ID LV211_HUMAN Reviewed; 119 AA. AC P01706; A0A075B6K3; P01707; P01708; P01712; P01713; P80422; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 02-NOV-2016, sequence version 2. DT 16-JAN-2019, entry version 105. DE RecName: Full=Immunoglobulin lambda variable 2-11 {ECO:0000303|PubMed:11872955, ECO:0000303|Ref.9}; DE AltName: Full=Ig gamma lambda chain V-II region DOT {ECO:0000305|PubMed:7737190}; DE AltName: Full=Ig lambda chain V-II region BOH {ECO:0000305|PubMed:804002}; DE AltName: Full=Ig lambda chain V-II region BUR {ECO:0000305|PubMed:113407}; DE AltName: Full=Ig lambda chain V-II region NIG-58 {ECO:0000305|PubMed:6787031}; DE AltName: Full=Ig lambda chain V-II region TRO {ECO:0000305|PubMed:118915}; DE AltName: Full=Ig lambda chain V-II region WIN {ECO:0000305|PubMed:102365}; DE Flags: Precursor; GN Name=IGLV2-11 {ECO:0000303|PubMed:11872955, ECO:0000303|Ref.9}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE RP IGLV2-11*01). RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J., RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., RA Khan A.S., Lane L., Tilahun Y., Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [2] RP PROTEIN SEQUENCE OF 20-119, AND PYROGLUTAMATE FORMATION AT GLN-20. RX PubMed=804002; RA Kohler H., Rudofsky S., Kluskens L.; RT "The primary structure of a human lambda II chain."; RL J. Immunol. 114:415-421(1975). RN [3] RP PROTEIN SEQUENCE OF 20-119, AND PYROGLUTAMATE FORMATION AT GLN-20. RX PubMed=102365; DOI=10.1016/0005-2795(78)90598-6; RA Chen B.L., Chiu Y.-Y.H., Humphrey R.L., Poljak R.J.; RT "Amino acid sequence of the human myeloma lambda chain Win."; RL Biochim. Biophys. Acta 537:9-21(1978). RN [4] RP PROTEIN SEQUENCE OF 20-119, AND PYROGLUTAMATE FORMATION AT GLN-20. RX PubMed=118915; RA Scholz R., Yang C., Hilschmann N.; RT "Rule of antibody structure. Primary structure of a human monoclonal RT IgAl-immunoglobulin (myeloma protein Tro). VI. Amino acid sequence of RT the L-chain, lambda-type, subgroup II."; RL Hoppe-Seyler's Z. Physiol. Chem. 360:1903-1918(1979). RN [5] RP PROTEIN SEQUENCE OF 20-119, AND PYROGLUTAMATE FORMATION AT GLN-20. RX PubMed=113407; RA Infante A.J., Putnam F.W.; RT "Primary structure of a human IgA1 immunoglobulin. V. Amino acid RT sequence of a human IgA lambda light chain (Bur)."; RL J. Biol. Chem. 254:9006-9016(1979). RN [6] RP PROTEIN SEQUENCE OF 20-119, AND PYROGLUTAMATE FORMATION AT GLN-20. RX PubMed=6787031; RA Takayasu T., Takahashi N., Shinoda T., Okuyama T., Tomioka H.; RT "Comparative studies on the structure of the light chains of human RT immunoglobulins. III. Amino acid sequence of a lambda type Bence Jones RT euglobulin."; RL J. Biochem. 89:421-436(1981). RN [7] RP PROTEIN SEQUENCE OF 20-119. RX PubMed=7737190; DOI=10.1111/j.1432-1033.1995.tb20336.x; RA Stoppini M., Bellotti V., Negri A., Merlini G., Garver F., Ferri G.; RT "Characterization of the two unique human anti-flavin monoclonal RT immunoglobulins."; RL Eur. J. Biochem. 228:886-893(1995). RN [8] RP NOMENCLATURE. RX PubMed=11872955; RA Lefranc M.P.; RT "Nomenclature of the human immunoglobulin lambda (IGL) genes."; RL Exp. Clin. Immunogenet. 18:242-254(2001). RN [9] RP NOMENCLATURE. RA Lefranc M.P., Lefranc G.; RT "The Immunoglobulin FactsBook."; RL (In) Lefranc M.P., Lefranc G. (eds.); RL The Immunoglobulin FactsBook., pp.1-458, Academic Press, London. RL (2001). RN [10] RP REVIEW ON SOMATIC HYPERMUTATION. RX PubMed=17576170; DOI=10.1146/annurev.genet.41.110306.130340; RA Teng G., Papavasiliou F.N.; RT "Immunoglobulin somatic hypermutation."; RL Annu. Rev. Genet. 