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Immunoglobulin lambda variable 1-51 (Ig lambda chain V-I region BL2) (Ig lambda chain V-I region EPS) (Ig lambda chain V-I region NEW) (Ig lambda chain V-I region NIG-64)

 LV151_HUMAN             Reviewed;         117 AA.
P01701; A0A075B6I5; P01702; P06316; P06888;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
07-SEP-2016, sequence version 2.
10-OCT-2018, entry version 106.
RecName: Full=Immunoglobulin lambda variable 1-51 {ECO:0000303|PubMed:11872955, ECO:0000303|Ref.7};
AltName: Full=Ig lambda chain V-I region BL2 {ECO:0000305|PubMed:6095199};
AltName: Full=Ig lambda chain V-I region EPS {ECO:0000305|PubMed:3929803};
AltName: Full=Ig lambda chain V-I region NEW {ECO:0000305|PubMed:4177823};
AltName: Full=Ig lambda chain V-I region NIG-64 {ECO:0000305|PubMed:6404900};
Flags: Precursor;
Name=IGLV1-51 {ECO:0000303|PubMed:11872955, ECO:0000303|Ref.7};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
PubMed=6095199; DOI=10.1093/nar/12.22.8407;
Tsujimoto Y., Croce C.M.;
"Molecular cloning of a human immunoglobulin lambda chain variable
Nucleic Acids Res. 12:8407-8414(1984).
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
Khan A.S., Lane L., Tilahun Y., Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
Langer B., Steinmetz-Kayne M., Hilschmann N.;
"The complete amino acid sequence of Bence Jones protein New (lambda-
type). Subgroups in the variable part of immunoglobulin L-chains of
the lambda-type.";
Hoppe-Seyler's Z. Physiol. Chem. 349:945-951(1968).
Kametani F., Takayasu T., Suzuki S., Shinoda T., Okuyama T.,
Shimizu A.;
"Comparative studies on the structure of the light chains of human
immunoglobulins. IV. Assignment of a subsubgroup.";
J. Biochem. 93:421-429(1983).
Toft K.G., Sletten K., Husby G.;
"The amino-acid sequence of the variable region of a carbohydrate-
containing amyloid fibril protein EPS (immunoglobulin light chain,
type lambda).";
Biol. Chem. Hoppe-Seyler 366:617-625(1985).
Lefranc M.P.;
"Nomenclature of the human immunoglobulin lambda (IGL) genes.";
Exp. Clin. Immunogenet. 18:242-254(2001).
Lefranc M.P., Lefranc G.;
"The Immunoglobulin FactsBook.";
(In) Lefranc M.P., Lefranc G. (eds.);
The Immunoglobulin FactsBook., pp.1-458, Academic Press, London.
PubMed=17576170; DOI=10.1146/annurev.genet.41.110306.130340;
Teng G., Papavasiliou F.N.;
"Immunoglobulin somatic hypermutation.";
Annu. Rev. Genet. 41:107-120(2007).
PubMed=20176268; DOI=10.1016/j.jaci.2009.09.046;
Schroeder H.W. Jr., Cavacini L.;
"Structure and function of immunoglobulins.";
J. Allergy Clin. Immunol. 125:S41-S52(2010).
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
PubMed=22158414; DOI=10.1038/nri3128;
McHeyzer-Williams M., Okitsu S., Wang N., McHeyzer-Williams L.;
"Molecular programming of B cell memory.";
Nat. Rev. Immunol. 12:24-34(2012).
PubMed=24600447; DOI=10.3389/fimmu.2014.00022;
Lefranc M.P.;
"Immunoglobulin and T Cell Receptor Genes: IMGT((R)) and the Birth and
Rise of Immunoinformatics.";
Front. Immunol. 5:22-22(2014).
-!- FUNCTION: V region of the variable domain of immunoglobulin light
chains that participates in the antigen recognition
(PubMed:24600447). Immunoglobulins, also known as antibodies, are
membrane-bound or secreted glycoproteins produced by B
lymphocytes. In the recognition phase of humoral immunity, the
membrane-bound immunoglobulins serve as receptors which, upon
binding of a specific antigen, trigger the clonal expansion and
differentiation of B lymphocytes into immunoglobulins-secreting
plasma cells. Secreted immunoglobulins mediate the effector phase
of humoral immunity, which results in the elimination of bound
antigens (PubMed:20176268, PubMed:22158414). The antigen binding
site is formed by the variable domain of one heavy chain, together
with that of its associated light chain. Thus, each immunoglobulin
has two antigen binding sites with remarkable affinity for a
particular antigen. The variable domains are assembled by a
process called V-(D)-J rearrangement and can then be subjected to
somatic hypermutations which, after exposure to antigen and
selection, allow affinity maturation for a particular antigen
(PubMed:17576170, PubMed:20176268). {ECO:0000303|PubMed:17576170,
ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414,
-!- SUBUNIT: Immunoglobulins are composed of two identical heavy
chains and two identical light chains; disulfide-linked.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268,
ECO:0000303|PubMed:22158414}. Cell membrane
{ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
-!- POLYMORPHISM: There are several alleles. The sequence shown is
that of IMGT allele IGLV1-51*01.
-!- CAUTION: For an example of a full-length immunoglobulin lambda
light chain see AC P0DOX8. {ECO:0000305}.
