ID   KV320_HUMAN             Reviewed;         116 AA.
AC   P01619; A0A0B4J1Z6; P01620; P01621; P01622; P01623; P04206; P06311; P18135;
AC   P18136;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2016, sequence version 2.
DT   27-MAR-2024, entry version 133.
DE   RecName: Full=Immunoglobulin kappa variable 3-20 {ECO:0000303|PubMed:11549845, ECO:0000303|Ref.10};
DE   AltName: Full=Ig kappa chain V-III region B6 {ECO:0000305|PubMed:11946339};
DE   AltName: Full=Ig kappa chain V-III region GOL {ECO:0000305|PubMed:3086710};
DE   AltName: Full=Ig kappa chain V-III region HAH {ECO:0000305|PubMed:3127527};
DE   AltName: Full=Ig kappa chain V-III region HIC {ECO:0000305|PubMed:3127527};
DE   AltName: Full=Ig kappa chain V-III region IARC/BL41 {ECO:0000305|PubMed:2997711};
DE   AltName: Full=Ig kappa chain V-III region NG9 {ECO:0000305|PubMed:6419127};
DE   AltName: Full=Ig kappa chain V-III region SIE {ECO:0000305|PubMed:6794615};
DE   AltName: Full=Ig kappa chain V-III region Ti {ECO:0000305|PubMed:5027703};
DE   AltName: Full=Ig kappa chain V-III region WOL {ECO:0000305|PubMed:6794615};
DE   Flags: Precursor;
GN   Name=IGKV3-20 {ECO:0000303|PubMed:11549845, ECO:0000303|Ref.10};
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=2997711; DOI=10.1093/nar/13.18.6499;
RA   Klobeck H.G., Meindl A., Combriato G., Solomon A., Zachau H.G.;
RT   "Human immunoglobulin kappa light chain genes of subgroups II and III.";
RL   Nucleic Acids Res. 13:6499-6513(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3127527; DOI=10.1084/jem.167.3.840;
RA   Kipps T.J., Tomhave E., Chen P.P., Carson D.A.;
RT   "Autoantibody-associated kappa light chain variable region gene expressed
RT   in chronic lymphocytic leukemia with little or no somatic mutation.
RT   Implications for etiology and immunotherapy.";
RL   J. Exp. Med. 167:840-852(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE IGKV3-20*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   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 17-116.
RX   PubMed=6419127; DOI=10.1038/307077a0;
RA   Bentley D.L.;
RT   "Most kappa immunoglobulin mRNA in human lymphocytes is homologous to a
RT   small family of germ-line V genes.";
RL   Nature 307:77-80(1984).
RN   [5]
RP   PROTEIN SEQUENCE OF 21-116.
RX   PubMed=11946339; DOI=10.1016/0014-5793(69)80048-7;
RA   Milstein C.;
RT   "The basic sequences of immunoglobulin kappa chains: sequence studies of
RT   Bence Jones proteins Rad, Fr4 and B6.";
RL   FEBS Lett. 2:301-304(1969).
RN   [6]
RP   PROTEIN SEQUENCE OF 21-116.
RX   PubMed=5027703;
RA   Suter L., Barnikol H.U., Watanabe S., Hilschmann N.;
RT   "Rule of antibody structure. The primary structure of a monoclonal
RT   immunoglobulin L-chain of kappa-type, subgroup 3 (Bence-Jones protein Ti).
RT   IV. The complete amino acid sequence and its significance for the mechanism
RT   of antibody production.";
RL   Hoppe-Seyler's Z. Physiol. Chem. 353:189-208(1972).
RN   [7]
RP   PROTEIN SEQUENCE OF 21-116.
RX   PubMed=6794615; DOI=10.1021/bi00523a026;
RA   Andrews D.W., Capra J.D.;
RT   "Amino acid sequence of the variable regions of light chains from two
RT   idiotypically cross-reactive human IgM anti-gamma-globulins of the Wa
RT   group.";
RL   Biochemistry 20:5816-5822(1981).
RN   [8]
RP   PROTEIN SEQUENCE OF 21-116.
