ID KV139_HUMAN Reviewed; 117 AA. AC P01597; A0A0B4J1Z7; A0A0C4DH57; A0A0U1RVJ5; P01600; P01606; P01612; AC P04431; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 02-NOV-2016, sequence version 2. DT 16-JAN-2019, entry version 109. DE RecName: Full=Immunoglobulin kappa variable 1-39 {ECO:0000303|PubMed:11549845, ECO:0000303|Ref.8}; DE AltName: Full=Ig kappa chain V-I region DEE {ECO:0000305|PubMed:5124396}; DE AltName: Full=Ig kappa chain V-I region Hau {ECO:0000305|PubMed:4097974}; DE AltName: Full=Ig kappa chain V-I region Mev {ECO:0000305|PubMed:6816713}; DE AltName: Full=Ig kappa chain V-I region OU {ECO:0000305|PubMed:5447531}; DE AltName: Full=Ig kappa chain V-I region Walker {ECO:0000305|PubMed:6091049}; DE Flags: Precursor; GN Name=IGKV1-39 {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 [GENOMIC DNA]. RX PubMed=6091049; DOI=10.1093/nar/12.18.6995; RA Klobeck H.G., Combriato G., Zachau H.G.; RT "Immunoglobulin genes of the kappa light chain type from two human RT lymphoid cell lines are closely related."; RL Nucleic Acids Res. 12:6995-7006(1984). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE RP IGKV1-39*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 [3] RP PROTEIN SEQUENCE OF 23-117. RX PubMed=4097974; RA Watanabe S., Hilschmann N.; RT "The primary structure of a monoclonal kappa-type immunoglobulin L- RT chain of subgroup I (Bence-Jones protein Hau): subdivision within RT subgroups."; RL Hoppe-Seyler's Z. Physiol. Chem. 351:1291-1295(1970). RN [4] RP PROTEIN SEQUENCE OF 23-117. RX PubMed=5447531; DOI=10.1126/science.169.3940.56; RA Kohler H., Shimizu A., Paul C., Putnam F.W.; RT "Macroglobulin structure: variable sequence of light and heavy RT chains."; RL Science 169:56-59(1970). RN [5] RP PROTEIN SEQUENCE OF 23-117. RX PubMed=5124396; DOI=10.1042/bj1230945; RA Milstein C.P., Deverson E.V.; RT "The amino acid sequence of a human kappa light chain."; RL Biochem. J. 123:945-958(1971). RN [6] RP PROTEIN SEQUENCE OF 23-117. RX PubMed=6816713; RA Eulitz M., Linke R.P.; RT "Primary structure of the variable part of an amyloidogenic Bence- RT Jones protein (Mev). An unusual insertion in the third hypervariable RT region of a human kappa-immunoglobulin light chain."; RL Hoppe-Seyler's Z. Physiol. Chem. 363:1347-1358(1982). 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). RN [13] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 23-117, AND DISULFIDE BOND. RX PubMed=12217656; DOI=10.1016/S1047-8477(02)00015-1; RA Nymalm Y., Kravchuk Z., Salminen T., Chumanevich A.A., RA Dubnovitsky A.P., Kankare J., Pentikainen O., Lehtonen J., Arosio P., RA Martsev S., Johnson M.S.; RT "Antiferritin VL homodimer binds human spleen ferritin with high RT specificity."; RL J. Struct. Biol. 138:171-186(2002). 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 IGKV1-39*01. CC -!- CAUTION: For an example of a full-length immunoglobulin kappa CC light chain see AC P0DOX7. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA25477.1; Type=Miscellaneous discrepancy; Note==Chimeric DNA. A chimeric DNA corresponding to regions V and J of immunoglobulin kappa light chain.; Evidence={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; X00965; CAA25477.1; ALT_SEQ; Genomic_DNA. DR EMBL; AC244255; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; A01865; K1HUDE. DR PIR; A01868; K1HUHU. DR PIR; A01872; K1HUOU. DR PIR; A01879; K1HUMV. DR PIR; A01883; K1HUWK. DR PIR; A27594; A27594. DR UniGene; Hs.449609; -. DR PDB; 1DGX; Model; -; L=23-117. DR PDB; 1F6L; X-ray; 2.80 A; L=23-117. DR PDB; 3UPA; X-ray; 1.80 A; A/B=23-117. DR PDBsum; 1DGX; -. DR PDBsum; 1F6L; -. DR PDBsum; 3UPA; -. DR ProteinModelPortal; P01597; -. DR SMR; P01597; -. DR IntAct; P01597; 1. DR IMGT_GENE-DB; IGKV1-39; -. DR CarbonylDB; P01597; -. DR BioMuta; IGKV1-39; -. DR DMDM; 125779; -. DR jPOST; P01597; -. DR PeptideAtlas; P01597; -. DR PRIDE; P01597; -. DR ProteomicsDB; 51399; -. DR ProteomicsDB; 51402; -. DR ProteomicsDB; 51408; -. DR ProteomicsDB; 51414; -. DR ProteomicsDB; 51706; -. DR Ensembl; ENST00000498574; ENSP00000419058; ENSG00000242371. DR Ensembl; ENST00000631411; ENSP00000488680; ENSG00000282120. DR DisGeNET; 28930; -. DR EuPathDB; HostDB:ENSG00000242371.1; -. DR EuPathDB; HostDB:ENSG00000251546.1; -. DR GeneCards; IGKV1-39; -. DR HGNC; HGNC:5740; IGKV1-39. DR neXtProt; NX_P01597; -. DR OpenTargets; ENSG00000242371; -. DR OpenTargets; ENSG00000251546; -. DR HOVERGEN; HBG018013; -. DR OMA; YEASKLH; -. DR PhylomeDB; P01597; -. 