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Immunoglobulin kappa variable 3-20 (Ig kappa chain V-III region B6) (Ig kappa chain V-III region GOL) (Ig kappa chain V-III region HAH) (Ig kappa chain V-III region HIC) (Ig kappa chain V-III region IARC/BL41) (Ig kappa chain V-III region NG9) (Ig kappa chain V-III region SIE) (Ig kappa chain V-III region Ti) (Ig kappa chain V-III region WOL)

 KV320_HUMAN             Reviewed;         116 AA.
P01619; A0A0B4J1Z6; P01620; P01621; P01622; P01623; P04206; P06311;
P18135; P18136;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
02-NOV-2016, sequence version 2.
25-OCT-2017, entry version 98.
RecName: Full=Immunoglobulin kappa variable 3-20 {ECO:0000303|PubMed:11549845, ECO:0000303|Ref.10};
AltName: Full=Ig kappa chain V-III region B6 {ECO:0000305|PubMed:11946339};
AltName: Full=Ig kappa chain V-III region GOL {ECO:0000305|PubMed:3086710};
AltName: Full=Ig kappa chain V-III region HAH {ECO:0000305|PubMed:3127527};
AltName: Full=Ig kappa chain V-III region HIC {ECO:0000305|PubMed:3127527};
AltName: Full=Ig kappa chain V-III region IARC/BL41 {ECO:0000305|PubMed:2997711};
AltName: Full=Ig kappa chain V-III region NG9 {ECO:0000305|PubMed:6419127};
AltName: Full=Ig kappa chain V-III region SIE {ECO:0000305|PubMed:6794615};
AltName: Full=Ig kappa chain V-III region Ti {ECO:0000305|PubMed:5027703};
AltName: Full=Ig kappa chain V-III region WOL {ECO:0000305|PubMed:6794615};
Flags: Precursor;
Name=IGKV3-20 {ECO:0000303|PubMed:11549845, ECO:0000303|Ref.10};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
PubMed=2997711; DOI=10.1093/nar/13.18.6499;
Klobeck H.G., Meindl A., Combriato G., Solomon A., Zachau H.G.;
"Human immunoglobulin kappa light chain genes of subgroups II and
Nucleic Acids Res. 13:6499-6513(1985).
PubMed=3127527; DOI=10.1084/jem.167.3.840;
Kipps T.J., Tomhave E., Chen P.P., Carson D.A.;
"Autoantibody-associated kappa light chain variable region gene
expressed in chronic lymphocytic leukemia with little or no somatic
mutation. Implications for etiology and immunotherapy.";
J. Exp. Med. 167:840-852(1988).
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
PubMed=6419127; DOI=10.1038/307077a0;
Bentley D.L.;
"Most kappa immunoglobulin mRNA in human lymphocytes is homologous to
a small family of germ-line V genes.";
Nature 307:77-80(1984).
PubMed=11946339; DOI=10.1016/0014-5793(69)80048-7;
Milstein C.;
"The basic sequences of immunoglobulin kappa chains: sequence studies
of Bence Jones proteins Rad, Fr4 and B6.";
FEBS Lett. 2:301-304(1969).
Suter L., Barnikol H.U., Watanabe S., Hilschmann N.;
"Rule of antibody structure. The primary structure of a monoclonal
immunoglobulin L-chain of kappa-type, subgroup 3 (Bence-Jones protein
Ti). IV. The complete amino acid sequence and its significance for the
mechanism of antibody production.";
Hoppe-Seyler's Z. Physiol. Chem. 353:189-208(1972).
PubMed=6794615; DOI=10.1021/bi00523a026;
Andrews D.W., Capra J.D.;
"Amino acid sequence of the variable regions of light chains from two
idiotypically cross-reactive human IgM anti-gamma-globulins of the Wa
Biochemistry 20:5816-5822(1981).
