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 02-SEP-2026, entry version 142. 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; 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 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., 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 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: some RT 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 primary RT 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 with RT 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., 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; 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 [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. (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 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:17576170, PubMed:20176268). 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 IGKV2D-28*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 EMBL; Z00009; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; A01886; K2HUFR. DR PIR; A01887; K2HUML. DR PIR; A01889; K2HUGM. DR PIR; A90370; K2HUTW. DR AlphaFoldDB; P01615; -. DR EMDB; EMD-13549; -. DR EMDB; EMD-27318; -. DR EMDB; EMD-32753; -. DR EMDB; EMD-41422; -. DR EMDB; EMD-41441; -. DR EMDB; EMD-48093; -. DR EMDB; EMD-48101; -. DR EMDB; EMD-48102; -. DR EMDB; EMD-48510; -. DR EMDB; EMD-48511; -. DR EMDB; EMD-48512; -. DR EMDB; EMD-48518; -. DR EMDB; EMD-60391; -. DR EMDB; EMD-60395; -. DR EMDB; EMD-60396; -. DR EMDB; EMD-60403; -. DR EMDB; EMD-64667; -. DR EMDB; EMD-70108; -. DR EMDB; EMD-70111; -. DR EMDB; EMD-70264; -. DR EMDB; EMD-70773; -. DR EMDB; EMD-71259; -. DR EMDB; EMD-9378; -. DR SMR; P01615; -. DR FunCoup; P01615; 358. DR IntAct; P01615; 6. DR DrugBank; DB08562; 4-(4-STYRYL-PHENYLCARBAMOYL)-BUTYRIC ACID. DR IMGT_GENE-DB; IGKV2D-28; -. DR GlyGen; P01615; 1 site. DR iPTMnet; P01615; -. DR PhosphoSitePlus; P01615; -. DR BioMuta; IGKV2D-28; -. DR DMDM; 125786; -. DR jPOST; P01615; -. DR MassIVE; P01615; -. DR PRIDE; P01615; -. DR Ensembl; ENST00000453166.2; ENSP00000393492.2; ENSG00000242534.3. DR Ensembl; ENST00000482769.1; ENSP00000419353.1; ENSG00000244116.3. DR Ensembl; ENST00000633682.1; ENSP00000487690.1; ENSG00000282025.1. DR AGR; HGNC:5799; -. DR GeneCards; IGKV2D-28; -. DR HGNC; HGNC:5799; IGKV2D-28. DR HPA; ENSG00000242534; Tissue enhanced (intestine, lymphoid tissue, salivary gland). DR OpenTargets; ENSG00000244116; -. DR VEuPathDB; HostDB:ENSG00000242534; -. DR GeneTree; ENSGT00940000154039; -. DR InParanoid; P01615; -. DR OMA; WQGTHIP; -. DR OrthoDB; 9519958at2759; -. DR PAN-GO; P01615; 2 GO annotations based on evolutionary models. DR PhylomeDB; P01615; -. DR PathwayCommons; 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-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; P01615; -. DR Agora; ENSG00000242534; -. DR Pharos; P01615; Tdark. DR PRO; PR:P01615; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; P01615; protein. DR Bgee; ENSG00000242534; Expressed in duodenum 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:0019814; C:immunoglobulin complex; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0003823; F:antigen binding; NAS:UniProtKB. DR GO; GO:0006955; P:immune response; IBA:GO_Central. DR FunFam; 2.60.40.10:FF:000365; If kappa light chain; 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; IPR013106; Ig_V-set. DR InterPro; IPR050150; IgV_Light_Chain. DR PANTHER; PTHR23267; IMMUNOGLOBULIN LIGHT CHAIN; 1. DR Pfam; PF07686; V-set; 1. DR SMART; SM00406; IGv; 1. DR SUPFAM; SSF48726; Immunoglobulin; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 1: Evidence at protein level; KW Adaptive immunity; Cell membrane; Direct protein sequencing; KW Disulfide bond; Immunity; Immunoglobulin; Immunoglobulin domain; Membrane; KW Reference proteome; Secreted; Signal. FT SIGNAL 1..19 FT /evidence="ECO:0000269|PubMed:4596149, FT ECO:0000269|PubMed:4700495, ECO:0000269|PubMed:821524, FT ECO:0000269|Ref.3" FT CHAIN 20..120 FT /note="Immunoglobulin kappa variable 2D-28" FT /evidence="ECO:0000269|PubMed:4596149, FT ECO:0000269|PubMed:821524, ECO:0000269|Ref.3" FT /id="PRO_0000059759" FT DOMAIN 20..>120 FT /note="Ig-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT REGION 21..43 FT /note="Framework-1" FT /evidence="ECO:0000250|UniProtKB:P01602" FT REGION 44..59 FT /note="Complementarity-determining-1" FT /evidence="ECO:0000250|UniProtKB:P01602" FT REGION 60..74 FT /note="Framework-2" FT /evidence="ECO:0000250|UniProtKB:P01602" FT REGION 75..81 FT /note="Complementarity-determining-2" FT /evidence="ECO:0000250|UniProtKB:P01602" FT REGION 82..113 FT /note="Framework-3" FT /evidence="ECO:0000250|UniProtKB:P01602" FT REGION 114..>120 FT /note="Complementarity-determining-3" FT /evidence="ECO:0000250|UniProtKB:P01602" FT DISULFID 43..113 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT CONFLICT 22 FT /note="I -> V (in Ref. 5; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 24 FT /note="M -> L (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 30 FT /note="S -> F (in Ref. 5; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 35 FT /note="P -> L (in Ref. 5; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 42 FT /note="S -> Q (in Ref. 5; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 48 FT /note="S -> N (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 50..52 FT /note="LHS -> VYR (in Ref. 5; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 51 FT /note="H -> Z (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 53..56 FT /note="NGYN -> DGFD (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 55..56 FT /note="YN -> BT (in Ref. 5; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 55 FT /note="Missing (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 59 FT /note="D -> N (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 66 FT /note="G -> Q (in Ref. 2; Z00009)" FT /evidence="ECO:0000305" FT CONFLICT 70 FT /note="Q -> E (in Ref. 5; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 75..76 FT /note="LG -> AL (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 76..80 FT /note="GSNRA -> SSYRD (in Ref. 5; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 85 FT /note="D -> N (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 89 FT /note="G -> D (in Ref. 5; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 101 FT /note="S -> T (in Ref. 5; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 104 FT /note="E -> Q (in Ref. 5; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 116 FT /note="A -> G (in Ref. 2; Z00009)" FT /evidence="ECO:0000305" FT CONFLICT 117..119 FT /note="LQT -> TZS (in Ref. 5; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 119 FT /note="T -> A (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT NON_TER 120 SQ SEQUENCE 120 AA; 12957 MW; 0B78BEF46FFB1F97 CRC64; MRLPAQLLGL LMLWVSGSSG DIVMTQSPLS LPVTPGEPAS ISCRSSQSLL HSNGYNYLDW YLQKPGQSPQ LLIYLGSNRA SGVPDRFSGS GSGTDFTLKI SRVEAEDVGV YYCMQALQTP //