41:107-120(2007). RN [11] RP REVIEW ON IMMUNOGLOBULINS. RX PubMed=20176268; DOI=10.1016/j.jaci.2009.09.046; RA Schroeder H.W. Jr., Cavacini L.; RT "Structure and function of immunoglobulins."; RL J. Allergy Clin. Immunol. 125:S41-S52(2010). RN [12] RP REVIEW ON FUNCTION. RX PubMed=22158414; DOI=10.1038/nri3128; RA McHeyzer-Williams M., Okitsu S., Wang N., McHeyzer-Williams L.; RT "Molecular programming of B cell memory."; RL Nat. Rev. Immunol. 12:24-34(2012). RN [13] RP NOMENCLATURE. RX PubMed=24600447; DOI=10.3389/fimmu.2014.00022; RA Lefranc M.P.; RT "Immunoglobulin and T Cell Receptor Genes: IMGT((R)) and the Birth and RT Rise of Immunoinformatics."; RL Front. Immunol. 5:22-22(2014). CC -!- FUNCTION: V region of the variable domain of immunoglobulin light CC chains that participates in the antigen recognition CC (PubMed:24600447). Immunoglobulins, also known as antibodies, are CC membrane-bound or secreted glycoproteins produced by B CC lymphocytes. In the recognition phase of humoral immunity, the CC membrane-bound immunoglobulins serve as receptors which, upon CC binding of a specific antigen, trigger the clonal expansion and CC differentiation of B lymphocytes into immunoglobulins-secreting CC plasma cells. Secreted immunoglobulins mediate the effector phase CC of humoral immunity, which results in the elimination of bound CC antigens (PubMed:20176268, PubMed:22158414). The antigen binding CC site is formed by the variable domain of one heavy chain, together CC with that of its associated light chain. Thus, each immunoglobulin CC has two antigen binding sites with remarkable affinity for a CC particular antigen. The variable domains are assembled by a CC process called V-(D)-J rearrangement and can then be subjected to CC somatic hypermutations which, after exposure to antigen and CC selection, allow affinity maturation for a particular antigen CC (PubMed:17576170, PubMed:20176268). {ECO:0000303|PubMed:17576170, CC ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414, CC ECO:0000303|PubMed:24600447}. CC -!- SUBUNIT: Immunoglobulins are composed of two identical heavy CC chains and two identical light chains; disulfide-linked. CC {ECO:0000303|PubMed:20176268}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268, CC ECO:0000303|PubMed:22158414}. Cell membrane CC {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. CC -!- POLYMORPHISM: There are several alleles. The sequence shown is CC that of IMGT allele IGLV2-11*01. CC -!- CAUTION: For an example of a full-length immunoglobulin lambda CC light chain see AC P0DOX8. {ECO:0000305}. 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; AC244157; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; A01972; L2HUBH. DR PIR; A01973; L2HUTR. DR PIR; A01974; L2HUBR. DR PIR; A01978; L2HUWN. DR PIR; A01979; L2HU58. DR ProteinModelPortal; P01706; -. DR SMR; P01706; -. DR IMGT_GENE-DB; IGLV2-11; -. DR BioMuta; IGLV2-11; -. DR DMDM; 126556; -. DR jPOST; P01706; -. DR PeptideAtlas; P01706; -. DR PRIDE; P01706; -. DR ProteomicsDB; 51434; -. DR ProteomicsDB; 51435; -. DR ProteomicsDB; 51436; -. DR ProteomicsDB; 51440; -. DR ProteomicsDB; 51441; -. DR ProteomicsDB; 57686; -. DR TopDownProteomics; P01706; -. DR Ensembl; ENST00000390314; ENSP00000374849; ENSG00000211668. DR EuPathDB; HostDB:ENSG00000211668.2; -. DR GeneCards; IGLV2-11; -. DR HGNC; HGNC:5887; IGLV2-11. DR neXtProt; NX_P01706; -. DR OpenTargets; ENSG00000211668; -. DR GeneTree; ENSGT00940000154179; -. DR HOVERGEN; HBG018013; -. DR OMA; SGASSWI; -. DR PhylomeDB; P01706; -. DR Reactome; R-HSA-166663; Initial triggering of complement. DR Reactome; R-HSA-173623; Classical antibody-mediated complement