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Immunoglobulin kappa variable 2D-28 (Ig kappa chain V-II region FR) (Ig kappa chain V-II region GM607) (Ig kappa chain V-II region MIL) (Ig kappa chain V-II region TEW)

 KVD28_HUMAN             Reviewed;         120 AA.
P01615; A0A0A0MTQ6; P01616; P01617; P06309;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
02-NOV-2016, sequence version 2.
16-JAN-2019, entry version 107.
RecName: Full=Immunoglobulin kappa variable 2D-28 {ECO:0000303|PubMed:11549845, ECO:0000303|Ref.8};
AltName: Full=Ig kappa chain V-II region FR {ECO:0000305|PubMed:821524};
AltName: Full=Ig kappa chain V-II region GM607 {ECO:0000305|PubMed:6325927};
AltName: Full=Ig kappa chain V-II region MIL {ECO:0000305|Ref.3};
AltName: Full=Ig kappa chain V-II region TEW {ECO:0000305|PubMed:4596149, ECO:0000305|PubMed:4700495};
Flags: Precursor;
Name=IGKV2D-28 {ECO:0000303|PubMed:11549845, ECO:0000303|Ref.8};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
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=6325927; DOI=10.1038/309073a0;
Klobeck H.G., Solomon A., Zachau H.G.;
"Contribution of human V kappa II germ-line genes to light-chain
Nature 309:73-76(1984).
Dreyer W.J., Gray W.R., Hood L.E.;
"The genetic, molecular, and cellular basis of antibody formation:
some facts and a unifying hypothesis.";
Cold Spring Harb. Symp. Quant. Biol. 32:353-367(1967).
PubMed=4596149; DOI=10.1021/bi00743a028;
Putnam F.W., Whitley E.J. Jr., Paul C., Davidson J.N.;
"Amino acid sequence of a kappa Bence Jones protein from a case of
primary amyloidosis.";
Biochemistry 12:3763-3780(1973).
PubMed=821524; DOI=10.1021/bi00662a028;
Riesen W.F., Jaton J.-C.;
"Variable region sequence of the light chain from a Waldenstroms IgM
with specificity for phosphorylcholine.";
Biochemistry 15:3829-3833(1976).
PubMed=4700495; DOI=10.1172/JCI107295;
Terry W.D., Page D.L., Kimura S., Isobe T., Osserman E.F.,
Glenner G.G.;
"Structural identity of Bence Jones and amyloid fibril proteins in a
patient with plasma cell dyscrasia and amyloidosis.";
J. Clin. Invest. 52:1276-1281(1973).
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=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 IGKV2D-28*01.
-!- CAUTION: For an example of a full-length immunoglobulin kappa
light chain see AC P0DOX7. {ECO:0000305}.
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
EMBL; AC233264; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z00009; -; NOT_ANNOTATED_CDS; Genomic_DNA.
PIR; A01886; K2HUFR.
PIR; A01887; K2HUML.
PIR; A01889; K2HUGM.
PIR; A90370; K2HUTW.
PDB; 1DH4; Model; -; L=21-120.
PDBsum; 1DH4; -.
ProteinModelPortal; P01615; -.
SMR; P01615; -.
IntAct; P01615; 1.
iPTMnet; P01615; -.
PhosphoSitePlus; P01615; -.
BioMuta; IGKV2D-28; -.
DMDM; 125786; -.
jPOST; P01615; -.
PeptideAtlas; P01615; -.
PRIDE; P01615; -.
ProteomicsDB; 51417; -.
ProteomicsDB; 51418; -.
ProteomicsDB; 51419; -.
ProteomicsDB; 51883; -.
Ensembl; ENST00000453166; ENSP00000393492; ENSG00000242534.
EuPathDB; HostDB:ENSG00000242534.2; -.
GeneCards; IGKV2D-28; -.
H-InvDB; HIX0161623; -.
H-InvDB; HIX0197200; -.
HGNC; HGNC:5799; IGKV2D-28.
neXtProt; NX_P01615; -.
OpenTargets; ENSG00000244116; -.
GeneTree; ENSGT00940000154039; -.
HOVERGEN; HBG018013; -.
PhylomeDB; P01615; -.
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:P01615; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000242534; Expressed in 83 organ(s), highest expression level in lymph node.
GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0003823; F:antigen binding; NAS:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
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:0006955; P:immune response; IBA:GO_Central.
GO; GO:0002377; P:immunoglobulin production; IBA:GO_Central.
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.
Gene3D;; -; 1.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013106; Ig_V-set.
Pfam; PF07686; V-set; 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 19 {ECO:0000269|PubMed:4596149,
CHAIN 20 120 Immunoglobulin kappa variable 2D-28.
DOMAIN 20 >120 Ig-like. {ECO:0000255|PROSITE-
REGION 21 43 Framework-1.
REGION 44 59 Complementarity-determining-1.
REGION 60 74 Framework-2.
REGION 75 81 Complementarity-determining-2.
REGION 82 113 Framework-3.
REGION 114 >120 Complementarity-determining-3.
DISULFID 43 113 {ECO:0000255|PROSITE-ProRule:PRU00114}.
CONFLICT 22 22 I -> V (in Ref. 5; AA sequence).
CONFLICT 24 24 M -> L (in Ref. 3; AA sequence).
CONFLICT 30 30 S -> F (in Ref. 5; AA sequence).
CONFLICT 35 35 P -> L (in Ref. 5; AA sequence).
CONFLICT 42 42 S -> Q (in Ref. 5; AA sequence).
CONFLICT 48 48 S -> N (in Ref. 3; AA sequence).
CONFLICT 50 52 LHS -> VYR (in Ref. 5; AA sequence).
CONFLICT 51 51 H -> Z (in Ref. 3; AA sequence).
CONFLICT 53 56 NGYN -> DGFD (in Ref. 4; AA sequence).
CONFLICT 55 56 YN -> BT (in Ref. 5; AA sequence).
CONFLICT 55 55 Missing (in Ref. 3; AA sequence).
CONFLICT 59 59 D -> N (in Ref. 4; AA sequence).
CONFLICT 66 66 G -> Q (in Ref. 2; Z00009).
CONFLICT 70 70 Q -> E (in Ref. 5; AA sequence).
CONFLICT 75 76 LG -> AL (in Ref. 4; AA sequence).
CONFLICT 76 80 GSNRA -> SSYRD (in Ref. 5; AA sequence).
CONFLICT 85 85 D -> N (in Ref. 3; AA sequence).
CONFLICT 89 89 G -> D (in Ref. 5; AA sequence).
CONFLICT 101 101 S -> T (in Ref. 5; AA sequence).
CONFLICT 104 104 E -> Q (in Ref. 5; AA sequence).
CONFLICT 116 116 A -> G (in Ref. 2; Z00009).
CONFLICT 117 119 LQT -> TZS (in Ref. 5; AA sequence).
CONFLICT 119 119 T -> A (in Ref. 4; AA sequence).
NON_TER 120 120
SEQUENCE 120 AA; 12957 MW; 0B78BEF46FFB1F97 CRC64;

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