PubMed=3086710; DOI=10.1016/0161-5890(86)90049-0;
Newkirk M., Chen P.P., Carson D.A., Posnett D., Capra J.D.;
"Amino acid sequence of a light chain variable region of a human
rheumatoid factor of the Wa idiotypic group, in part predicted by its
reactivity with antipeptide antibodies.";
Mol. Immunol. 23:239-244(1986).
Lefranc M.P.;
"Nomenclature of the human immunoglobulin kappa (IGK) genes.";
Exp. Clin. Immunogenet. 18:161-174(2001).
Lefranc M.P., Lefranc G.;
"The Immunoglobulin FactsBook.";
(In) Lefranc M.P., Lefranc G. (eds.);
The Immunoglobulin FactsBook., pp.1-458, Academic Press, London.
PubMed=17576170; DOI=10.1146/annurev.genet.41.110306.130340;
Teng G., Papavasiliou F.N.;
"Immunoglobulin somatic hypermutation.";
Annu. Rev. Genet. 41:107-120(2007).
PubMed=20176268; DOI=10.1016/j.jaci.2009.09.046;
Schroeder H.W. Jr., Cavacini L.;
"Structure and function of immunoglobulins.";
J. Allergy Clin. Immunol. 125:S41-S52(2010).
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
PubMed=22158414; DOI=10.1038/nri3128;
McHeyzer-Williams M., Okitsu S., Wang N., McHeyzer-Williams L.;
"Molecular programming of B cell memory.";
Nat. Rev. Immunol. 12:24-34(2012).
PubMed=24600447; DOI=10.3389/fimmu.2014.00022;
Lefranc M.P.;
"Immunoglobulin and T Cell Receptor Genes: IMGT((R)) and the Birth and
Rise of Immunoinformatics.";
Front. Immunol. 5:22-22(2014).
-!- FUNCTION: V region of the variable domain of immunoglobulin light
chains that participates in the antigen recognition
(PubMed:24600447). Immunoglobulins, also known as antibodies, are
membrane-bound or secreted glycoproteins produced by B
lymphocytes. In the recognition phase of humoral immunity, the
membrane-bound immunoglobulins serve as receptors which, upon
binding of a specific antigen, trigger the clonal expansion and
differentiation of B lymphocytes into immunoglobulins-secreting
plasma cells. Secreted immunoglobulins mediate the effector phase
of humoral immunity, which results in the elimination of bound
antigens (PubMed:20176268, PubMed:22158414). The antigen binding
site is formed by the variable domain of one heavy chain, together
with that of its associated light chain. Thus, each immunoglobulin
has two antigen binding sites with remarkable affinity for a
particular antigen. The variable domains are assembled by a
process called V-(D)-J rearrangement and can then be subjected to
somatic hypermutations which, after exposure to antigen and
selection, allow affinity maturation for a particular antigen
(PubMed:20176268, PubMed:17576170). {ECO:0000303|PubMed:17576170,
ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414,
-!- SUBUNIT: Immunoglobulins are composed of two identical heavy
chains and two identical light chains; disulfide-linked.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268,
ECO:0000303|PubMed:22158414}. Cell membrane
{ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
-!- POLYMORPHISM: There are several alleles. The sequence shown is
that of IMGT allele IGKV3-20*01.
-!- CAUTION: For an example of a full-length immunoglobulin kappa
light chain see AC P0DOX7. {ECO:0000305}.
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};
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
EMBL; Z00021; CAA77316.1; ALT_SEQ; Genomic_DNA.
EMBL; AC245015; -; NOT_ANNOTATED_CDS; Genomic_DNA.
PIR; A01891; K3HUB6.
PIR; A01892; K3HUSI.
PIR; A01893; K3HUGO.
PIR; A01894; K3HUNG.
PIR; A01895; K3HUTI.
PIR; A01896; K3HUWL.
PIR; A01899; K3HU41.
PIR; C27594; C27594.
PIR; E30607; E30607.
PIR; PL0021; K3HUHI.
