ID LV301_HUMAN Reviewed; 115 AA. AC P01715; A0A075B6K7; P01716; P06889; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 02-NOV-2016, sequence version 2. DT 16-JAN-2019, entry version 115. DE RecName: Full=Immunoglobulin lambda variable 3-1 {ECO:0000303|PubMed:11872955, ECO:0000303|Ref.6}; DE AltName: Full=Ig lambda chain V-IV region Bau {ECO:0000305|PubMed:4435717}; DE AltName: Full=Ig lambda chain V-IV region MOL {ECO:0000305|PubMed:3103603}; DE AltName: Full=Ig lambda chain V-IV region X {ECO:0000305|PubMed:4883841}; DE Flags: Precursor; GN Name=IGLV3-1 {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 IGLV3-1*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 21-115. RX PubMed=4883841; DOI=10.1042/bj1100631; RA Milstein C., Clegg J.B., Jarvis J.M.; RT "Immunoglobulin lambda-chains. The complete amino acid sequence of a RT Bence-Jones protein."; RL Biochem. J. 110:631-652(1968). RN [3] RP PROTEIN SEQUENCE OF 21-115. RX PubMed=4435717; RA Baczko K., Braun D., Hilschmann N.; RT "Pattern of antibody structure, the primary structure of monoclonal RT immunoglobulin L-chain of the lambda-type, subgroup IV (Bence-Jones RT protein Bau.)."; RL Hoppe-Seyler's Z. Physiol. Chem. 355:131-154(1974). RN [4] RP PROTEIN SEQUENCE OF 21-115. RX PubMed=3103603; DOI=10.1042/bj2390545; RA Holm E., Sletten K., Husby G.; RT "Structural studies of a carbohydrate-containing immunoglobulin- RT lambda-light-chain amyloid-fibril protein (AL) of variable subgroup RT III."; RL Biochem. J. 239:545-551(1986). 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 IGLV3-1*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; A01981; L4HUBU. DR PIR; A01982; L4HUX. DR PIR; A26019; L4HUML. DR ProteinModelPortal; P01715; -. DR SMR; P01715; -. DR IMGT_GENE-DB; IGLV3-1; -. DR BioMuta; IGLV3-1; -. DR DMDM; 126566; -. DR jPOST; P01715; -. DR PeptideAtlas; P01715; -. DR PRIDE; P01715; -. DR ProteomicsDB; 51443; -. DR ProteomicsDB; 51444; -. DR ProteomicsDB; 51943; -. DR Ensembl; ENST00000390319; ENSP00000374854; ENSG00000211673. DR EuPathDB; HostDB:ENSG00000211673.2; -. DR GeneCards; IGLV3-1; -. DR HGNC; HGNC:5896; IGLV3-1. DR neXtProt; NX_P01715; -. DR OpenTargets; ENSG00000211673; -. DR GeneTree; ENSGT00940000153120; -. DR HOVERGEN; HBG018013; -. DR OMA; PCHTEQE; -. DR OrthoDB; 737753at2759; -. DR PhylomeDB; P01715; -. 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; IGLV3-1; human. DR PRO; PR:P01715; -. DR Proteomes; UP000005640; Chromosome 22. DR Bgee; ENSG00000211673; Expressed in 83 organ(s), highest expression level in adrenal gland. 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 20 {ECO:0000269|PubMed:3103603, FT ECO:0000269|PubMed:4435717, FT ECO:0000269|PubMed:4883841}. FT CHAIN 21 115 Immunoglobulin lambda variable 3-1. FT {ECO:0000269|PubMed:3103603, FT ECO:0000269|PubMed:4435717, FT ECO:0000269|PubMed:4883841}. FT /FTId=PRO_0000059844. FT DOMAIN 21 >115 Ig-like. {ECO:0000255|PROSITE- FT ProRule:PRU00114}. FT DISULFID 41 106 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT CONFLICT 22 22 E -> D (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 22 22 E -> G (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 29 29 V -> L (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 38 40 SIT -> TIS (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 48 52 DKYAC -> ESYYD (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 48 51 DKYA -> EQYV (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 50 51 YA -> DV (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 57 57 K -> R (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 57 57 K -> S (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 63 63 V -> L (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 68 70 QDS -> EGD (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 68 68 Q -> H (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 70 73 SKRP -> NQRS (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 87 87 N -> T (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 97 98 QA -> ES (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 110 110 D -> N (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 112 115 STAH -> MSVV (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 112 115 STAH -> YTVI (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 113 115 TAH -> SVL (in Ref. 4; AA sequence). FT {ECO:0000305}. FT NON_TER 115 115 SQ SEQUENCE 115 AA; 12296 MW; 04ECCC92731F7847 CRC64; MAWIPLFLGV LAYCTGSVAS YELTQPPSVS VSPGQTASIT CSGDKLGDKY ACWYQQKPGQ SPVLVIYQDS KRPSGIPERF SGSNSGNTAT LTISGTQAMD EADYYCQAWD SSTAH //