ID LV657_HUMAN Reviewed; 117 AA. AC P01721; A0A075B6I2; P01722; P06317; P06318; P06319; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 02-NOV-2016, sequence version 2. DT 16-JAN-2019, entry version 106. DE RecName: Full=Immunoglobulin lambda variable 6-57 {ECO:0000303|PubMed:11872955, ECO:0000303|Ref.8}; DE AltName: Full=Ig lambda chain V-VI region AR {ECO:0000305|PubMed:6797401}; DE AltName: Full=Ig lambda chain V-VI region EB4 {ECO:0000305|PubMed:3923440}; DE AltName: Full=Ig lambda chain V-VI region NIG-48 {ECO:0000305|PubMed:118171}; DE AltName: Full=Ig lambda chain V-VI region SUT {ECO:0000305|Ref.6}; DE AltName: Full=Ig lambda chain V-VI region WLT {ECO:0000305|PubMed:4089539}; DE Flags: Precursor; GN Name=IGLV6-57 {ECO:0000303|PubMed:11872955, 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 [MRNA]. RX PubMed=3923440; DOI=10.1093/nar/13.8.2931; RA Anderson M.L.M., Brown L., McKenzie E., Kellow J.E., Young B.D.; RT "Cloning and sequence analysis of an Ig lambda light chain mRNA RT expressed in the Burkitt's lymphoma cell line EB4."; RL Nucleic Acids Res. 13:2931-2941(1985). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE RP IGLV6-57*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 [3] RP PROTEIN SEQUENCE OF 20-117. RX PubMed=118171; DOI=10.1093/oxfordjournals.jbchem.a132670; RA Takahashi N., Takayasu T., Isobe T., Shinoda T., Okuyama T., RA Shimizu A.; RT "Comparative study on the structure of the light chains of human RT immunoglobulins. II. Assignment of a new subgroup."; RL J. Biochem. 86:1523-1535(1979). RN [4] RP PROTEIN SEQUENCE OF 20-117. RX PubMed=6797401; DOI=10.1042/bj1950561; RA Sletten K., Natvig J.B., Husby G., Juul J.; RT "The complete amino acid sequence of a prototype immunoglobulin-lambda RT light-chain-type amyloid-fibril protein AR."; RL Biochem. J. 195:561-572(1981). RN [5] RP PROTEIN SEQUENCE OF 20-117. RX PubMed=4089539; DOI=10.1111/j.1365-3083.1985.tb01927.x; RA Dwulet F.E., Strako K., Benson M.D.; RT "Amino acid sequence of a lambda VI primary (AL) amyloid protein RT (WLT)."; RL Scand. J. Immunol. 22:653-660(1985). RN [6] RP PROTEIN SEQUENCE OF 20-117. RA Solomon A., Kyle R.A., Frangione B.; RT "Light chain variable region subgroups of monoclonal immunoglobulins RT in amyloidosis AL."; RL (In) Glenner G.G., Osserman E.F., Benditt E.P., Calkins E., RL Cohen A.S., Zucker-Franklin D. (eds.); RL Amyloidosis, pp.449-462, Plenum Press, New York (1986). RN [7] 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 [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: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 IGLV6-57*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; AC245060; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; A01987; L6HUAR. DR PIR; A01988; L6HUST. DR PIR; A01989; L6HULT. DR PIR; A01990; L6HUEB. DR PIR; A01991; L6HU48. DR UniGene; Hs.535668; -. DR PDB; 1CD0; X-ray; 1.90 A; A/B=20-117. DR PDB; 1PEW; X-ray; 1.60 A; A/B=20-117. DR PDB; 2CD0; X-ray; 1.80 A; A/B=20-117. DR PDB; 5IR3; X-ray; 1.70 A; A=20-117. DR PDBsum; 1CD0; -. DR PDBsum; 1PEW; -. DR PDBsum; 2CD0; -. DR PDBsum; 5IR3; -. DR ProteinModelPortal; P01721; -. DR SMR; P01721; -. DR IMGT_GENE-DB; IGLV6-57; -. DR BioMuta; IGLV6-57; -. DR DMDM; 126575; -. DR PeptideAtlas; P01721; -. DR PRIDE; P01721; -. DR ProteomicsDB; 51449; -. DR ProteomicsDB; 51450; -. DR ProteomicsDB; 51891; -. DR ProteomicsDB; 51892; -. DR ProteomicsDB; 51893; -. DR Ensembl; ENST00000390285; ENSP00000374820; ENSG00000211640. DR DisGeNET; 28778; -. DR EuPathDB; HostDB:ENSG00000211640.3; -. DR GeneCards; IGLV6-57; -. DR HGNC; HGNC:5927; IGLV6-57. DR neXtProt; NX_P01721; -. DR OpenTargets; ENSG00000211640; -. DR GeneTree; ENSGT00940000161640; -. DR HOVERGEN; HBG018013; -. DR PhylomeDB; P01721; -. 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; IGLV6-57; human. DR PRO; PR:P01721; -. DR Proteomes; UP000005640; Chromosome 22. DR Bgee; ENSG00000211640; Expressed in 79 organ(s), highest expression level in lymph node. 