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 04-NOV-2026, entry version 213. 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; DOI=10.4049/jimmunol.143.5.1723; 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 IN COMPLEXES WITH B2M; GANGLIOSIDE GM2 AND RP 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 IN COMPLEX WITH B2M AND GLUCOSE MONOMYCOLATE, AND RP 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 IN COMPLEX WITH B2M; PHOSPHATIDYLCHOLINE AND SPACER RP LIGAND, GLYCOSYLATION AT ASN-38 AND ASN-75, IDENTIFICATION BY MASS RP 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=6; 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_001764.3. [P29016-1] DR RefSeq; XP_011508421.1; XM_011510119.4. [P29016-2] DR RefSeq; XP_054195511.1; XM_054339536.1. [P29016-2] DR PDB; 1GZP; X-ray; 2.80 A; A=17-304. DR PDB; 1GZQ; X-ray; 2.26 A; A=17-304. DR PDB; 1UQS; X-ray; 3.10 A; A=17-304. 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=204-295. 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 PDB; 7MX4; X-ray; 1.73 A; A=212-258, A=264-296. DR PDB; 7MXF; X-ray; 2.00 A; A=212-258, A=264-296. DR PDB; 7MXH; X-ray; 2.11 A; A=212-258, A=264-296. DR PDB; 8DV3; X-ray; 1.90 A; A=20-296. DR PDB; 8DV4; X-ray; 2.40 A; A=20-296. DR PDB; 8GLE; X-ray; 1.85 A; A=20-296. DR PDB; 8GLF; X-ray; 2.00 A; A=20-296. DR PDB; 8GLG; X-ray; 1.60 A; A=20-296. DR PDB; 8GLH; X-ray; 1.83 A; A=20-296. DR PDB; 8GLI; X-ray; 2.10 A; A=20-296. DR PDB; 8ZOX; EM; 3.18 A; A=18-295. DR PDB; 9OI0; X-ray; 1.84 A; A=22-296. DR AlphaFoldDB; P29016; -. DR EMDB; EMD-60321; -. DR MDRepo; P29016; -. DR SMR; P29016; -. DR BioGRID; 107348; 89. DR ComplexPortal; CPX-647; CD1B-B2M complex. DR FunCoup; P29016; 305. DR IntAct; P29016; 61. DR STRING; 9606.ENSP00000357150; -. DR GlyCosmos; P29016; 4 sites, No reported glycans. DR GlyGen; P29016; 4 sites, 5 N-linked glycans (2 sites). DR iPTMnet; P29016; -. DR PhosphoSitePlus; P29016; -. DR BioMuta; CD1B; -. DR DMDM; 115962; -. DR MassIVE; P29016; -. DR PaxDb; 9606-ENSP00000357150; -. DR PeptideAtlas; P29016; -. DR ProteomicsDB; 54511; -. [P29016-1] DR ProteomicsDB; 54512; -. [P29016-2] DR ABCD; P29016; 1 sequenced antibody. DR Antibodypedia; 20455; 745 antibodies from 41 providers. DR DNASU; 910; -. DR Ensembl; ENST00000368168.4; ENSP00000357150.3; ENSG00000158485.12. [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 AGR; HGNC:1635; -. DR ClinPGx; PA26194; -. 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 OpenTargets; ENSG00000158485; -. DR VEuPathDB; HostDB:ENSG00000158485; -. DR eggNOG; ENOG502SJH6; Eukaryota. DR GeneTree; ENSGT01120000271825; -. DR HOGENOM; CLU_047501_9_2_1; -. DR InParanoid; P29016; -. DR OMA; ACPKWDG; -. DR OrthoDB; 8890485at2759; -. DR PAN-GO; P29016; 9 GO annotations based on evolutionary models. DR PhylomeDB; P29016; -. DR PathwayCommons; P29016; -. DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell. DR SignaLink; P29016; -. DR Agora; ENSG00000158485; -. DR BioGRID-ORCS; 910; 6 hits in 1150 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 71 other cell types or tissues. DR ExpressionAtlas; P29016; baseline and differential. DR GO; GO:0009986; C:cell surface; HDA:UniProtKB. DR GO; GO:0010008; C:endosome membrane; EXP:UniProtKB. DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central. DR GO; GO:0005576; C:extracellular region; IBA:GO_Central. DR GO; GO:0005765; C:lysosomal membrane; EXP:UniProtKB. DR GO; GO:0016020; C:membrane; TAS:ProtInc. DR GO; GO:0005886; C:plasma membrane; EXP:UniProtKB. 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: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:0006955; P:immune response; IBA:GO_Central. DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IBA:GO_Central. DR CDD; cd21029; IgC1_CD1; 1. DR FunFam; 2.60.40.10:FF:000254; Antigen-presenting glycoprotein CD1d1; 1. DR FunFam; 3.30.500.10:FF:000002; Antigen-presenting glycoprotein CD1d1; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 1. DR Gene3D; 3.30.500.10; MHC class I-like antigen recognition-like; 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; IPR050208; MHC_class-I_related. 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 PANTHER; PTHR16675; MHC CLASS I-RELATED; 1. DR PANTHER; PTHR16675:SF130; T-CELL SURFACE GLYCOPROTEIN CD1B; 1. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF16497; MHC_I_3; 1. DR SMART; SM00407; IGc1; 1. DR SUPFAM; SSF48726; Immunoglobulin; 1. DR SUPFAM; SSF54452; MHC antigen-recognition domain; 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; Proteomics identification; Reference proteome; Signal; KW Transmembrane; 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 TURN 124..126 FT /evidence="ECO:0007829|PDB:8ZOX" 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..178 FT /evidence="ECO:0007829|PDB:5WL1" FT HELIX 179..183 FT /evidence="ECO:0007829|PDB:5WL1" FT HELIX 184..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 215..217 FT /evidence="ECO:0007829|PDB:1UQS" 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 274..276 FT /evidence="ECO:0007829|PDB:8DV4" 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 //