ID KVD33_HUMAN Reviewed; 117 AA. AC P01593; A0A0B4J1U0; P01595; P01605; P01607; P01608; P01609; P01613; P80362; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 02-NOV-2016, sequence version 2. DT 27-MAR-2024, entry version 141. DE RecName: Full=Immunoglobulin kappa variable 1D-33 {ECO:0000303|PubMed:11549845, ECO:0000303|Ref.15}; DE AltName: Full=Ig kappa chain V-I region AG {ECO:0000305|PubMed:4893682}; DE AltName: Full=Ig kappa chain V-I region Bi {ECO:0000305|PubMed:4563064}; DE AltName: Full=Ig kappa chain V-I region Lay {ECO:0000305|PubMed:2496160, ECO:0000305|PubMed:824717}; DE AltName: Full=Ig kappa chain V-I region Ni {ECO:0000305|PubMed:4709625}; DE AltName: Full=Ig kappa chain V-I region Rei {ECO:0000305|PubMed:809329}; DE AltName: Full=Ig kappa chain V-I region Roy {ECO:0000305|PubMed:5595110}; DE AltName: Full=Ig kappa chain V-I region Scw {ECO:0000305|PubMed:4435756}; DE AltName: Full=Ig kappa chain V-I region WAT {ECO:0000305|PubMed:6167731, ECO:0000305|PubMed:7993911}; DE Flags: Precursor; GN Name=IGKV1D-33 {ECO:0000303|PubMed:11549845, ECO:0000303|Ref.15}; 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 IGKV1D-33*01). RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [2] RP PROTEIN SEQUENCE OF 23-117. RX PubMed=5595110; RA Hilschmann N.; RT "Chemical structure of 2 kappa-type Bence Jones proteins (Roy and Cum.)."; RL Hoppe-Seyler's Z. Physiol. Chem. 348:1077-1080(1967). RN [3] RP SEQUENCE REVISION TO 61 AND 63. RA Hilschmann N., Barnikol H.U., Hess M., Langer B., Ponstingl H., RA Steinmetz-Kayne M., Suter L., Watanabe S.; RL (In) Franek F., Shugar D. (eds.); RL Gamma globulins: structure and function, pp.57-74, Academic Press, New York RL (1969). RN [4] RP PROTEIN SEQUENCE OF 23-117. RX PubMed=4893682; DOI=10.1016/s0021-9258(18)83405-6; RA Titani K., Shinoda T., Putnam F.W.; RT "The amino acid sequence of a kappa type Bence-Jones protein. 3. The RT complete sequence and the location of the disulfide bridges."; RL J. Biol. Chem. 244:3550-3560(1969). RN [5] RP PROTEIN SEQUENCE OF 23-117. RX PubMed=4563064; RA Braun M., Leibold W., Barnikol H.U., Hilschmann N.; RT "Principle of antibody structure. The primary structure of a monoclonal RT kappa I-type immunoglobulin L-chain (Bence Jones protein Bi). 3. The RT complete amino acid sequence and the genetic significance of the RT variability principles for the mechanism of antibody formation."; RL Hoppe-Seyler's Z. Physiol. Chem. 353:1284-1306(1972). RN [6] RP PROTEIN SEQUENCE OF 23-117. RX PubMed=4709625; RA Shinoda T.; RT "Amino acid sequence of a human kappa type Bence-Jones protein. II. RT Chymotryptic peptides and sequence of protein Ni."; RL J. Biochem. 73:433-446(1973). RN [7] RP PROTEIN SEQUENCE OF 23-117. RX PubMed=4435756; RA Eulitz M., Hilschmann N.; RT "The primary structure of a human immunoglobulin L-chain of kappa-type RT (Bence-Jones protein Scw.), II: the chymotryptic peptides and the complete RT amino acid sequence."; RL Hoppe-Seyler's Z. Physiol. Chem. 355:842-866(1974). RN [8] RP PROTEIN SEQUENCE OF 23-117. RX PubMed=809329; RA Palm W., Hilschmann N.; RT "The primary structure of a crystalline monoclonal immunoglobulin kappa- RT type L-chain, subgroup I (Bence-Jones protein Rei); isolation and RT characterization of the tryptic peptides; the complete amino acid sequence RT of the protein; a contribution to the elucidation of the three-dimensional RT structure of antibodies, in particular their combining site."; RL Hoppe-Seyler's Z. Physiol. Chem. 356:167-191(1975). RN [9] RP PROTEIN SEQUENCE OF 23-117. RX PubMed=824717; DOI=10.1111/j.1365-3083.1976.tb03017.x; RA Capra J.D., Klapper D.G.; RT "Complete amino acid sequence of the variable domains of two human IgM RT anti-gamma globulins (Lay/Pom) with shared idiotypic specificities."; RL Scand. J. Immunol. 5:677-684(1976). RN [10] RP PROTEIN SEQUENCE OF 23-117. RX PubMed=2496160; RA Goni F.R., Chen P.P., McGinnis D., Arjonilla M.L., Fernandez J., Carson D., RA Solomon A., Mendez E., Frangione B.; RT "Structural and idiotypic characterization of the L chains of human IgM RT autoantibodies with different specificities."; RL J. Immunol. 