ID KV117_HUMAN Reviewed; 117 AA. AC P01599; A0A0B4J1Z4; P01610; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 05-OCT-2016, sequence version 2. DT 16-JAN-2019, entry version 112. DE RecName: Full=Immunoglobulin kappa variable 1-17 {ECO:0000303|PubMed:11549845, ECO:0000303|Ref.5}; DE AltName: Full=Ig kappa chain V-I region Gal {ECO:0000305|PubMed:4215718}; DE AltName: Full=Ig kappa chain V-I region WEA {ECO:0000305|PubMed:6410398}; DE Flags: Precursor; GN Name=IGKV1-17 {ECO:0000303|PubMed:11549845, ECO:0000303|Ref.5}; 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 IGKV1-17*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 PROTEIN SEQUENCE OF 23-117. RX PubMed=4215718; RA Laure C.J., Watanabe S., Hilschmann N.; RT "The primary structure of a monoclonal IgM-immunoglobulin RT (macroglobulin Gal.), I. The amino acid sequence of the L-chain of RT kappa-type, subgroup I."; RL Hoppe-Seyler's Z. Physiol. Chem. 354:1503-1504(1973). RN [3] RP PROTEIN SEQUENCE OF 23-117. RX PubMed=6410398; DOI=10.1073/pnas.80.15.4837; RA Goni F., Frangione B.; RT "Amino acid sequence of the Fv region of a human monoclonal IgM RT (protein WEA) with antibody activity against 3,4-pyruvylated galactose RT in Klebsiella polysaccharides K30 and K33."; RL Proc. Natl. Acad. Sci. U.S.A. 80:4837-4841(1983). RN [4] 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 [5] 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 [6] 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 [7] 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 [8] 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 [9] 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 IGKV1-17*01. CC -!- CAUTION: For an example of a full-length immunoglobulin kappa CC light 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; AC245015; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; A01867; K1HUGL. DR PIR; A01876; K1HUWE. DR ProteinModelPortal; P01599; -. DR SMR; P01599; -. DR IMGT_GENE-DB; IGKV1-17; -. DR BioMuta; IGKV1-17; -. DR DMDM; 125763; -. DR PeptideAtlas; P01599; -. DR PRIDE; P01599; -. DR ProteomicsDB; 51401; -. DR ProteomicsDB; 51412; -. DR Ensembl; ENST00000490686; ENSP00000418357; ENSG00000240382. DR Ensembl; ENST00000632229; ENSP00000488092; ENSG00000281978. DR EuPathDB; HostDB:ENSG00000240382.3; -. DR GeneCards; IGKV1-17; -. DR HGNC; HGNC:5733; IGKV1-17. DR neXtProt; NX_P01599; -. DR OpenTargets; ENSG00000240382; -. DR GeneTree; ENSGT00940000153048; -. DR HOVERGEN; HBG018013; -. DR OMA; CHASQSI; -. DR PhylomeDB; P01599; -. 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:P01599; -. DR Proteomes; UP000005640; Chromosome 2. DR Bgee; ENSG00000240382; Expressed in 81 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 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 22 {ECO:0000269|PubMed:4215718, FT ECO:0000269|PubMed:6410398}. FT CHAIN 23 117 Immunoglobulin kappa variable 1-17. FT {ECO:0000269|PubMed:4215718, FT ECO:0000269|PubMed:6410398}. FT /FTId=PRO_0000059743. FT DOMAIN 24 >117 Ig-like. {ECO:0000255|PROSITE- FT ProRule:PRU00114}. FT REGION 23 45 Framework-1. FT {ECO:0000250|UniProtKB:P01602}. FT REGION 46 56 Complementarity-determining-1. FT {ECO:0000250|UniProtKB:P01602}. FT REGION 57 71 Framework-2. FT {ECO:0000250|UniProtKB:P01602}. FT REGION 72 78 Complementarity-determining-2. FT {ECO:0000250|UniProtKB:P01602}. FT REGION 79 110 Framework-3. FT {ECO:0000250|UniProtKB:P01602}. FT REGION 111 >117 Complementarity-determining-2. FT {ECO:0000250|UniProtKB:P01602}. FT DISULFID 45 110 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT CONFLICT 44 44 T -> I (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 56 56 G -> T (in Ref. 2; AA sequence and 3; AA FT sequence). {ECO:0000305}. FT CONFLICT 64 64 K -> T (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 68 68 R -> E (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 72 74 AAS -> GAT (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 75 75 S -> N (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 89 89 S -> A (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 98 98 S -> N (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 113 116 HNSY -> YSSF (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 113 113 H -> Q (in Ref. 2; AA sequence). FT {ECO:0000305}. FT NON_TER 117 117 SQ SEQUENCE 117 AA; 12779 MW; 8F0682D45A41B4DF CRC64; MDMRVPAQLL GLLLLWFPGA RCDIQMTQSP SSLSASVGDR VTITCRASQG IRNDLGWYQQ KPGKAPKRLI YAASSLQSGV PSRFSGSGSG TEFTLTISSL QPEDFATYYC LQHNSYP //