ID LV151_HUMAN Reviewed; 117 AA. AC P01701; A0A075B6I5; P01702; P06316; P06888; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 07-SEP-2016, sequence version 2. DT 16-JAN-2019, entry version 109. DE RecName: Full=Immunoglobulin lambda variable 1-51 {ECO:0000303|PubMed:11872955, ECO:0000303|Ref.7}; DE AltName: Full=Ig lambda chain V-I region BL2 {ECO:0000305|PubMed:6095199}; DE AltName: Full=Ig lambda chain V-I region EPS {ECO:0000305|PubMed:3929803}; DE AltName: Full=Ig lambda chain V-I region NEW {ECO:0000305|PubMed:4177823}; DE AltName: Full=Ig lambda chain V-I region NIG-64 {ECO:0000305|PubMed:6404900}; DE Flags: Precursor; GN Name=IGLV1-51 {ECO:0000303|PubMed:11872955, ECO:0000303|Ref.7}; 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=6095199; DOI=10.1093/nar/12.22.8407; RA Tsujimoto Y., Croce C.M.; RT "Molecular cloning of a human immunoglobulin lambda chain variable RT sequence."; RL Nucleic Acids Res. 12:8407-8414(1984). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE RP IGLV1-51*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, AND PYROGLUTAMATE FORMATION AT GLN-20. RX PubMed=4177823; RA Langer B., Steinmetz-Kayne M., Hilschmann N.; RT "The complete amino acid sequence of Bence Jones protein New (lambda- RT type). Subgroups in the variable part of immunoglobulin L-chains of RT the lambda-type."; RL Hoppe-Seyler's Z. Physiol. Chem. 349:945-951(1968). RN [4] RP PROTEIN SEQUENCE OF 20-117, AND PYROGLUTAMATE FORMATION AT GLN-20. RX PubMed=6404900; RA Kametani F., Takayasu T., Suzuki S., Shinoda T., Okuyama T., RA Shimizu A.; RT "Comparative studies on the structure of the light chains of human RT immunoglobulins. IV. Assignment of a subsubgroup."; RL J. Biochem. 93:421-429(1983). RN [5] RP PROTEIN SEQUENCE OF 20-117. RX PubMed=3929803; RA Toft K.G., Sletten K., Husby G.; RT "The amino-acid sequence of the variable region of a carbohydrate- RT containing amyloid fibril protein EPS (immunoglobulin light chain, RT type lambda)."; RL Biol. Chem. Hoppe-Seyler 366:617-625(1985). RN [6] 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 [7] 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 [8] 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 [9] 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 [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). 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 IGLV1-51*01. CC -!- CAUTION: For an example of a full-length immunoglobulin lambda CC light chain see AC P0DOX8. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA25598.1; Type=Miscellaneous discrepancy; Note=Chimeric mRNA corresponding to regions V and J of immunoglobulin kappa light chain.; Evidence={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; X01147; CAA25598.1; ALT_SEQ; mRNA. DR EMBL; AC245060; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; A01964; L1HUNW. DR PIR; A01965; L1HUNG. DR PIR; A01966; L1HUBL. DR PIR; A24656; L1HUEP. DR ProteinModelPortal; P01701; -. DR SMR; P01701; -. DR IMGT_GENE-DB; IGLV1-51; -. DR BioMuta; IGLV1-51; -. DR DMDM; 126543; -. DR jPOST; P01701; -. DR PeptideAtlas; P01701; -. DR PRIDE; P01701; -. DR ProteomicsDB; 51429; -. DR ProteomicsDB; 51430; -. DR ProteomicsDB; 51890; -. DR ProteomicsDB; 51942; -. DR Ensembl; ENST00000390290; ENSP00000374825; ENSG00000211644. DR UCSC; uc062cbm.1; human. DR EuPathDB; HostDB:ENSG00000211644.2; -. DR GeneCards; IGLV1-51; -. DR HGNC; HGNC:5882; IGLV1-51. DR neXtProt; NX_P01701; -. DR OpenTargets; ENSG00000211644; -. DR GeneTree; ENSGT00940000154293; -. DR HOVERGEN; HBG018013; -. DR OrthoDB; 970259at2759; -. 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:P01701; -. DR Proteomes; UP000005640; Chromosome 22. DR Bgee; ENSG00000211644; Expressed in 88 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 Cell membrane; Complete proteome; Direct protein sequencing; KW Disulfide bond; Immunoglobulin domain; Immunoglobulin V region; KW Membrane; Polymorphism; Pyrrolidone carboxylic acid; KW Reference proteome; Secreted; Signal. FT SIGNAL 1 19 {ECO:0000269|PubMed:3929803, FT ECO:0000269|PubMed:4177823, FT ECO:0000269|PubMed:6404900}. FT CHAIN 20 117 Immunoglobulin lambda variable 1-51. FT {ECO:0000269|PubMed:3929803, FT ECO:0000269|PubMed:4177823, FT ECO:0000269|PubMed:6404900}. FT /FTId=PRO_0000059824. FT DOMAIN 20 >117 Ig-like. {ECO:0000255|PROSITE- FT ProRule:PRU00114}. FT MOD_RES 20 20 Pyrrolidone carboxylic acid. FT {ECO:0000269|PubMed:4177823, FT ECO:0000269|PubMed:6404900}. FT DISULFID 41 108 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT CONFLICT 29 29 V -> L (in Ref. 5; AA sequence). FT {ECO:0000305}. FT CONFLICT 36 38 KVT -> RVS (in Ref. 5; AA sequence). FT {ECO:0000305}. FT CONFLICT 36 36 K -> E (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 44 46 SSS -> GST (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 50 54 NNYVS -> KNYVD (in Ref. 5; AA sequence). FT {ECO:0000305}. FT CONFLICT 50 52 NNY -> DNF (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 51 51 N -> D (in Ref. 1; CAA25598). FT {ECO:0000305}. FT CONFLICT 56 58 YQQ -> HQH (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 59 59 L -> V (in Ref. 1; CAA25598). FT {ECO:0000305}. FT CONFLICT 69 70 YD -> FN (in Ref. 5; AA sequence). FT {ECO:0000305}. FT CONFLICT 70 71 DN -> ED (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 82 84 FSG -> ISA (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 99 99 Q -> R (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 105 105 D -> I (in Ref. 5; AA sequence). FT {ECO:0000305}. FT CONFLICT 109 109 G -> A (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 112 117 DSSLSA -> NNSLSG (in Ref. 1; CAA25598). FT {ECO:0000305}. FT CONFLICT 113 117 SSLSA -> NRRSV (in Ref. 5; AA sequence). FT {ECO:0000305}. FT CONFLICT 116 116 S -> N (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 117 117 A -> V (in Ref. 4; AA sequence). FT {ECO:0000305}. FT NON_TER 117 117 SQ SEQUENCE 117 AA; 12249 MW; 46700D34C2882B7F CRC64; MTCSPLLLTL LIHCTGSWAQ SVLTQPPSVS AAPGQKVTIS CSGSSSNIGN NYVSWYQQLP GTAPKLLIYD NNKRPSGIPD RFSGSKSGTS ATLGITGLQT GDEADYYCGT WDSSLSA //