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 24-JAN-2024, entry version 132.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 IGLV1-51*01).
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., 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., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., 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., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA 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-type).
RT Subgroups in the variable part of immunoglobulin L-chains of the lambda-
RT 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; DOI=10.1093/oxfordjournals.jbchem.a134196;
RA Kametani F., Takayasu T., Suzuki S., Shinoda T., Okuyama T., 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; DOI=10.1515/bchm3.1985.366.2.617;
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, type
RT lambda).";
RL Biol. Chem. Hoppe-Seyler 366:617-625(1985).
RN [6]
RP NOMENCLATURE.
RX PubMed=11872955; DOI=10.1159/000049203;
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. (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., Buerckstuemmer T.,
RA 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 Rise
RT 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 (PubMed:24600447).
CC Immunoglobulins, also known as antibodies, are membrane-bound or
CC secreted glycoproteins produced by B lymphocytes. In the recognition
CC phase of humoral immunity, the membrane-bound immunoglobulins serve as
CC receptors which, upon binding of a specific antigen, trigger the clonal
CC expansion and differentiation of B lymphocytes into immunoglobulins-
CC secreting plasma cells. Secreted immunoglobulins mediate the effector
CC phase of humoral immunity, which results in the elimination of bound
CC antigens (PubMed:20176268, PubMed:22158414). The antigen binding site
CC is formed by the variable domain of one heavy chain, together with that
CC of its associated light chain. Thus, each immunoglobulin has two
CC antigen binding sites with remarkable affinity for a particular
CC antigen. The variable domains are assembled by a process called V-(D)-J
CC rearrangement and can then be subjected to somatic hypermutations
CC which, after exposure to antigen and selection, allow affinity
CC maturation for a particular antigen (PubMed:17576170, PubMed:20176268).
CC {ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268,
CC ECO:0000303|PubMed:22158414, ECO:0000303|PubMed:24600447}.
CC -!- SUBUNIT: Immunoglobulins are composed of two identical heavy chains and
CC 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 that of
CC IMGT allele IGLV1-51*01.
CC -!- CAUTION: For an example of a full-length immunoglobulin lambda light
CC 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 AlphaFoldDB; P01701; -.
DR EMDB; EMD-23717; -.
DR EMDB; EMD-25149; -.
DR EMDB; EMD-25606; -.
DR EMDB; EMD-30486; -.
DR EMDB; EMD-30487; -.
DR EMDB; EMD-30488; -.
DR EMDB; EMD-30573; -.
DR EMDB; EMD-30993; -.
DR EMDB; EMD-30994; -.
DR EMDB; EMD-33307; -.
DR EMDB; EMD-33308; -.
DR EMDB; EMD-33434; -.
DR EMDB; EMD-33493; -.
DR SMR; P01701; -.
DR IMGT_GENE-DB; IGLV1-51; -.
DR GlyGen; P01701; 1 site, 1 O-linked glycan (1 site).
DR BioMuta; IGLV1-51; -.
DR DMDM; 126543; -.
DR jPOST; P01701; -.
DR MassIVE; P01701; -.
DR PeptideAtlas; P01701; -.
DR Ensembl; ENST00000390290.3; ENSP00000374825.3; ENSG00000211644.3.
DR UCSC; uc062cbm.1; human.
DR AGR; HGNC:5882; -.
DR GeneCards; IGLV1-51; -.
DR HGNC; HGNC:5882; IGLV1-51.
DR HPA; ENSG00000211644; Tissue enhanced (intestine, lymphoid tissue, urinary bladder).
DR neXtProt; NX_P01701; -.
DR OpenTargets; ENSG00000211644; -.
DR VEuPathDB; HostDB:ENSG00000211644; -.
DR GeneTree; ENSGT00940000154293; -.
DR InParanoid; P01701; -.
DR OMA; QPGASLC; -.
DR PathwayCommons; P01701; -.
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-9664323; FCGR3A-mediated IL10 synthesis.
DR Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis.
DR Reactome; R-HSA-9679191; Potential therapeutics for SARS.
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 SignaLink; P01701; -.
DR Pharos; P01701; Tdark.
DR PRO; PR:P01701; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P01701; Protein.
DR Bgee; ENSG00000211644; Expressed in duodenum and 94 other cell types or tissues.
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:0019814; C:immunoglobulin complex; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0003823; F:antigen binding; NAS:UniProtKB.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0006955; P:immune response; IBA:GO_Central.
DR Gene3D; 2.60.40.10; Immunoglobulins; 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 PANTHER; PTHR23267:SF470; IMMUNOGLOBULIN LAMBDA VARIABLE 1-51; 1.
DR PANTHER; PTHR23267; IMMUNOGLOBULIN LIGHT CHAIN; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00406; IGv; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW Adaptive immunity; Cell membrane; Direct protein sequencing;
KW Disulfide bond; Immunity; Immunoglobulin; Immunoglobulin domain; Membrane;
KW Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:3929803,
FT ECO:0000269|PubMed:4177823, ECO:0000269|PubMed:6404900"
FT CHAIN 20..117
FT /note="Immunoglobulin lambda variable 1-51"
FT /evidence="ECO:0000269|PubMed:3929803,
FT ECO:0000269|PubMed:4177823, ECO:0000269|PubMed:6404900"
FT /id="PRO_0000059824"
FT DOMAIN 20..>117
FT /note="Ig-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT MOD_RES 20
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:4177823,
FT ECO:0000269|PubMed:6404900"
FT DISULFID 41..108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 29
FT /note="V -> L (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 36..38
FT /note="KVT -> RVS (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 36
FT /note="K -> E (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 44..46
FT /note="SSS -> GST (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 50..54
FT /note="NNYVS -> KNYVD (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 50..52
FT /note="NNY -> DNF (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="N -> D (in Ref. 1; CAA25598)"
FT /evidence="ECO:0000305"
FT CONFLICT 56..58
FT /note="YQQ -> HQH (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="L -> V (in Ref. 1; CAA25598)"
FT /evidence="ECO:0000305"
FT CONFLICT 69..70
FT /note="YD -> FN (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 70..71
FT /note="DN -> ED (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 82..84
FT /note="FSG -> ISA (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="Q -> R (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="D -> I (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="G -> A (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 112..117
FT /note="DSSLSA -> NNSLSG (in Ref. 1; CAA25598)"
FT /evidence="ECO:0000305"
FT CONFLICT 113..117
FT /note="SSLSA -> NRRSV (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="S -> N (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="A -> V (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 117
SQ SEQUENCE 117 AA; 12249 MW; 46700D34C2882B7F CRC64;
MTCSPLLLTL LIHCTGSWAQ SVLTQPPSVS AAPGQKVTIS CSGSSSNIGN NYVSWYQQLP
GTAPKLLIYD NNKRPSGIPD RFSGSKSGTS ATLGITGLQT GDEADYYCGT WDSSLSA
//