RX   PubMed=3086710; DOI=10.1016/0161-5890(86)90049-0;
RA   Newkirk M., Chen P.P., Carson D.A., Posnett D., Capra J.D.;
RT   "Amino acid sequence of a light chain variable region of a human rheumatoid
RT   factor of the Wa idiotypic group, in part predicted by its reactivity with
RT   antipeptide antibodies.";
RL   Mol. Immunol. 23:239-244(1986).
RN   [9]
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   [10]
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   [11]
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   [12]
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   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [14]
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   [15]
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: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 IGKV3-20*01.
CC   -!- CAUTION: For an example of a full-length immunoglobulin kappa light
CC       chain see AC P0DOX7. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA77316.1; Type=Miscellaneous discrepancy; Note=Chimeric DNA. A chimeric DNA corresponding to regions V and J of immunoglobulin kappa light chain.; Evidence={ECO:0000305};
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DR   EMBL; Z00021; CAA77316.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC245015; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; A01891; K3HUB6.
DR   PIR; A01892; K3HUSI.
DR   PIR; A01893; K3HUGO.
DR   PIR; A01894; K3HUNG.
DR   PIR; A01895; K3HUTI.
DR   PIR; A01896; K3HUWL.
DR   PIR; A01899; K3HU41.
DR   PIR; C27594; C27594.
DR   PIR; E30607; E30607.
DR   PIR; PL0021; K3HUHI.
DR   PIR; PL0022; K3HUHA.
DR   PDB; 4LRN; X-ray; 1.89 A; L=21-116.
DR   PDB; 4M62; X-ray; 1.80 A; L/M=21-116.
DR   PDB; 4M8Q; X-ray; 2.89 A; B/L=21-116.
DR   PDB; 4OB5; X-ray; 1.70 A; L=21-116.
DR   PDB; 4ODX; X-ray; 3.10 A; B/L=21-116.
DR   PDBsum; 4LRN; -.
DR   PDBsum; 4M62; -.
DR   PDBsum; 4M8Q; -.
DR   PDBsum; 4OB5; -.
DR   PDBsum; 4ODX; -.
DR   AlphaFoldDB; P01619; -.
DR   EMDB; EMD-13415; -.
DR   EMDB; EMD-13869; -.
DR   EMDB; EMD-14887; -.
DR   EMDB; EMD-15269; -.
DR   EMDB; EMD-15270; -.
DR   EMDB; EMD-15271; -.
DR   EMDB; EMD-15273; -.
DR   EMDB; EMD-21864; -.
DR   EMDB; EMD-21865; -.
DR   EMDB; EMD-22659; -.
DR   EMDB; EMD-22660; -.
DR   EMDB; EMD-22668; -.
DR   EMDB; EMD-23579; -.
DR   EMDB; EMD-23580; -.
DR   EMDB; EMD-23582; -.
DR   EMDB; EMD-23816; -.
DR   EMDB; EMD-24190; -.
DR   EMDB; EMD-24236; -.
DR   EMDB; EMD-24649; -.
DR   EMDB; EMD-24695; -.
DR   EMDB; EMD-24696; -.
DR   EMDB; EMD-25039; -.
DR   EMDB; EMD-25040; -.
DR   EMDB; EMD-25263; -.
DR   EMDB; EMD-25265; -.
DR   EMDB; EMD-25266; -.
DR   EMDB; EMD-25733; -.
DR   EMDB; EMD-25794; -.
DR   EMDB; EMD-25808; -.
DR   EMDB; EMD-25992; -.
DR   EMDB; EMD-27270; -.
DR   EMDB; EMD-27318; -.
DR   EMDB; EMD-27798; -.
DR   EMDB; EMD-27799; -.
DR   EMDB; EMD-28729; -.
DR   EMDB; EMD-32422; -.
DR   EMDB; EMD-32423; -.
DR   EMDB; EMD-32444; -.
DR   EMDB; EMD-32445; -.
DR   EMDB; EMD-32446; -.
DR   EMDB; EMD-32447; -.
DR   EMDB; EMD-32839; -.
DR   EMDB; EMD-33220; -.
DR   EMDB; EMD-33221; -.
