LV211_HUMAN
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 03-AUG-2022, entry version 121.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE IGLV2-11*01).
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., 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., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., 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., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA 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 IgAl-
RT immunoglobulin (myeloma protein Tro). VI. Amino acid sequence of the L-
RT 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; DOI=10.1016/s0021-9258(19)86802-3;
RA Infante A.J., Putnam F.W.;
RT "Primary structure of a human IgA1 immunoglobulin. V. Amino acid sequence
RT 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; DOI=10.1093/oxfordjournals.jbchem.a133217;
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; DOI=10.1159/000049203;
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. (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 Rise
RT 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 (PubMed:24600447).
CC Immunoglobulins, also known as antibodies, are membrane-bound or
CC secreted glycoproteins produced by B lymphocytes. In the recognition
CC phase of humoral immunity, the membrane-bound immunoglobulins serve as
CC receptors which, upon binding of a specific antigen, trigger the clonal
CC expansion and differentiation of B lymphocytes into immunoglobulins-
CC secreting plasma cells. Secreted immunoglobulins mediate the effector
CC phase of humoral immunity, which results in the elimination of bound
CC antigens (PubMed:20176268, PubMed:22158414). The antigen binding site
CC is formed by the variable domain of one heavy chain, together with that
CC of its associated light chain. Thus, each immunoglobulin has two
CC antigen binding sites with remarkable affinity for a particular
CC antigen. The variable domains are assembled by a process called V-(D)-J
CC rearrangement and can then be subjected to somatic hypermutations
CC which, after exposure to antigen and selection, allow affinity
CC maturation for a particular antigen (PubMed:17576170, PubMed:20176268).
CC {ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268,
CC ECO:0000303|PubMed:22158414, ECO:0000303|PubMed:24600447}.
CC -!- SUBUNIT: Immunoglobulins are composed of two identical heavy chains and
CC 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 that of
CC IMGT allele IGLV2-11*01.
CC -!- CAUTION: For an example of a full-length immunoglobulin lambda light
CC chain see AC P0DOX8. {ECO:0000305}.
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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 AlphaFoldDB; P01706; -.
DR SMR; P01706; -.
DR IMGT_GENE-DB; IGLV2-11; -.
DR BioMuta; IGLV2-11; -.
DR DMDM; 126556; -.
DR jPOST; P01706; -.
DR MassIVE; P01706; -.
DR PeptideAtlas; P01706; -.
DR PRIDE; P01706; -.
DR TopDownProteomics; P01706; -.
DR Ensembl; ENST00000390314.2; ENSP00000374849.2; ENSG00000211668.2.
DR GeneCards; IGLV2-11; -.
DR HGNC; HGNC:5887; IGLV2-11.
DR HPA; ENSG00000211668; Tissue enhanced (intestine, lymphoid tissue).
DR neXtProt; NX_P01706; -.
DR OpenTargets; ENSG00000211668; -.
DR VEuPathDB; HostDB:ENSG00000211668; -.
DR GeneTree; ENSGT00940000154179; -.
DR OMA; SYNGVGW; -.
DR PhylomeDB; P01706; -.
DR PathwayCommons; 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-9664323; FCGR3A-mediated IL10 synthesis.
DR Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis.
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 ChiTaRS; IGLV2-11; human.
DR Pharos; P01706; Tdark.
DR PRO; PR:P01706; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P01706; protein.
DR Bgee; ENSG00000211668; Expressed in duodenum and 90 other tissues.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0019814; C:immunoglobulin complex; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0003823; F:antigen binding; NAS:UniProtKB.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0006955; P:immune response; IBA:GO_Central.
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; Direct protein sequencing;
KW Disulfide bond; Immunity; Immunoglobulin; Immunoglobulin domain; Membrane;
KW Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:102365,
FT ECO:0000269|PubMed:113407, ECO:0000269|PubMed:118915,
FT ECO:0000269|PubMed:6787031, ECO:0000269|PubMed:7737190,
FT ECO:0000269|PubMed:804002"
FT CHAIN 20..119
FT /note="Immunoglobulin lambda variable 2-11"
FT /evidence="ECO:0000269|PubMed:102365,
FT ECO:0000269|PubMed:113407, ECO:0000269|PubMed:118915,
FT ECO:0000269|PubMed:6787031, ECO:0000269|PubMed:7737190,
FT ECO:0000269|PubMed:804002"
FT /id="PRO_0000059832"
FT DOMAIN 20..>119
FT /note="Ig-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT MOD_RES 20
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:102365,
FT ECO:0000269|PubMed:113407, ECO:0000269|PubMed:118915,
FT ECO:0000269|PubMed:6787031, ECO:0000269|PubMed:804002"
FT DISULFID 41..109
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 20
FT /note="Q -> A (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 27..28
FT /note="RS -> PR (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 29
FT /note="V -> L (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 35
FT /note="Q -> H (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 36
FT /note="S -> A (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 37
FT /note="V -> L (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 42..46
FT /note="TGTSS -> SGAPC (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="T -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="T -> I (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 44..53
FT /note="TSSDVGGYNY -> LPSVVDDDNF (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 44..49
FT /note="TSSDVG -> SYSNVT (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="D -> N (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 49..53
FT /note="GGYNY -> DGCES (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 50..52
FT /note="GYN -> DYK (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="G -> A (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 51..53
FT /note="YNY -> NHF (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 53
FT /note="Y -> H (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 53
FT /note="Y -> S (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="H -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="H -> T (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="K -> R (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="A -> V (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 66..68
FT /note="KLM -> RLL (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="M -> I (in Ref. 5; AA sequence, 6; AA sequence and
FT 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="Y -> F (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 71..74
FT /note="DVSK -> GFSN (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 71..73
FT /note="DVS -> GVN (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="D -> E (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 72..74
FT /note="VSK -> DSL (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="S -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="S -> T (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="K -> S (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="D -> L (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="D -> N (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="D -> Y (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="F -> L (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 89..93
FT /note="GNTAS -> DTKAA (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="G -> A (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 90
FT /note="N -> D (in Ref. 4; AA sequence and 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="T -> A (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 100..102
FT /note="QAE -> RAD (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 101..102
FT /note="AE -> PD (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="A -> V (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 102..103
FT /note="ED -> NN (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 106..108
FT /note="DYY -> TYF (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="D -> H (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="C -> S (in Ref. 3; AA sequence and 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 113..119
FT /note="AGSYTFH -> GGTYSLI (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 113..119
FT /note="AGSYTFH -> VGNYIFV (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="A -> I (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 114..119
FT /note="GSYTFH -> DSSVIF (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="S -> R (in Ref. 2; AA sequence and 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 116..119
FT /note="YTFH -> FTWV (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 117..119
FT /note="TFH -> SVI (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 117..119
FT /note="TFH -> VFG (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 119
SQ SEQUENCE 119 AA; 12644 MW; 5077937A60FFE912 CRC64;
MAWALLLLSL LTQGTGSWAQ SALTQPRSVS GSPGQSVTIS CTGTSSDVGG YNYVSWYQQH
PGKAPKLMIY DVSKRPSGVP DRFSGSKSGN TASLTISGLQ AEDEADYYCC SYAGSYTFH