activation. DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell. DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall. DR Reactome; R-HSA-2029481; FCGR activation. DR Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation. DR Reactome; R-HSA-2029485; Role of phospholipids in phagocytosis. DR Reactome; R-HSA-2168880; Scavenging of heme from plasma. DR Reactome; R-HSA-2454202; Fc epsilon receptor (FCERI) signaling. DR Reactome; R-HSA-2730905; Role of LAT2/NTAL/LAB on calcium mobilization. DR Reactome; R-HSA-2871796; FCERI mediated MAPK activation. DR Reactome; R-HSA-2871809; FCERI mediated Ca+2 mobilization. DR Reactome; R-HSA-2871837; FCERI mediated NF-kB activation. DR Reactome; R-HSA-5690714; CD22 mediated BCR regulation. DR Reactome; R-HSA-977606; Regulation of Complement cascade. DR Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers. DR PRO; PR:P01706; -. DR Proteomes; UP000005640; Chromosome 22. DR Bgee; ENSG00000211668; Expressed in 86 organ(s), highest expression level in lymph node. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0003823; F:antigen binding; NAS:UniProtKB. DR GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome. DR GO; GO:0006956; P:complement activation; TAS:Reactome. DR GO; GO:0006958; P:complement activation, classical pathway; TAS:Reactome. DR GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome. DR GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome. DR GO; GO:0006955; P:immune response; IBA:GO_Central. DR GO; GO:0002377; P:immunoglobulin production; IBA:GO_Central. DR GO; GO:0050900; P:leukocyte migration; TAS:Reactome. DR GO; GO:0006898; P:receptor-mediated endocytosis; TAS:Reactome. DR GO; GO:0030449; P:regulation of complement activation; TAS:Reactome. DR GO; GO:0050776; P:regulation of immune response; TAS:Reactome. DR Gene3D; 2.60.40.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR013106; Ig_V-set. DR Pfam; PF07686; V-set; 1. DR SMART; SM00409; IG; 1. DR SMART; SM00406; IGv; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 1: Evidence at protein level; KW Adaptive immunity; Cell membrane; Complete proteome; KW Direct protein sequencing; Disulfide bond; Immunity; KW Immunoglobulin domain; Immunoglobulin V region; Membrane; KW Polymorphism; Pyrrolidone carboxylic acid; Reference proteome; KW Secreted; Signal. FT SIGNAL 1 19 {ECO:0000269|PubMed:102365, FT ECO:0000269|PubMed:113407, FT ECO:0000269|PubMed:118915, FT ECO:0000269|PubMed:6787031, FT ECO:0000269|PubMed:7737190, FT ECO:0000269|PubMed:804002}. FT CHAIN 20 119 Immunoglobulin lambda variable 2-11. FT {ECO:0000269|PubMed:102365, FT ECO:0000269|PubMed:113407, FT ECO:0000269|PubMed:118915, FT ECO:0000269|PubMed:6787031, FT ECO:0000269|PubMed:7737190, FT ECO:0000269|PubMed:804002}. FT /FTId=PRO_0000059832. FT DOMAIN 20 >119 Ig-like. {ECO:0000255|PROSITE- FT ProRule:PRU00114}. FT MOD_RES 20 20 Pyrrolidone carboxylic acid. FT {ECO:0000269|PubMed:102365, FT ECO:0000269|PubMed:113407, FT ECO:0000269|PubMed:118915, FT ECO:0000269|PubMed:6787031, FT ECO:0000269|PubMed:804002}. FT DISULFID 41 109 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT CONFLICT 20 20 Q -> A (in Ref. 7; AA sequence). FT {ECO:0000305}. FT CONFLICT 27 28 RS -> PR (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 29 29 V -> L (in Ref. 7; AA sequence). FT {ECO:0000305}. FT CONFLICT 35 35 Q -> H (in Ref. 5; AA sequence). FT {ECO:0000305}. FT CONFLICT 36 36 S -> A (in Ref. 7; AA sequence). FT {ECO:0000305}. FT CONFLICT 37 37 V -> L (in Ref. 6; AA sequence). FT {ECO:0000305}. FT CONFLICT 42 46 TGTSS -> SGAPC (in Ref. 6; AA sequence). FT {ECO:0000305}. FT CONFLICT 42 42 T -> A (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 42 42 T -> I (in Ref. 