DR   EMDB; EMD-33222; -.
DR   EMDB; EMD-33709; -.
DR   EMDB; EMD-33892; -.
DR   EMDB; EMD-34228; -.
DR   EMDB; EMD-40273; -.
DR   EMDB; EMD-6793; -.
DR   EMDB; EMD-7089; -.
DR   EMDB; EMD-7460; -.
DR   EMDB; EMD-7621; -.
DR   EMDB; EMD-7622; -.
DR   EMDB; EMD-7859; -.
DR   EMDB; EMD-7861; -.
DR   EMDB; EMD-7862; -.
DR   EMDB; EMD-7863; -.
DR   EMDB; EMD-7864; -.
DR   EMDB; EMD-7865; -.
DR   EMDB; EMD-7866; -.
DR   EMDB; EMD-9189; -.
DR   EMDB; EMD-9319; -.
DR   EMDB; EMD-9320; -.
DR   SMR; P01619; -.
DR   IntAct; P01619; 5.
DR   MINT; P01619; -.
DR   DrugBank; DB09130; Copper.
DR   DrugBank; DB01593; Zinc.
DR   DrugBank; DB14487; Zinc acetate.
DR   IMGT_GENE-DB; IGKV3-20; -.
DR   BioMuta; IGKV3-20; -.
DR   DMDM; 125801; -.
DR   jPOST; P01619; -.
DR   MassIVE; P01619; -.
DR   PeptideAtlas; P01619; -.
DR   PRIDE; P01619; -.
DR   Pumba; P01619; -.
DR   TopDownProteomics; P01619; -.
DR   Ensembl; ENST00000492167.1; ENSP00000418649.1; ENSG00000239951.1.
DR   Ensembl; ENST00000632822.1; ENSP00000487628.1; ENSG00000282402.1.
DR   AGR; HGNC:5817; -.
DR   GeneCards; IGKV3-20; -.
DR   HGNC; HGNC:5817; IGKV3-20.
DR   HPA; ENSG00000239951; Tissue enhanced (intestine, lymphoid tissue).
DR   neXtProt; NX_P01619; -.
DR   OpenTargets; ENSG00000239951; -.
DR   VEuPathDB; HostDB:ENSG00000239951; -.
DR   GeneTree; ENSGT00940000154413; -.
DR   InParanoid; P01619; -.
DR   OMA; ADYYCEH; -.
DR   PhylomeDB; P01619; -.
DR   PathwayCommons; P01619; -.
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; P01619; -.
DR   Pharos; P01619; Tbio.
DR   PRO; PR:P01619; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; P01619; Protein.
DR   Bgee; ENSG00000239951; Expressed in rectum and 89 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; IDA:UniProtKB.
DR   GO; GO:0071748; C:monomeric IgA immunoglobulin complex; IDA:UniProtKB.
DR   GO; GO:0071756; C:pentameric IgM immunoglobulin complex; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0071751; C:secretory IgA immunoglobulin complex; IDA:UniProtKB.
DR   GO; GO:0003823; F:antigen binding; NAS:UniProtKB.
DR   GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR   GO; GO:0019731; P:antibacterial humoral response; IDA:UniProtKB.
DR   GO; GO:0003094; P:glomerular filtration; IMP:UniProtKB.