142:3158-3163(1989). RN [11] RP ERRATUM OF PUBMED:2496160. RA Goni F.R., Chen P.P., McGinnis D., Arjonilla M.L., Fernandez J., Carson D., RA Solomon A., Mendez E., Frangione B.; RL J. Immunol. 143:3864-3864(1989). RN [12] RP PROTEIN SEQUENCE OF 23-117, AND X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF RP 23-117. RX PubMed=7993911; DOI=10.1021/bi00253a024; RA Huang D.-B., Chang C.-H., Ainsworth C., Bruenger A.T., Eulitz M., RA Solomon A., Stevens F.J., Schiffer M.; RT "Comparison of crystal structures of two homologous proteins: structural RT origin of altered domain interactions in immunoglobulin light-chain RT dimers."; RL Biochemistry 33:14848-14857(1994). RN [13] RP PROTEIN SEQUENCE OF 23-57. RX PubMed=6167731; DOI=10.1016/0022-2836(81)90086-3; RA Stevens F.J., Westholm F.A., Panagiotopoulos N., Schiffer M., Popp R.A., RA Solomon A.; RT "Characterization and preliminary crystallographic data on the VL-related RT fragment of the human kI Bence Jones protein Wat."; RL J. Mol. Biol. 147:185-193(1981). RN [14] RP NOMEMCLATURE. RX PubMed=11549845; DOI=10.1159/000049195; RA Lefranc M.P.; RT "Nomenclature of the human immunoglobulin kappa (IGK) genes."; RL Exp. Clin. Immunogenet. 18:161-174(2001). RN [15] 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 [16] 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 [17] 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 [18] 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 [19] 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). RN [20] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 23-117, AND DISULFIDE BOND. RX PubMed=1182131; DOI=10.1021/bi00693a025; RA Epp O., Lattman E.E., Schiffer M., Huber R., Palm W.; RT "The molecular structure of a dimer composed of the variable portions of RT the Bence-Jones protein REI refined at 2.0-A resolution."; RL Biochemistry 14:4943-4952(1975). 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:20176268, PubMed:17576170). 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 IGKV1D-33*01. CC -!- CAUTION: For an example of a full-length immunoglobulin kappa light CC chain see AC P0DOX7. {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; AC233264; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; A01861; K1HUAG. DR PIR; A01863; K1HUBI. DR PIR; A01871; K1HULY. DR PIR; A01875; K1HUSW. DR PIR; A01880; K1HUNY. DR PIR; A91638; K1HURY. DR PIR; A91663; K1HURE. DR PDB; 1AR2; X-ray; 2.80 A; A=23-117. DR PDB; 1BWW; X-ray; 1.70 A; A/B=23-117. DR PDB; 1REI; X-ray; 2.00 A; A/B=23-117. DR PDB; 1WTL; X-ray; 1.90 A; A/B=23-117. DR PDB; 4L1H; X-ray; 1.68 A; A=23-117. DR PDB; 5XP1; X-ray; 2.88 A; A/B/C/D/E/F/G/H=23-117. DR PDBsum; 1AR2; -. DR PDBsum; 1BWW; -. DR PDBsum; 1REI; -. DR PDBsum; 1WTL; -. DR PDBsum; 4L1H; -. DR PDBsum; 5XP1; -. DR AlphaFoldDB; P01593; -. DR EMDB; EMD-13742; -. DR EMDB; EMD-15971; -. DR EMDB; EMD-17819; -. DR EMDB; EMD-23792; -. DR EMDB; EMD-24236; -. DR EMDB; EMD-24237; -. DR EMDB; EMD-25263; -. DR EMDB; EMD-25264; -. DR EMDB; EMD-25265; -. DR EMDB; EMD-25267; -. DR EMDB; EMD-25655; -. DR EMDB; EMD-25991; -. DR EMDB; EMD-25992; -. DR EMDB; EMD-28757; -. DR EMDB; EMD-30192; -. DR EMDB; EMD-30193; -. DR EMDB; EMD-30194; -. DR EMDB; EMD-30195; -. DR EMDB; EMD-30196; -. DR EMDB; EMD-30197; -. DR EMDB; EMD-32770; -. DR EMDB; EMD-32771; -. DR EMDB; EMD-32772; -. DR EMDB; EMD-33552; -. DR EMDB; EMD-34263; -. DR SMR; P01593; -. DR IntAct; P01593; 3. DR DrugBank; DB04147; Dodecyldimethylamine N-oxide. DR IMGT_GENE-DB; IGKV1D-33; -. DR GlyCosmos; P01593; 2 sites, 1 glycan. DR GlyGen; P01593; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; P01593; -. DR BioMuta; IGKV1D-33; -. DR DMDM; 125759; -. DR jPOST; P01593; -. DR MassIVE; P01593; -. DR PeptideAtlas; P01593; -. DR Ensembl; ENST00000390265.2; ENSP00000374800.2; ENSG00000239975.3. DR AGR; HGNC:5753; -. DR GeneCards; IGKV1D-33; -. DR HGNC; HGNC:5753; IGKV1D-33. DR HPA; ENSG00000239975; Tissue enhanced (gallbladder, lymphoid tissue, stomach, urinary bladder). DR neXtProt; NX_P01593; -. DR VEuPathDB; HostDB:ENSG00000239975; -. DR InParanoid; P01593; -. DR PhylomeDB; P01593; -. DR PathwayCommons; P01593; -. 