGLSCR VKHSSLEGQD IILYWRNPTS
IGSIVLAIIV PSLLLLLCLA LWYMRRRSYQ NIP