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:SF472; IMMUNOGLOBULIN KAPPA VARIABLE 3-20-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..20
FT                   /evidence="ECO:0000269|PubMed:11946339,
FT                   ECO:0000269|PubMed:3086710, ECO:0000269|PubMed:5027703,
FT                   ECO:0000269|PubMed:6794615"
FT   CHAIN           21..116
FT                   /note="Immunoglobulin kappa variable 3-20"
FT                   /evidence="ECO:0000269|PubMed:11946339,
FT                   ECO:0000269|PubMed:3086710, ECO:0000269|PubMed:5027703,
FT                   ECO:0000269|PubMed:6794615"
FT                   /id="PRO_0000059762"
FT   DOMAIN          21..>116
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   REGION          21..43
FT                   /note="Framework-1"
FT                   /evidence="ECO:0000303|PubMed:2997711"
FT   REGION          44..55
FT                   /note="Complementarity-determining-1"
FT                   /evidence="ECO:0000303|PubMed:2997711"
FT   REGION          56..70
FT                   /note="Framework-2"
FT                   /evidence="ECO:0000303|PubMed:2997711"
FT   REGION          71..77
FT                   /note="Complementarity-determining-2"
FT                   /evidence="ECO:0000303|PubMed:2997711"
FT   REGION          78..109
FT                   /note="Framework-3"
FT                   /evidence="ECO:0000303|PubMed:2997711"
FT   REGION          110..>116
FT                   /note="Complementarity-determining-3"
FT                   /evidence="ECO:0000303|PubMed:2997711"
FT   DISULFID        43..109
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   CONFLICT        17..19
FT                   /note="DTT -> VPS (in Ref. 4)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        38
FT                   /note="R -> S (in Ref. 1; CAA77316)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        40
FT                   /note="T -> A (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        46..52
FT                   /note="SQSVSSS -> ALLSSRG (in Ref. 8; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        49..52
FT                   /note="VSSS -> LSGN (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        51
FT                   /note="S -> N (in Ref. 7; AA sequence and 6; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        52..53
FT                   /note="SY -> N (in Ref. 1; CAA77316)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        52
FT                   /note="S -> G (in Ref. 7; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        53
FT                   /note="Y -> F (in Ref. 6; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        55
FT                   /note="A -> G (in Ref. 7; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        61
FT                   /note="P -> R (in Ref. 1; CAA77316)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        64
FT                   /note="A -> S (in Ref. 1; CAA77316)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        69
FT                   /note="I -> M (in Ref. 5; AA sequence and 8; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        70..71
FT                   /note="YG -> RD (in Ref. 1; CAA77316)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        71
FT                   /note="G -> V (in Ref. 6; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        72
FT                   /note="A -> V (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        73
FT                   /note="S -> T (in Ref. 4)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        77
FT                   /note="T -> N (in Ref. 1; CAA77316)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        87
FT                   /note="G -> A (in Ref. 4)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        90
FT                   /note="T -> A (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        95
FT                   /note="T -> I (in Ref. 1; CAA77316)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        102
FT                   /note="E -> D (in Ref. 7; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        113
FT                   /note="G -> S (in Ref. 1; CAA77316)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        114..116
FT                   /note="SSP -> NSQ (in Ref. 4)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        114
FT                   /note="S -> T (in Ref. 2 and 1; CAA77316)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        115..116
FT                   /note="SP -> LG (in Ref. 7; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   NON_TER         116
FT   STRAND          24..27
FT                   /evidence="ECO:0007829|PDB:4OB5"
FT   STRAND          29..33
FT                   /evidence="ECO:0007829|PDB:4OB5"
FT   STRAND          39..47
FT                   /evidence="ECO:0007829|PDB:4OB5"
FT   HELIX           50..52
FT                   /evidence="ECO:0007829|PDB:4OB5"
FT   STRAND          54..59
FT                   /evidence="ECO:0007829|PDB:4OB5"
FT   STRAND          66..70
FT                   /evidence="ECO:0007829|PDB:4OB5"
FT   TURN            71..73
FT                   /evidence="ECO:0007829|PDB:4OB5"
FT   STRAND          83..88
FT                   /evidence="ECO:0007829|PDB:4OB5"
FT   STRAND          91..98
FT                   /evidence="ECO:0007829|PDB:4OB5"
FT   HELIX           101..103
FT                   /evidence="ECO:0007829|PDB:4OB5"
FT   STRAND          105..111
FT                   /evidence="ECO:0007829|PDB:4OB5"
FT   STRAND          113..116
FT                   /evidence="ECO:0007829|PDB:4OB5"
SQ   SEQUENCE   116 AA;  12557 MW;  FAC198A8B24553DD CRC64;
     METPAQLLFL LLLWLPDTTG EIVLTQSPGT LSLSPGERAT LSCRASQSVS SSYLAWYQQK
     PGQAPRLLIY GASSRATGIP DRFSGSGSGT DFTLTISRLE PEDFAVYYCQ QYGSSP
//