5; AA sequence). FT {ECO:0000305}. FT CONFLICT 44 53 TSSDVGGYNY -> LPSVVDDDNF (in Ref. 7; AA FT sequence). {ECO:0000305}. FT CONFLICT 44 49 TSSDVG -> SYSNVT (in Ref. 3; AA FT sequence). {ECO:0000305}. FT CONFLICT 47 47 D -> N (in Ref. 5; AA sequence). FT {ECO:0000305}. FT CONFLICT 49 53 GGYNY -> DGCES (in Ref. 6; AA sequence). FT {ECO:0000305}. FT CONFLICT 50 52 GYN -> DYK (in Ref. 5; AA sequence). FT {ECO:0000305}. FT CONFLICT 50 50 G -> A (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 51 53 YNY -> NHF (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 53 53 Y -> H (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 53 53 Y -> S (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 60 60 H -> D (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 60 60 H -> T (in Ref. 7; AA sequence). FT {ECO:0000305}. FT CONFLICT 63 63 K -> R (in Ref. 7; AA sequence). FT {ECO:0000305}. FT CONFLICT 64 64 A -> V (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 66 68 KLM -> RLL (in Ref. 7; AA sequence). FT {ECO:0000305}. FT CONFLICT 68 68 M -> I (in Ref. 5; AA sequence, 6; AA FT sequence and 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 70 70 Y -> F (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 71 74 DVSK -> GFSN (in Ref. 6; AA sequence). FT {ECO:0000305}. FT CONFLICT 71 73 DVS -> GVN (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 71 71 D -> E (in Ref. 5; AA sequence). FT {ECO:0000305}. FT CONFLICT 72 74 VSK -> DSL (in Ref. 7; AA sequence). FT {ECO:0000305}. FT CONFLICT 73 73 S -> D (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 73 73 S -> T (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 74 74 K -> S (in Ref. 5; AA sequence). FT {ECO:0000305}. FT CONFLICT 81 81 D -> L (in Ref. 6; AA sequence). FT {ECO:0000305}. FT CONFLICT 81 81 D -> N (in Ref. 7; AA sequence). FT {ECO:0000305}. FT CONFLICT 81 81 D -> Y (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 83 83 F -> L (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 89 93 GNTAS -> DTKAA (in Ref. 7; AA sequence). FT {ECO:0000305}. FT CONFLICT 89 89 G -> A (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 90 90 N -> D (in Ref. 4; AA sequence and 6; AA FT sequence). {ECO:0000305}. FT CONFLICT 91 91 T -> A (in Ref. 6; AA sequence). FT {ECO:0000305}. FT CONFLICT 100 102 QAE -> RAD (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 101 102 AE -> PD (in Ref. 7; AA sequence). FT {ECO:0000305}. FT CONFLICT 101 101 A -> V (in Ref. 6; AA sequence). FT {ECO:0000305}. FT CONFLICT 102 103 ED -> NN (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 106 108 DYY -> TYF (in Ref. 7; AA sequence). FT {ECO:0000305}. FT CONFLICT 106 106 D -> H (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 110 110 C -> S (in Ref. 3; AA sequence and 6; AA FT sequence). {ECO:0000305}. FT CONFLICT 113 119 AGSYTFH -> GGTYSLI (in Ref. 3; AA FT sequence). {ECO:0000305}. FT CONFLICT 113 119 AGSYTFH -> VGNYIFV (in Ref. 7; AA FT sequence). {ECO:0000305}. FT CONFLICT 113 113 A -> I (in Ref. 5; AA sequence). FT {ECO:0000305}. FT CONFLICT 114 119 GSYTFH -> DSSVIF (in Ref. 6; AA FT sequence). {ECO:0000305}. FT CONFLICT 115 115 S -> R (in Ref. 2; AA sequence and 4; AA FT sequence). {ECO:0000305}. FT CONFLICT 116 119 YTFH -> FTWV (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 117 119 TFH -> SVI (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 117 119 TFH -> VFG (in Ref. 5; AA sequence). FT {ECO:0000305}. FT NON_TER 119 119 SQ SEQUENCE 119 AA; 12644 MW; 5077937A60FFE912 CRC64; MAWALLLLSL LTQGTGSWAQ SALTQPRSVS GSPGQSVTIS CTGTSSDVGG YNYVSWYQQH PGKAPKLMIY DVSKRPSGVP DRFSGSKSGN TASLTISGLQ AEDEADYYCC SYAGSYTFH //