ID LV214_HUMAN Reviewed; 120 AA. AC P01704; A0A075B6K1; P01711; P04209; 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 lambda variable 2-14 {ECO:0000303|PubMed:11872955, ECO:0000303|Ref.6}; DE AltName: Full=Ig lambda chain V-II region NIG-84 {ECO:0000305|PubMed:3922791}; DE AltName: Full=Ig lambda chain V-II region TOG {ECO:0000305|PubMed:500108}; DE AltName: Full=Ig lambda chain V-II region VIL {ECO:0000305|PubMed:5087637}; DE Flags: Precursor; GN Name=IGLV2-14 {ECO:0000303|PubMed:11872955, ECO:0000303|Ref.6}; 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 IGLV2-14*01). RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J., RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., RA Khan A.S., Lane L., Tilahun Y., Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [2] RP PROTEIN SEQUENCE OF 20-120. RX PubMed=5087637; RA Ponstingl H., Hilschmann N.; RT "Structural rule of antibodies. Complete primary structure of a RT monoclonal immunoglobin L chain of the lambda type, subgroup II (Bence RT Jones protein VIL)."; RL Hoppe-Seyler's Z. Physiol. Chem. 352:859-877(1971). RN [3] RP PROTEIN SEQUENCE OF 20-120, AND PYROGLUTAMATE FORMATION AT GLN-20. RX PubMed=500108; DOI=10.1016/0161-5890(79)90068-3; RA Nabeshima Y., Ikenaka T.; RT "Primary structure of cryo Bence-Jones protein (Tog) from the urine of RT a patient with IgD myeloma."; RL Mol. Immunol. 16:439-444(1979). RN [4] RP PROTEIN SEQUENCE OF 20-120. RX PubMed=3922791; DOI=10.1016/0014-5793(85)80757-2; RA Tonoike H., Kametani F., Hoshi A., Shinoda T., Isobe T.; RT "Amino acid sequence of an amyloidogenic Bence Jones protein in RT myeloma-associated systemic amyloidosis."; RL FEBS Lett. 185:139-141(1985). RN [5] RP NOMENCLATURE. RX PubMed=11872955; RA Lefranc M.P.; RT "Nomenclature of the human immunoglobulin lambda (IGL) genes."; RL Exp. Clin. Immunogenet. 18:242-254(2001). RN [6] 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 [7] 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 [8] 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 [9] 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 [10] 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:17576170, PubMed:20176268). {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 IGLV2-14*01. CC -!- CAUTION: For an example of a full-length immunoglobulin lambda CC light chain see AC P0DOX8. {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; AC244250; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; A01969; L2HUTG. DR PIR; A01971; L2HUNG. DR PIR; A01977; L2HUVL. DR PDB; 5C2B; X-ray; 1.40 A; L=20-111. DR PDB; 5C6W; X-ray; 1.54 A; H/J=20-120. DR PDB; 5CBA; X-ray; 2.50 A; B/D=20-111. DR PDB; 5CBE; X-ray; 2.40 A; B/D=20-109. DR PDBsum; 5C2B; -. DR PDBsum; 5C6W; -. DR PDBsum; 5CBA; -. DR PDBsum; 5CBE; -. DR ProteinModelPortal; P01704; -. DR SMR; P01704; -. DR IMGT_GENE-DB; IGLV2-14; -. DR BioMuta; IGLV2-14; -. DR DMDM; 126552; -. DR jPOST; P01704; -. DR PeptideAtlas; P01704; -. DR PRIDE; P01704; -. DR ProteomicsDB; 51432; -. DR ProteomicsDB; 51439; -. DR ProteomicsDB; 51681; -. DR Ensembl; ENST00000390312; ENSP00000374847; ENSG00000211666. DR EuPathDB; HostDB:ENSG00000211666.2; -. DR GeneCards; IGLV2-14; -. DR HGNC; HGNC:5888; IGLV2-14. DR neXtProt; NX_P01704; -. DR OpenTargets; ENSG00000211666; -. DR GeneTree; ENSGT00940000154179; -. DR HOVERGEN; HBG018013; -. DR OMA; CTELPRS; -. DR PhylomeDB; P01704; -. 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; IGLV2-14; human. DR PRO; PR:P01704; -. DR Proteomes; UP000005640; Chromosome 22. DR Bgee; ENSG00000211666; Expressed in 82 organ(s), highest expression level in lymph node. 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 Polymorphism; Pyrrolidone carboxylic acid; Reference proteome; KW Secreted; Signal. FT SIGNAL 1 19 {ECO:0000269|PubMed:3922791, FT ECO:0000269|PubMed:500108, FT ECO:0000269|PubMed:5087637}. FT CHAIN 20 120 Immunoglobulin lambda variable 2-14. FT {ECO:0000269|PubMed:3922791, FT ECO:0000269|PubMed:500108, FT ECO:0000269|PubMed:5087637}. FT /FTId=PRO_0000059830. FT DOMAIN 20 119 Ig-like. {ECO:0000255|PROSITE- FT ProRule:PRU00114}. FT MOD_RES 20 20 Pyrrolidone carboxylic acid. FT {ECO:0000269|PubMed:500108}. FT DISULFID 41 109 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT CONFLICT 20 20 Q -> H (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 31 31 G -> A (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 33 33 P -> L (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 45 52 SSDVGGYN -> TNDIGSYS (in Ref. 3; AA FT sequence). {ECO:0000305}. FT CONFLICT 45 45 S -> T (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 52 53 NY -> DF (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 57 57 Y -> F (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 60 60 H -> Y (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 63 63 K -> T (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 67 74 LMIYEVSN -> VLIFDVNS (in Ref. 3; AA FT sequence). {ECO:0000305}. FT CONFLICT 68 70 MIY -> IIS (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 68 68 M -> L (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 71 74 EVSN -> DVNS (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 73 73 S -> R (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 79 79 V -> I (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 81 81 N -> D (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 81 81 N -> H (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 89 89 G -> A (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 106 108 DYY -> HYF (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 112 120 YTSSSTLHS -> FTTTNSRAV (in Ref. 4; AA FT sequence). {ECO:0000305}. FT CONFLICT 113 120 TSSSTLHS -> RTSGTIIF (in Ref. 3; AA FT sequence). {ECO:0000305}. FT CONFLICT 116 120 STLHS -> NSVVF (in Ref. 2; AA sequence). FT {ECO:0000305}. FT NON_TER 120 120 SQ SEQUENCE 120 AA; 12597 MW; 76569E85B25B5611 CRC64; MAWALLLLTL LTQGTGSWAQ SALTQPASVS GSPGQSITIS CTGTSSDVGG YNYVSWYQQH PGKAPKLMIY EVSNRPSGVS NRFSGSKSGN TASLTISGLQ AEDEADYYCS SYTSSSTLHS //