PIR; PL0022; K3HUHA.
UniGene; Hs.449609; -.
UniGene; Hs.719895; -.
PDB; 1DH5; Model; -; L=21-116.
PDB; 4LRN; X-ray; 1.89 A; L=21-116.
PDB; 4M62; X-ray; 1.80 A; L/M=21-116.
PDB; 4M8Q; X-ray; 2.89 A; B/L=21-116.
PDB; 4OB5; X-ray; 1.70 A; L=21-116.
PDB; 4ODX; X-ray; 3.10 A; B/L=21-116.
PDBsum; 1DH5; -.
PDBsum; 4LRN; -.
PDBsum; 4M62; -.
PDBsum; 4M8Q; -.
PDBsum; 4OB5; -.
PDBsum; 4ODX; -.
ProteinModelPortal; P01619; -.
SMR; P01619; -.
IntAct; P01619; 2.
MINT; MINT-202307; -.
DMDM; 125795; -.
DMDM; 125797; -.
DMDM; 125799; -.
DMDM; 125801; -.
DMDM; 125803; -.
DMDM; 125807; -.
DMDM; 125817; -.
PeptideAtlas; P01619; -.
PRIDE; P01619; -.
TopDownProteomics; P18135; -.
Ensembl; ENST00000492167; ENSP00000418649; ENSG00000239951.
Ensembl; ENST00000632822; ENSP00000487628; ENSG00000282402.
DisGeNET; 28912; -.
EuPathDB; HostDB:ENSG00000239951.1; -.
GeneCards; IGKV3-20; -.
H-InvDB; HIX0029811; -.
HGNC; HGNC:5817; IGKV3-20.
neXtProt; NX_P01619; -.
OpenTargets; ENSG00000239951; -.
GeneTree; ENSGT00780000121852; -.
HOVERGEN; HBG018013; -.
PhylomeDB; P01619; -.
Reactome; R-HSA-166663; Initial triggering of complement.
Reactome; R-HSA-173623; Classical antibody-mediated complement activation.
Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
Reactome; R-HSA-2029481; FCGR activation.
Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-HSA-2029485; Role of phospholipids in phagocytosis.
Reactome; R-HSA-2168880; Scavenging of heme from plasma.
Reactome; R-HSA-2454202; Fc epsilon receptor (FCERI) signaling.
Reactome; R-HSA-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
Reactome; R-HSA-2871796; FCERI mediated MAPK activation.
Reactome; R-HSA-2871809; FCERI mediated Ca+2 mobilization.
Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
Reactome; R-HSA-5690714; CD22 mediated BCR regulation.
Reactome; R-HSA-977606; Regulation of Complement cascade.
Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
PRO; PR:P01619; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000239951; -.
GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0071748; C:monomeric IgA immunoglobulin complex; IDA:UniProtKB.
GO; GO:0071756; C:pentameric IgM immunoglobulin complex; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0071751; C:secretory IgA immunoglobulin complex; IDA:UniProtKB.
GO; GO:0003823; F:antigen binding; NAS:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
GO; GO:0019731; P:antibacterial humoral response; IDA:UniProtKB.
GO; GO:0006956; P:complement activation; TAS:Reactome.
GO; GO:0006958; P:complement activation, classical pathway; TAS:Reactome.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
GO; GO:0003094; P:glomerular filtration; IMP:UniProtKB.
GO; GO:0006955; P:immune response; NAS:UniProtKB.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0006898; P:receptor-mediated endocytosis; TAS:Reactome.
GO; GO:0030449; P:regulation of complement activation; TAS:Reactome.
GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR003599; Ig_sub.
InterPro; IPR013106; Ig_V-set.
Pfam; PF07686; V-set; 1.
SMART; SM00409; IG; 1.
SMART; SM00406; IGv; 1.
SUPFAM; SSF48726; SSF48726; 1.
