ID LV144_HUMAN Reviewed; 117 AA. AC P01699; A0A0B4J1U1; A0A0G2JQC2; A0A0U1RVH6; P06887; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 02-NOV-2016, sequence version 2. DT 16-JAN-2019, entry version 110. DE RecName: Full=Immunoglobulin lambda variable 1-44 {ECO:0000303|PubMed:11872955, ECO:0000303|Ref.5}; DE AltName: Full=Ig lambda chain V-I region MEM {ECO:0000305|PubMed:2410269}; DE AltName: Full=Ig lambda chain V-I region VOR {ECO:0000305|PubMed:809332}; DE Flags: Precursor; GN Name=IGLV1-44 {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 IGLV1-44*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 20-117, AND PYROGLUTAMATE FORMATION AT GLN-20. RX PubMed=809332; RA Engelhard M., Hilschmann N.; RT "Pattern of antibody structure. The amino acid sequence of a RT monoclonal immunoglobulin L-chain of lambda-type, subgroup I (Bence- RT Jones-protein Vor.). A contribution to the elucidation of the origin RT of antibody specificity."; RL Hoppe-Seyler's Z. Physiol. Chem. 356:1413-1444(1975). RN [3] RP PROTEIN SEQUENCE OF 20-117, AND PYROGLUTAMATE FORMATION AT GLN-20. RX PubMed=2410269; DOI=10.1111/j.1432-1033.1985.tb09027.x; RA Mihaesco E., Roy J.P., Congy N., Peran-Rivat L., Mihaesco C.; RT "The amino acid sequence of a lambda light chain presenting abnormal RT physicochemical and antigenic features."; RL Eur. J. Biochem. 150:349-357(1985). 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). 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 IGLV1-44*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; AC245291; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; A01962; L1HUVO. DR PIR; A25479; L1HUMM. DR UniGene; Hs.449585; -. DR UniGene; Hs.655198; -. DR ProteinModelPortal; P01699; -. DR SMR; P01699; -. DR IMGT_GENE-DB; IGLV1-44; -. DR BioMuta; IGLV1-44; -. DR DMDM; 126537; -. DR jPOST; P01699; -. DR PeptideAtlas; P01699; -. DR PRIDE; P01699; -. DR ProteomicsDB; 51427; -. DR ProteomicsDB; 51941; -. DR Ensembl; ENST00000390297; ENSP00000374832; ENSG00000211651. DR Ensembl; ENST00000628287; ENSP00000485735; ENSG00000274854. DR DisGeNET; 28823; -. DR EuPathDB; HostDB:ENSG00000211651.3; -. DR GeneCards; IGLV1-44; -. DR HGNC; HGNC:5879; IGLV1-44. DR neXtProt; NX_P01699; -. DR OpenTargets; ENSG00000211651; -. DR GeneTree; ENSGT00940000154293; -. DR HOVERGEN; HBG018013; -. DR OMA; LLIQCAG; -. DR OrthoDB; 1451150at2759; -. DR PhylomeDB; P01699; -. 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; IGLV1-44; human. DR PRO; PR:P01699; -. DR Proteomes; UP000005640; Chromosome 22. DR Bgee; ENSG00000211651; Expressed in 81 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 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:2410269, FT ECO:0000269|PubMed:809332}. FT CHAIN 20 117 Immunoglobulin lambda variable 1-44. FT {ECO:0000269|PubMed:2410269, FT ECO:0000269|PubMed:809332}. FT /FTId=PRO_0000059822. FT DOMAIN 20 >117 Ig-like. {ECO:0000255|PROSITE- FT ProRule:PRU00114}. FT MOD_RES 20 20 Pyrrolidone carboxylic acid. FT {ECO:0000269|PubMed:2410269, FT ECO:0000269|PubMed:809332}. FT DISULFID 41 108 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT CONFLICT 35 35 Q -> G (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 44 47 SSSN -> GNFD (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 48 48 I -> V (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 50 52 SNT -> RNS (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 52 54 TVN -> ZPAY (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 58 59 QL -> VH (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 65 65 K -> R (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 70 71 SN -> NY (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 71 72 NN -> SD (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 75 75 P -> S (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 84 86 GSK -> ASR (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 102 102 D -> N (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 107 107 Y -> F (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 110 110 A -> T (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 116 116 N -> D (in Ref. 2; AA sequence and 3; AA FT sequence). {ECO:0000305}. FT NON_TER 117 117 SQ SEQUENCE 117 AA; 12201 MW; 5302215AD2E70E7C CRC64; MASFPLLLTL LTHCAGSWAQ SVLTQPPSAS GTPGQRVTIS CSGSSSNIGS NTVNWYQQLP GTAPKLLIYS NNQRPSGVPD RFSGSKSGTS ASLAISGLQS EDEADYYCAA WDDSLNG //