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-9679191; Potential therapeutics for SARS. 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 SignaLink; P01593; -. DR ChiTaRS; IGKV1D-33; human. DR Pharos; P01593; Tdark. DR PRO; PR:P01593; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; P01593; Protein. DR Bgee; ENSG00000239975; Expressed in bone marrow cell and 87 other cell types or tissues. DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. 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 CDD; cd04980; IgV_L_kappa; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 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 PANTHER; PTHR23267:SF527; IMMUNOGLOBULIN KAPPA VARIABLE 1-33-RELATED; 1. DR PANTHER; PTHR23267; IMMUNOGLOBULIN LIGHT CHAIN; 1. DR Pfam; PF07686; V-set; 1. DR SMART; SM00409; IG; 1. DR SMART; SM00406; IGv; 1. DR SUPFAM; SSF48726; Immunoglobulin; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 1: Evidence at protein level; KW 3D-structure; Adaptive immunity; Cell membrane; Direct protein sequencing; KW Disulfide bond; Immunity; Immunoglobulin; Immunoglobulin domain; Membrane; KW Reference proteome; Secreted; Signal. FT SIGNAL 1..22 FT /evidence="ECO:0000269|PubMed:2496160, FT ECO:0000269|PubMed:4435756, ECO:0000269|PubMed:4563064, FT ECO:0000269|PubMed:4709625, ECO:0000269|PubMed:4893682, FT ECO:0000269|PubMed:5595110, ECO:0000269|PubMed:6167731, FT ECO:0000269|PubMed:7993911, ECO:0000269|PubMed:809329, FT ECO:0000269|PubMed:824717" FT CHAIN 23..117 FT /note="Immunoglobulin kappa variable 1D-33" FT /evidence="ECO:0000269|PubMed:2496160, FT ECO:0000269|PubMed:4435756, ECO:0000269|PubMed:4563064, FT ECO:0000269|PubMed:4709625, ECO:0000269|PubMed:4893682, FT ECO:0000269|PubMed:5595110, ECO:0000269|PubMed:7993911, FT ECO:0000269|PubMed:809329, ECO:0000269|PubMed:824717" FT /id="PRO_0000059737" FT DOMAIN 24..>117 FT /note="Ig-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT REGION 23..45 FT /note="Framework-1" FT REGION 46..56 FT /note="Complementarity-determining-1" FT REGION 57..71 FT /note="Framework-2" FT REGION 72..78 FT /note="Complementarity-determining-2" FT REGION 79..110 FT /note="Framework-3" FT REGION 111..117 FT /note="Complementarity-determining-3" FT DISULFID 45..110 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:1182131" FT CONFLICT 32 FT /note="S -> P (in Ref. 5; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 35 FT /note="A -> V (in Ref. 9; AA sequence and 10; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 36 FT /note="S -> T (in Ref. 6; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 40 FT /note="R -> S (in Ref. 5; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 43..46 FT /note="ITCQ -> LLCE (in Ref. 6; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 46 FT /note="Q -> R (in Ref. 12; AA sequence and 13; AA FT sequence)" FT /evidence="ECO:0000305" FT CONFLICT 50..56 FT /note="DISNYLN -> SVLESGNTFLA (in Ref. 6; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 50..53 FT /note="DISN -> NVNA (in Ref. 9; AA sequence and 10; AA FT sequence)" FT /evidence="ECO:0000305" FT CONFLICT 52..56 FT /note="SNYLN -> RNSLI (in Ref. 5; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 52..54 FT /note="SNY -> RKH (in Ref. 7; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 52..53 FT /note="SN -> IK (in Ref. 8; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 52..53 FT /note="SN -> NH (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 52 FT /note="S -> T (in Ref. 12; AA sequence and 13; AA FT sequence)" FT /evidence="ECO:0000305" FT CONFLICT 53..54 FT /note="NY -> IF (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 53 FT /note="N -> D (in Ref. 13; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 55 FT /note="L -> V (in Ref. 12; AA sequence and 13; AA FT sequence)" FT /evidence="ECO:0000305" FT CONFLICT 58 FT /note="Y -> F (in Ref. 12; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 59 FT /note="Q -> D (in Ref. 7; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 61 FT /note="K -> G (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 61 FT /note="K -> R (in Ref. 12; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 61 FT /note="K -> T (in Ref. 8; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 63 FT /note="G -> K (in Ref. 6; AA sequence and 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 64 FT /note="K -> L (in Ref. 9; AA sequence and 10; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 64 FT /note="K -> Q (in Ref. 12; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 67 FT /note="K -> R (in Ref. 7; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 68 FT /note="L -> F (in Ref. 5; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 68 FT /note="L -> I (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 68 FT /note="L -> V (in Ref. 12; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 72 FT /note="D -> E (in Ref. 8; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 72 FT /note="D -> G (in Ref. 12; AA sequence, 7; AA sequence, 9; FT AA sequence and 10; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 74 FT /note="S -> E (in Ref. 5; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 75 FT /note="N -> I (in Ref. 12; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 75 FT /note="N -> K (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 75 FT /note="N -> T (in Ref. 7; AA sequence, 9; AA sequence and FT 10; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 76 FT /note="L -> R (in Ref. 9; AA sequence and 10; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 77 FT /note="E -> Q (in Ref. 8; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 78 FT /note="T -> A (in Ref. 2; AA sequence, 9; AA sequence, 10; FT AA sequence and 8; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 78 FT /note="T -> I (in Ref. 5; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 85 FT /note="S -> R (in Ref. 5; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 86 FT /note="G -> E (in Ref. 6; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 87 FT /note="S -> T (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 89 FT /note="S -> F (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 93 FT /note="F -> Y (in Ref. 8; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 94..96 FT /note="TFT -> ALS (in Ref. 5; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 95 FT /note="F -> L (in Ref. 7; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 99 FT /note="S -> G (in Ref. 4; AA sequence and 6; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 99 FT /note="S -> T (in Ref. 7; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 105 FT /note="I -> F (in Ref. 5; AA sequence and 6; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 106..107 FT /note="AT -> GN (in Ref. 7; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 107 FT /note="T -> V (in Ref. 6; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 113 FT /note="Y -> F (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 114..116 FT /note="DNL -> NNW (in Ref. 9; AA sequence and 10; AA FT sequence)" FT /evidence="ECO:0000305" FT CONFLICT 114..115 FT /note="DN -> QS (in Ref. 8; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 114 FT /note="D -> Y (in Ref. 5; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 115 FT /note="N -> T (in Ref. 12; AA sequence, 6; AA sequence and FT 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 116 FT /note="L -> V (in Ref. 7; AA sequence)" FT /evidence="ECO:0000305" FT NON_TER 117 FT STRAND 26..29 FT /evidence="ECO:0007829|PDB:4L1H" FT STRAND 31..35 FT /evidence="ECO:0007829|PDB:4L1H" FT STRAND 41..49 FT /evidence="ECO:0007829|PDB:4L1H" FT STRAND 55..60 FT /evidence="ECO:0007829|PDB:4L1H" FT STRAND 67..71 FT /evidence="ECO:0007829|PDB:4L1H" FT TURN 72..74 FT /evidence="ECO:0007829|PDB:4L1H" FT STRAND 84..89 FT /evidence="ECO:0007829|PDB:4L1H" FT STRAND 92..99 FT /evidence="ECO:0007829|PDB:4L1H" FT HELIX 102..104 FT /evidence="ECO:0007829|PDB:4L1H" FT STRAND 106..112 FT /evidence="ECO:0007829|PDB:4L1H" FT STRAND 114..117 FT /evidence="ECO:0007829|PDB:4L1H" SQ SEQUENCE 117 AA; 12848 MW; EE4F871C54A514FB CRC64; MDMRVPAQLL GLLLLWLSGA RCDIQMTQSP SSLSASVGDR VTITCQASQD ISNYLNWYQQ KPGKAPKLLI YDASNLETGV PSRFSGSGSG TDFTFTISSL QPEDIATYYC QQYDNLP //