1: Evidence at protein level;
3D-structure; Adaptive immunity; Cell membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; Immunity;
Immunoglobulin domain; Immunoglobulin V region; Membrane;
Polymorphism; Reference proteome; Secreted; Signal.
SIGNAL 1 20 {ECO:0000269|PubMed:11946339,
CHAIN 21 116 Immunoglobulin kappa variable 3-20.
DOMAIN 21 >116 Ig-like. {ECO:0000255|PROSITE-
REGION 21 43 Framework-1.
REGION 44 55 Complementarity-determining-1.
REGION 56 70 Framework-2.
REGION 71 77 Complementarity-determining-2.
REGION 78 109 Framework-3.
REGION 110 >116 Complementarity-determining-3.
DISULFID 43 109 {ECO:0000255|PROSITE-ProRule:PRU00114}.
CONFLICT 17 19 DTT -> VPS (in Ref. 4). {ECO:0000305}.
CONFLICT 38 38 R -> S (in Ref. 1; CAA77316).
CONFLICT 40 40 T -> A (in Ref. 5; AA sequence).
sequence). {ECO:0000305}.
CONFLICT 49 52 VSSS -> LSGN (in Ref. 5; AA sequence).
CONFLICT 51 51 S -> N (in Ref. 7; AA sequence and 6; AA
sequence). {ECO:0000305}.
CONFLICT 52 53 SY -> N (in Ref. 1; CAA77316).
CONFLICT 52 52 S -> G (in Ref. 7; AA sequence).
CONFLICT 53 53 Y -> F (in Ref. 6; AA sequence).
CONFLICT 55 55 A -> G (in Ref. 7; AA sequence).
CONFLICT 61 61 P -> R (in Ref. 1; CAA77316).
CONFLICT 64 64 A -> S (in Ref. 1; CAA77316).
CONFLICT 69 69 I -> M (in Ref. 5; AA sequence and 8; AA
sequence). {ECO:0000305}.
CONFLICT 70 71 YG -> RD (in Ref. 1; CAA77316).
CONFLICT 71 71 G -> V (in Ref. 6; AA sequence).
CONFLICT 72 72 A -> V (in Ref. 5; AA sequence).
CONFLICT 73 73 S -> T (in Ref. 4). {ECO:0000305}.
CONFLICT 77 77 T -> N (in Ref. 1; CAA77316).
CONFLICT 87 87 G -> A (in Ref. 4). {ECO:0000305}.
CONFLICT 90 90 T -> A (in Ref. 5; AA sequence).
CONFLICT 95 95 T -> I (in Ref. 1; CAA77316).
CONFLICT 102 102 E -> D (in Ref. 7; AA sequence).
CONFLICT 113 113 G -> S (in Ref. 1; CAA77316).
CONFLICT 114 116 SSP -> NSQ (in Ref. 4). {ECO:0000305}.
CONFLICT 114 114 S -> T (in Ref. 2 and 1; CAA77316).
CONFLICT 115 116 SP -> LG (in Ref. 7; AA sequence).
NON_TER 116 116
STRAND 24 27 {ECO:0000244|PDB:4OB5}.
STRAND 29 33 {ECO:0000244|PDB:4OB5}.
STRAND 39 47 {ECO:0000244|PDB:4OB5}.
HELIX 50 52 {ECO:0000244|PDB:4OB5}.
STRAND 54 59 {ECO:0000244|PDB:4OB5}.
STRAND 66 70 {ECO:0000244|PDB:4OB5}.
TURN 71 73 {ECO:0000244|PDB:4OB5}.
STRAND 83 88 {ECO:0000244|PDB:4OB5}.
STRAND 91 98 {ECO:0000244|PDB:4OB5}.
HELIX 101 103 {ECO:0000244|PDB:4OB5}.
STRAND 105 111 {ECO:0000244|PDB:4OB5}.
STRAND 113 116 {ECO:0000244|PDB:4OB5}.
SEQUENCE 116 AA; 12557 MW; FAC198A8B24553DD CRC64;

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