ID LV208_HUMAN Reviewed; 118 AA. AC P01709; A0A087WZW9; P01710; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 02-NOV-2016, sequence version 2. DT 16-JAN-2019, entry version 140. DE RecName: Full=Immunoglobulin lambda variable 2-8 {ECO:0000303|PubMed:11872955, ECO:0000303|Ref.5}; DE AltName: Full=Ig lambda chain V-II region BO {ECO:0000305|PubMed:5532228}; DE AltName: Full=Ig lambda chain V-II region MGC {ECO:0000305|PubMed:4415202}; DE Flags: Precursor; GN Name=IGLV2-8 {ECO:0000303|PubMed:11872955, 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 IGLV2-8*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 20-118, AND PYROGLUTAMATE FORMATION AT GLN-20. RX PubMed=5532228; RA Wikler M., Putnam F.W.; RT "Amino acid sequence of human lambda chains. 3. Tryptic peptides, RT chymotryptic peptides, and sequence of protein Bo."; RL J. Biol. Chem. 245:4488-4507(1970). RN [3] RP PROTEIN SEQUENCE OF 20-118, AND PYROGLUTAMATE FORMATION AT GLN-20. RX PubMed=4415202; DOI=10.1021/bi00717a007; RA Fett J.W., Deutsch H.F.; RT "Primary structure of the Mcg lambda chain."; RL Biochemistry 13:4102-4114(1974). RN [4] 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 [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). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 21-118. RX PubMed=2515285; DOI=10.1016/0022-2836(89)90135-6; RA Ely K.R., Herron J.N., Harker M., Edmundson A.B.; RT "Three-dimensional structure of a light chain dimer crystallized in RT water. Conformational flexibility of a molecule in two crystal RT forms."; RL J. Mol. Biol. 210:601-615(1989). 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 IGLV2-8*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; AC245028; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; A01976; L2HUBO. DR PIR; A90381; L2HUMC. DR PDB; 1A8J; X-ray; 2.70 A; H/L=21-118. DR PDB; 1DCL; X-ray; 2.30 A; A/B=21-118. DR PDB; 1MCW; X-ray; 3.50 A; M=21-118. DR PDB; 2MCG; X-ray; 2.00 A; 1/2=21-118. DR PDB; 3MCG; X-ray; 2.00 A; 1/2=21-118. DR PDB; 4UNT; X-ray; 2.70 A; A/B/C/D/E/F/G/H=20-118. DR PDB; 4UNU; X-ray; 0.95 A; A/B=20-118. DR PDB; 4UNV; X-ray; 1.60 A; A=20-118. DR PDB; 5ACL; X-ray; 1.49 A; A=20-118. DR PDB; 5ACM; X-ray; 1.05 A; A/B=20-118. DR PDBsum; 1A8J; -. DR PDBsum; 1DCL; -. DR PDBsum; 1MCW; -. DR PDBsum; 2MCG; -. DR PDBsum; 3MCG; -. DR PDBsum; 4UNT; -. DR PDBsum; 4UNU; -. DR PDBsum; 4UNV; -. DR PDBsum; 5ACL; -. DR PDBsum; 5ACM; -. DR ProteinModelPortal; P01709; -. DR SMR; P01709; -. DR MINT; P01709; -. DR DrugBank; DB03088; Pyroglutamic Acid. DR IMGT_GENE-DB; IGLV2-8; -. DR BioMuta; IGLV2-8; -. DR DMDM; 126560; -. DR jPOST; P01709; -. DR PeptideAtlas; P01709; -. DR PRIDE; P01709; -. DR ProteomicsDB; 51437; -. DR ProteomicsDB; 51438; -. DR Ensembl; ENST00000620395; ENSP00000482937; ENSG00000278196. DR EuPathDB; HostDB:ENSG00000278196.1; -. DR GeneCards; IGLV2-8; -. DR HGNC; HGNC:5895; IGLV2-8. DR neXtProt; NX_P01709; -. DR OpenTargets; ENSG00000278196; -. DR GeneTree; ENSGT00940000154179; -. DR HOVERGEN; HBG018013; -. DR PhylomeDB; P01709; -. 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 EvolutionaryTrace; P01709; -. DR PRO; PR:P01709; -. DR Proteomes; UP000005640; Chromosome 22. DR Bgee; ENSG00000278196; Expressed in 83 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; Pyrrolidone carboxylic acid; Reference proteome; KW Secreted; Signal. FT SIGNAL 1 19 {ECO:0000269|PubMed:4415202, FT ECO:0000269|PubMed:5532228}. FT CHAIN 20 118 Immunoglobulin lambda variable 2-8. FT {ECO:0000269|PubMed:4415202, FT ECO:0000269|PubMed:5532228}. FT /FTId=PRO_0000059835. FT DOMAIN 20 >118 Ig-like. {ECO:0000255|PROSITE- FT ProRule:PRU00114}. FT MOD_RES 20 20 Pyrrolidone carboxylic acid. FT {ECO:0000269|PubMed:4415202, FT ECO:0000269|PubMed:5532228}. FT DISULFID 41 109 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT CONFLICT 33 33 P -> L (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 50 52 GYN -> DNK (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 61 61 P -> A (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 63 63 K -> R (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 67 68 LM -> VI (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 68 70 MIY -> VIF (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 73 73 S -> N (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 74 74 K -> Q (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 89 89 G -> D (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 100 100 Q -> R (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 113 115 AGS -> VDN (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 113 113 A -> E (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 116 116 N -> D (in Ref. 3; AA sequence). FT {ECO:0000305}. FT NON_TER 118 118 FT STRAND 27 32 {ECO:0000244|PDB:4UNU}. FT STRAND 37 42 {ECO:0000244|PDB:4UNU}. FT TURN 45 50 {ECO:0000244|PDB:4UNU}. FT STRAND 54 59 {ECO:0000244|PDB:4UNU}. FT STRAND 61 63 {ECO:0000244|PDB:1A8J}. FT STRAND 66 70 {ECO:0000244|PDB:4UNU}. FT TURN 71 73 {ECO:0000244|PDB:4UNU}. FT STRAND 77 79 {ECO:0000244|PDB:2MCG}. FT STRAND 83 88 {ECO:0000244|PDB:4UNU}. FT STRAND 91 96 {ECO:0000244|PDB:4UNU}. FT HELIX 101 103 {ECO:0000244|PDB:4UNU}. FT STRAND 105 112 {ECO:0000244|PDB:4UNU}. FT STRAND 114 116 {ECO:0000244|PDB:2MCG}. SQ SEQUENCE 118 AA; 12382 MW; B94EEE11F9DA8260 CRC64; MAWALLLLTL LTQGTGSWAQ SALTQPPSAS GSPGQSVTIS CTGTSSDVGG YNYVSWYQQH PGKAPKLMIY EVSKRPSGVP DRFSGSKSGN TASLTVSGLQ AEDEADYYCS SYAGSNNF //