ID   KVD28_HUMAN             Reviewed;         120 AA.
AC   P01615; A0A0A0MTQ6; P01616; P01617; P06309;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2016, sequence version 2.
DT   16-JAN-2019, entry version 107.
DE   RecName: Full=Immunoglobulin kappa variable 2D-28 {ECO:0000303|PubMed:11549845, ECO:0000303|Ref.8};
DE   AltName: Full=Ig kappa chain V-II region FR {ECO:0000305|PubMed:821524};
DE   AltName: Full=Ig kappa chain V-II region GM607 {ECO:0000305|PubMed:6325927};
DE   AltName: Full=Ig kappa chain V-II region MIL {ECO:0000305|Ref.3};
DE   AltName: Full=Ig kappa chain V-II region TEW {ECO:0000305|PubMed:4596149, ECO:0000305|PubMed:4700495};
DE   Flags: Precursor;
GN   Name=IGKV2D-28 {ECO:0000303|PubMed:11549845, ECO:0000303|Ref.8};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE
RP   IGKV2D-28*01).
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   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.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   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.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 4.";
RL   Nature 434:724-731(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 17-120.
RX   PubMed=6325927; DOI=10.1038/309073a0;
RA   Klobeck H.G., Solomon A., Zachau H.G.;
RT   "Contribution of human V kappa II germ-line genes to light-chain
RT   diversity.";
RL   Nature 309:73-76(1984).
RN   [3]
RP   PROTEIN SEQUENCE OF 21-120.
RA   Dreyer W.J., Gray W.R., Hood L.E.;
RT   "The genetic, molecular, and cellular basis of antibody formation:
RT   some facts and a unifying hypothesis.";
RL   Cold Spring Harb. Symp. Quant. Biol. 32:353-367(1967).
RN   [4]
RP   PROTEIN SEQUENCE OF 21-120.
RX   PubMed=4596149; DOI=10.1021/bi00743a028;
RA   Putnam F.W., Whitley E.J. Jr., Paul C., Davidson J.N.;
RT   "Amino acid sequence of a kappa Bence Jones protein from a case of
RT   primary amyloidosis.";
RL   Biochemistry 12:3763-3780(1973).
RN   [5]
RP   PROTEIN SEQUENCE OF 21-120.
RX   PubMed=821524; DOI=10.1021/bi00662a028;
RA   Riesen W.F., Jaton J.-C.;
RT   "Variable region sequence of the light chain from a Waldenstroms IgM
RT   with specificity for phosphorylcholine.";
RL   Biochemistry 15:3829-3833(1976).
RN   [6]
RP   PROTEIN SEQUENCE OF 21-47.
RX   PubMed=4700495; DOI=10.1172/JCI107295;
RA   Terry W.D., Page D.L., Kimura S., Isobe T., Osserman E.F.,
RA   Glenner G.G.;
RT   "Structural identity of Bence Jones and amyloid fibril proteins in a
RT   patient with plasma cell dyscrasia and amyloidosis.";
RL   J. Clin. Invest. 52:1276-1281(1973).
RN   [7]
RP   NOMEMCLATURE.
RX   PubMed=11549845;
RA   Lefranc M.P.;
RT   "Nomenclature of the human immunoglobulin kappa (IGK) genes.";
RL   Exp. Clin. Immunogenet. 18:161-174(2001).
RN   [8]
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.
RL   (2001).
RN   [9]
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   [10]
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   [11]
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   [12]
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
RT   Rise 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
CC       (PubMed:24600447). Immunoglobulins, also known as antibodies, are
CC       membrane-bound or secreted glycoproteins produced by B
CC       lymphocytes. In the recognition phase of humoral immunity, the
CC       membrane-bound immunoglobulins serve as receptors which, upon
CC       binding of a specific antigen, trigger the clonal expansion and
CC       differentiation of B lymphocytes into immunoglobulins-secreting
CC       plasma cells. Secreted immunoglobulins mediate the effector phase
CC       of humoral immunity, which results in the elimination of bound
CC       antigens (PubMed:20176268, PubMed:22158414). The antigen binding
CC       site is formed by the variable domain of one heavy chain, together
CC       with that of its associated light chain. Thus, each immunoglobulin
CC       has two antigen binding sites with remarkable affinity for a
CC       particular antigen. The variable domains are assembled by a
CC       process called V-(D)-J rearrangement and can then be subjected to
CC       somatic hypermutations which, after exposure to antigen and
CC       selection, allow affinity maturation for a particular antigen
CC       (PubMed:20176268, PubMed:17576170). {ECO:0000303|PubMed:17576170,
CC       ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414,
CC       ECO:0000303|PubMed:24600447}.
CC   -!- SUBUNIT: Immunoglobulins are composed of two identical heavy
CC       chains and 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
CC       that of IMGT allele IGKV2D-28*01.
CC   -!- CAUTION: For an example of a full-length immunoglobulin kappa
CC       light chain see AC P0DOX7. {ECO:0000305}.
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DR   EMBL; AC233264; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z00009; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; A01886; K2HUFR.
DR   PIR; A01887; K2HUML.
DR   PIR; A01889; K2HUGM.
DR   PIR; A90370; K2HUTW.
DR   PDB; 1DH4; Model; -; L=21-120.
DR   PDBsum; 1DH4; -.
DR   ProteinModelPortal; P01615; -.
DR   SMR; P01615; -.
DR   IntAct; P01615; 1.
DR   DrugBank; DB08562; 4-(4-STYRYL-PHENYLCARBAMOYL)-BUTYRIC ACID.