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 ChiTaRS; IGKV1-39; human. DR PRO; PR:P01597; -. DR Proteomes; UP000005640; Chromosome 2. DR Bgee; ENSG00000242371; Expressed in 65 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; IPR003599; Ig_sub. DR InterPro; IPR013106; Ig_V-set. DR Pfam; PF07686; V-set; 1. DR SMART; SM00409; IG; 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 Reference proteome; Secreted; Signal. FT SIGNAL 1 22 {ECO:0000269|PubMed:4097974, FT ECO:0000269|PubMed:5124396, FT ECO:0000269|PubMed:5447531, FT ECO:0000269|PubMed:6816713}. FT CHAIN 23 117 Immunoglobulin kappa variable 1-39. FT {ECO:0000269|PubMed:4097974, FT ECO:0000269|PubMed:5124396, FT ECO:0000269|PubMed:5447531, FT ECO:0000269|PubMed:6816713}. FT /FTId=PRO_0000059741. FT DOMAIN 24 >117 Ig-like. {ECO:0000255|PROSITE- FT ProRule:PRU00114}. FT REGION 23 45 Framework-1. FT {ECO:0000303|PubMed:6091049}. FT REGION 46 56 Complementarity-determining-1. FT {ECO:0000303|PubMed:6091049}. FT REGION 57 71 Framework-2. FT {ECO:0000303|PubMed:6091049}. FT REGION 72 78 Complementarity-determining-2. FT {ECO:0000303|PubMed:6091049}. FT REGION 79 110 Framework-3. FT {ECO:0000303|PubMed:6091049}. FT REGION 111 >117 Complementarity-determining-3. FT {ECO:0000303|PubMed:6091049}. FT DISULFID 45 110 {ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:12217656}. FT CONFLICT 24 24 I -> D (in Ref. 6; AA sequence). FT {ECO:0000305}. FT CONFLICT 42 42 T -> I (in Ref. 6; AA sequence). FT {ECO:0000305}. FT CONFLICT 48 48 S -> G (in Ref. 5; AA sequence). FT {ECO:0000305}. FT CONFLICT 50 50 S -> T (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 51 53 ISS -> SVD (in Ref. 6; AA sequence). FT {ECO:0000305}. FT CONFLICT 51 53 ISS -> VNK (in Ref. 5; AA sequence). FT {ECO:0000305}. FT CONFLICT 53 53 S -> N (in Ref. 1; CAA25477). FT {ECO:0000305}. FT CONFLICT 56 56 N -> S (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 67 67 K -> B (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 67 67 K -> Q (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 68 68 L -> V (in Ref. 5; AA sequence and 3; AA FT sequence). {ECO:0000305}. FT CONFLICT 71 71 Y -> F (in Ref. 5; AA sequence and 6; AA FT sequence). {ECO:0000305}. FT CONFLICT 72 73 AA -> DT (in Ref. 6; AA sequence). FT {ECO:0000305}. FT CONFLICT 75 77 SLQ -> BLH (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 75 75 S -> N (in Ref. 6; AA sequence). FT {ECO:0000305}. FT CONFLICT 77 77 Q -> K (in Ref. 5; AA sequence). FT {ECO:0000305}. FT CONFLICT 77 77 Q -> P (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 81 81 P -> T (in Ref. 1; CAA25477). FT {ECO:0000305}. FT CONFLICT 87 88 SG -> GR (in Ref. 6; AA sequence). FT {ECO:0000305}. FT CONFLICT 95 95 L -> F (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 99 101 SLQ -> GLL (in Ref. 5; AA sequence). FT {ECO:0000305}. FT CONFLICT 103 103 E -> D (in Ref. 6; AA sequence). FT {ECO:0000305}. FT CONFLICT 105 105 F -> S (in Ref. 1; CAA25477). FT {ECO:0000305}. FT CONFLICT 113 115 SYS -> NYI (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 115 115 S -> T (in Ref. 5; AA sequence and 6; AA FT sequence). {ECO:0000305}. FT CONFLICT 116 116 T -> N (in Ref. 6; AA sequence). FT {ECO:0000305}. FT CONFLICT 116 116 T -> S (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 117 117 P -> L (in Ref. 1; CAA25477). FT {ECO:0000305}. FT NON_TER 117 117 FT STRAND 26 29 {ECO:0000244|PDB:3UPA}. FT STRAND 31 35 {ECO:0000244|PDB:3UPA}. FT STRAND 41 49 {ECO:0000244|PDB:3UPA}. FT STRAND 55 60 {ECO:0000244|PDB:3UPA}. FT STRAND 67 71 {ECO:0000244|PDB:3UPA}. FT TURN 72 74 {ECO:0000244|PDB:3UPA}. FT STRAND 84 89 {ECO:0000244|PDB:3UPA}. FT STRAND 92 99 {ECO:0000244|PDB:3UPA}. FT HELIX 102 104 {ECO:0000244|PDB:3UPA}. FT STRAND 106 112 {ECO:0000244|PDB:3UPA}. FT STRAND 114 117 {ECO:0000244|PDB:3UPA}. SQ SEQUENCE 117 AA; 12737 MW; ED1DC5B0055AB9D4 CRC64; MDMRVPAQLL GLLLLWLRGA RCDIQMTQSP SSLSASVGDR VTITCRASQS ISSYLNWYQQ KPGKAPKLLI YAASSLQSGV PSRFSGSGSG TDFTLTISSL QPEDFATYYC QQSYSTP //