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; Reference proteome; Secreted; Signal. FT SIGNAL 1 19 {ECO:0000269|PubMed:118171, FT ECO:0000269|PubMed:4089539, FT ECO:0000269|PubMed:6797401, FT ECO:0000269|Ref.6}. FT CHAIN 20 117 Immunoglobulin lambda variable 6-57. FT {ECO:0000269|PubMed:118171, FT ECO:0000269|PubMed:4089539, FT ECO:0000269|PubMed:6797401, FT ECO:0000269|Ref.6}. FT /FTId=PRO_0000059850. FT DOMAIN 20 >117 Ig-like. {ECO:0000255|PROSITE- FT ProRule:PRU00114}. FT REGION 20 41 Framework-1. {ECO:0000303|Ref.6}. FT REGION 42 54 Complementarity-determining-1. FT {ECO:0000303|PubMed:3923440}. FT REGION 55 69 Framework-2. {ECO:0000303|Ref.6}. FT REGION 70 76 Complementarity-determining-2. FT {ECO:0000303|PubMed:3923440}. FT REGION 77 110 Framework-3. {ECO:0000303|Ref.6}. FT REGION 111 >117 Complementarity-determining-3. FT {ECO:0000303|PubMed:3923440}. FT DISULFID 41 110 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT CONFLICT 16 17 GS -> DC (in Ref. 1). {ECO:0000305}. FT CONFLICT 20 20 N -> D (in Ref. 4; AA sequence and 6; AA FT sequence). {ECO:0000305}. FT CONFLICT 21 21 F -> L (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 24 24 T -> I (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 27 27 H -> L (in Ref. 5; AA sequence). FT {ECO:0000305}. FT CONFLICT 27 27 H -> P (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 31 31 E -> G (in Ref. 5; AA sequence). FT {ECO:0000305}. FT CONFLICT 34 34 G -> E (in Ref. 5; AA sequence). FT {ECO:0000305}. FT CONFLICT 38 38 T -> I (in Ref. 6; AA sequence). FT {ECO:0000305}. FT CONFLICT 39 39 I -> F (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 39 39 I -> M (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 43 47 GSSGS -> RSDGT (in Ref. 6; AA sequence). FT {ECO:0000305}. FT CONFLICT 43 46 GSSG -> RTSD (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 44 44 S -> N (in Ref. 1). {ECO:0000305}. FT CONFLICT 45 45 S -> G (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 49 49 A -> G (in Ref. 5; AA sequence). FT {ECO:0000305}. FT CONFLICT 50 52 SNY -> DSF (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 50 51 SN -> GY (in Ref. 6; AA sequence). FT {ECO:0000305}. FT CONFLICT 57 57 Q -> R (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 60 61 PG -> RV (in Ref. 1). {ECO:0000305}. FT CONFLICT 62 62 S -> G (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 62 62 S -> R (in Ref. 6; AA sequence). FT {ECO:0000305}. FT CONFLICT 66 66 T -> I (in Ref. 1). {ECO:0000305}. FT CONFLICT 66 66 T -> N (in Ref. 5; AA sequence). FT {ECO:0000305}. FT CONFLICT 67 67 V -> L (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 69 69 Y -> F (in Ref. 6; AA sequence). FT {ECO:0000305}. FT CONFLICT 70 70 E -> D (in Ref. 4; AA sequence and 3; AA FT sequence). {ECO:0000305}. FT CONFLICT 71 71 D -> N (in Ref. 5; AA sequence). FT {ECO:0000305}. FT CONFLICT 71 71 D -> T (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 72 72 N -> T (in Ref. 6; AA sequence). FT {ECO:0000305}. FT CONFLICT 76 76 S -> L (in Ref. 1). {ECO:0000305}. FT CONFLICT 77 77 G -> E (in Ref. 5; AA sequence). FT {ECO:0000305}. FT CONFLICT 80 80 D -> N (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 86 86 I -> F (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 88 90 SSS -> DSA (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 88 88 S -> R (in Ref. 6; AA sequence). FT {ECO:0000305}. FT CONFLICT 101 109 KTEDEADYY -> TNDDTAMYF (in Ref. 3; AA FT sequence). {ECO:0000305}. FT CONFLICT 101 101 K -> Q (in Ref. 6; AA sequence). FT {ECO:0000305}. FT CONFLICT 113 116 YDSS -> FDNT (in Ref. 1). {ECO:0000305}. FT CONFLICT 114 117 DSSN -> NSNH (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 115 117 SSN -> NNN (in Ref. 5; AA sequence). FT {ECO:0000305}. FT CONFLICT 115 117 SSN -> RDH (in Ref. 6; AA sequence). FT {ECO:0000305}. FT NON_TER 117 117 FT STRAND 27 31 {ECO:0000244|PDB:1PEW}. FT STRAND 37 46 {ECO:0000244|PDB:1PEW}. FT HELIX 48 50 {ECO:0000244|PDB:1PEW}. FT STRAND 54 58 {ECO:0000244|PDB:1PEW}. FT STRAND 65 69 {ECO:0000244|PDB:1PEW}. FT TURN 70 72 {ECO:0000244|PDB:1PEW}. FT STRAND 82 87 {ECO:0000244|PDB:1PEW}. FT TURN 88 91 {ECO:0000244|PDB:1PEW}. FT STRAND 92 97 {ECO:0000244|PDB:1PEW}. FT HELIX 102 104 {ECO:0000244|PDB:1PEW}. FT STRAND 106 114 {ECO:0000244|PDB:1PEW}. SQ SEQUENCE 117 AA; 12566 MW; 1FA030C806D9F49F CRC64; MAWAPLLLTL LAHCTGSWAN FMLTQPHSVS ESPGKTVTIS CTGSSGSIAS NYVQWYQQRP GSAPTTVIYE DNQRPSGVPD RFSGSIDSSS NSASLTISGL KTEDEADYYC QSYDSSN //