DR   IMGT_GENE-DB; IGKV2D-28; -.
DR   iPTMnet; P01615; -.
DR   PhosphoSitePlus; P01615; -.
DR   BioMuta; IGKV2D-28; -.
DR   DMDM; 125786; -.
DR   jPOST; P01615; -.
DR   PeptideAtlas; P01615; -.
DR   PRIDE; P01615; -.
DR   ProteomicsDB; 51417; -.
DR   ProteomicsDB; 51418; -.
DR   ProteomicsDB; 51419; -.
DR   ProteomicsDB; 51883; -.
DR   Ensembl; ENST00000453166; ENSP00000393492; ENSG00000242534.
DR   EuPathDB; HostDB:ENSG00000242534.2; -.
DR   GeneCards; IGKV2D-28; -.
DR   H-InvDB; HIX0161623; -.
DR   H-InvDB; HIX0197200; -.
DR   HGNC; HGNC:5799; IGKV2D-28.
DR   neXtProt; NX_P01615; -.
DR   OpenTargets; ENSG00000244116; -.
DR   GeneTree; ENSGT00940000154039; -.
DR   HOVERGEN; HBG018013; -.
DR   PhylomeDB; P01615; -.
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-977606; Regulation of Complement cascade.
DR   Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR   PRO; PR:P01615; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   Bgee; ENSG00000242534; Expressed in 83 organ(s), highest expression level in lymph node.
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:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0003823; F:antigen binding; NAS:UniProtKB.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
DR   GO; GO:0006956; P:complement activation; TAS:Reactome.
DR   GO; GO:0006958; P:complement activation, classical pathway; TAS:Reactome.
DR   GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
DR   GO; GO:0006955; P:immune response; IBA:GO_Central.
DR   GO; GO:0002377; P:immunoglobulin production; IBA:GO_Central.
DR   GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; TAS:Reactome.
DR   GO; GO:0030449; P:regulation of complement activation; TAS:Reactome.
DR   GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
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; IPR013106; Ig_V-set.
DR   Pfam; PF07686; V-set; 1.
DR   SMART; SM00406; IGv; 1.
DR   SUPFAM; SSF48726; SSF48726; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Adaptive immunity; Cell membrane; Complete proteome;
KW   Direct protein sequencing; Disulfide bond; Immunity;
KW   Immunoglobulin domain; Immunoglobulin V region; Membrane;
KW   Polymorphism; Reference proteome; Secreted; Signal.
FT   SIGNAL        1     19       {ECO:0000269|PubMed:4596149,
FT                                ECO:0000269|PubMed:4700495,
FT                                ECO:0000269|PubMed:821524,
FT                                ECO:0000269|Ref.3}.
FT   CHAIN        20    120       Immunoglobulin kappa variable 2D-28.
FT                                {ECO:0000269|PubMed:4596149,
FT                                ECO:0000269|PubMed:821524,
FT                                ECO:0000269|Ref.3}.
FT                                /FTId=PRO_0000059759.
FT   DOMAIN       20   >120       Ig-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00114}.
FT   REGION       21     43       Framework-1.
FT                                {ECO:0000303|PubMed:6325927}.
FT   REGION       44     59       Complementarity-determining-1.
FT                                {ECO:0000303|PubMed:6325927}.
FT   REGION       60     74       Framework-2.
FT                                {ECO:0000303|PubMed:6325927}.
FT   REGION       75     81       Complementarity-determining-2.
FT                                {ECO:0000303|PubMed:6325927}.
FT   REGION       82    113       Framework-3.
FT                                {ECO:0000303|PubMed:6325927}.
FT   REGION      114   >120       Complementarity-determining-3.
FT                                {ECO:0000303|PubMed:6325927}.
FT   DISULFID     43    113       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   CONFLICT     22     22       I -> V (in Ref. 5; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     24     24       M -> L (in Ref. 3; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     30     30       S -> F (in Ref. 5; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     35     35       P -> L (in Ref. 5; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     42     42       S -> Q (in Ref. 5; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     48     48       S -> N (in Ref. 3; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     50     52       LHS -> VYR (in Ref. 5; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     51     51       H -> Z (in Ref. 3; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     53     56       NGYN -> DGFD (in Ref. 4; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     55     56       YN -> BT (in Ref. 5; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     55     55       Missing (in Ref. 3; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     59     59       D -> N (in Ref. 4; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     66     66       G -> Q (in Ref. 2; Z00009).
FT                                {ECO:0000305}.
FT   CONFLICT     70     70       Q -> E (in Ref. 5; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     75     76       LG -> AL (in Ref. 4; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     76     80       GSNRA -> SSYRD (in Ref. 5; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     85     85       D -> N (in Ref. 3; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     89     89       G -> D (in Ref. 5; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    101    101       S -> T (in Ref. 5; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    104    104       E -> Q (in Ref. 5; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    116    116       A -> G (in Ref. 2; Z00009).
FT                                {ECO:0000305}.
FT   CONFLICT    117    119       LQT -> TZS (in Ref. 5; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    119    119       T -> A (in Ref. 4; AA sequence).
FT                                {ECO:0000305}.
FT   NON_TER     120    120
SQ   SEQUENCE   120 AA;  12957 MW;  0B78BEF46FFB1F97 CRC64;
     MRLPAQLLGL LMLWVSGSSG DIVMTQSPLS LPVTPGEPAS ISCRSSQSLL HSNGYNYLDW
     YLQKPGQSPQ LLIYLGSNRA SGVPDRFSGS GSGTDFTLKI SRVEAEDVGV YYCMQALQTP
//