Sequence=CAA25598.1; Type=Miscellaneous discrepancy; Note=Chimeric mRNA corresponding to regions V and J of immunoglobulin kappa light chain.; Evidence={ECO:0000305};
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
EMBL; X01147; CAA25598.1; ALT_SEQ; mRNA.
EMBL; AC245060; -; NOT_ANNOTATED_CDS; Genomic_DNA.
PIR; A01964; L1HUNW.
PIR; A01965; L1HUNG.
PIR; A01966; L1HUBL.
PIR; A24656; L1HUEP.
ProteinModelPortal; P01701; -.
SMR; P01701; -.
DMDM; 126543; -.
PeptideAtlas; P01701; -.
PRIDE; P01701; -.
ProteomicsDB; 51429; -.
ProteomicsDB; 51430; -.
ProteomicsDB; 51890; -.
ProteomicsDB; 51942; -.
Ensembl; ENST00000390290; ENSP00000374825; ENSG00000211644.
UCSC; uc062cbm.1; human.
EuPathDB; HostDB:ENSG00000211644.2; -.
GeneCards; IGLV1-51; -.
HGNC; HGNC:5882; IGLV1-51.
neXtProt; NX_P01701; -.
OpenTargets; ENSG00000211644; -.
GeneTree; ENSGT00900000140816; -.
HOVERGEN; HBG018013; -.
Reactome; R-HSA-166663; Initial triggering of complement.
Reactome; R-HSA-173623; Classical antibody-mediated complement activation.
Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
Reactome; R-HSA-2029481; FCGR activation.
Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-HSA-2029485; Role of phospholipids in phagocytosis.
Reactome; R-HSA-2168880; Scavenging of heme from plasma.
Reactome; R-HSA-2454202; Fc epsilon receptor (FCERI) signaling.
Reactome; R-HSA-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
Reactome; R-HSA-2871796; FCERI mediated MAPK activation.
Reactome; R-HSA-2871809; FCERI mediated Ca+2 mobilization.
Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
Reactome; R-HSA-5690714; CD22 mediated BCR regulation.
Reactome; R-HSA-977606; Regulation of Complement cascade.
Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
PRO; PR:P01701; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000211644; Expressed in 88 organ(s), highest expression level in lymph node.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0003823; F:antigen binding; NAS:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
GO; GO:0006956; P:complement activation; TAS:Reactome.
GO; GO:0006958; P:complement activation, classical pathway; TAS:Reactome.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
GO; GO:0006955; P:immune response; NAS:UniProtKB.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0006898; P:receptor-mediated endocytosis; TAS:Reactome.
GO; GO:0030449; P:regulation of complement activation; TAS:Reactome.
GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
Gene3D;; -; 1.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR013106; Ig_V-set.
Pfam; PF07686; V-set; 1.
SMART; SM00409; IG; 1.
SMART; SM00406; IGv; 1.
SUPFAM; SSF48726; SSF48726; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Direct protein sequencing;
Disulfide bond; Immunoglobulin domain; Immunoglobulin V region;
Membrane; Polymorphism; Pyrrolidone carboxylic acid;
Reference proteome; Secreted; Signal.
SIGNAL 1 19 {ECO:0000269|PubMed:3929803,
CHAIN 20 117 Immunoglobulin lambda variable 1-51.
DOMAIN 20 >117 Ig-like. {ECO:0000255|PROSITE-
MOD_RES 20 20 Pyrrolidone carboxylic acid.
DISULFID 41 108 {ECO:0000255|PROSITE-ProRule:PRU00114}.
CONFLICT 29 29 V -> L (in Ref. 5; AA sequence).
CONFLICT 36 38 KVT -> RVS (in Ref. 5; AA sequence).
CONFLICT 36 36 K -> E (in Ref. 4; AA sequence).
CONFLICT 44 46 SSS -> GST (in Ref. 3; AA sequence).
CONFLICT 50 54 NNYVS -> KNYVD (in Ref. 5; AA sequence).
CONFLICT 50 52 NNY -> DNF (in Ref. 4; AA sequence).
CONFLICT 51 51 N -> D (in Ref. 1; CAA25598).
CONFLICT 56 58 YQQ -> HQH (in Ref. 3; AA sequence).
CONFLICT 59 59 L -> V (in Ref. 1; CAA25598).
CONFLICT 69 70 YD -> FN (in Ref. 5; AA sequence).
CONFLICT 70 71 DN -> ED (in Ref. 3; AA sequence).
CONFLICT 82 84 FSG -> ISA (in Ref. 3; AA sequence).
CONFLICT 99 99 Q -> R (in Ref. 3; AA sequence).
CONFLICT 105 105 D -> I (in Ref. 5; AA sequence).
CONFLICT 109 109 G -> A (in Ref. 3; AA sequence).
CONFLICT 112 117 DSSLSA -> NNSLSG (in Ref. 1; CAA25598).
CONFLICT 113 117 SSLSA -> NRRSV (in Ref. 5; AA sequence).
CONFLICT 116 116 S -> N (in Ref. 3; AA sequence).
CONFLICT 117 117 A -> V (in Ref. 4; AA sequence).
NON_TER 117 117
SEQUENCE 117 AA; 12249 MW; 46700D34C2882B7F CRC64;

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