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Immunoglobulin lambda variable 1-47 (Ig lambda chain V-I region HA) (Ig lambda chain V-I region WAH)

 LV147_HUMAN             Reviewed;         117 AA.
P01700; A0A075B6I8; P04208;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
02-NOV-2016, sequence version 2.
25-OCT-2017, entry version 103.
RecName: Full=Immunoglobulin lambda variable 1-47 {ECO:0000303|PubMed:11872955, ECO:0000303|Ref.5};
AltName: Full=Ig lambda chain V-I region HA {ECO:0000305|PubMed:5532227};
AltName: Full=Ig lambda chain V-I region WAH {ECO:0000305|PubMed:6407018};
Flags: Precursor;
Name=IGLV1-47 {ECO:0000303|PubMed:11872955, ECO:0000303|Ref.5};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE
IGLV1-47*02).
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).
[2]
PROTEIN SEQUENCE OF 20-117, AND PYROGLUTAMATE FORMATION AT GLN-20.
PubMed=5532227;
Shinoda T., Titani K., Putnam F.W.;
"Amino acid sequence of human lambda chains. II. Chymotryptic peptides
and sequence of protein Ha.";
J. Biol. Chem. 245:4475-4487(1970).
[3]
PROTEIN SEQUENCE OF 20-117.
PubMed=6407018; DOI=10.1073/pnas.80.12.3686;
Takahashi Y., Takahashi N., Tetaert D., Putnam F.W.;
"Complete covalent structure of a human immunoglobulin D: sequence of
the lambda light chain.";
Proc. Natl. Acad. Sci. U.S.A. 80:3686-3690(1983).
[4]
NOMEMCLATURE.
PubMed=11872955;
Lefranc M.P.;
"Nomenclature of the human immunoglobulin lambda (IGL) genes.";
Exp. Clin. Immunogenet. 18:242-254(2001).
[5]
NOMENCLATURE.
Lefranc M.P., Lefranc G.;
"The Immunoglobulin FactsBook.";
(In) Lefranc M.P., Lefranc G. (eds.);
The Immunoglobulin FactsBook., pp.1-458, Academic Press, London.
(2001).
[6]
REVIEW ON SOMATIC HYPERMUTATION.
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).
[7]
REVIEW ON IMMUNOGLOBULINS.
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).
[8]
REVIEW ON FUNCTION.
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).
[9]
NOMENCLATURE.
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,
ECO:0000303|PubMed:24600447}.
-!- SUBUNIT: Immunoglobulins are composed of two identical heavy
chains and two identical light chains; disulfide-linked.
{ECO:0000303|PubMed:20176268}.
-!- 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 IGLV1-47*02.
-!- CAUTION: For an example of a full-length immunoglobulin lambda
light chain see AC P0DOX8. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AC245060; -; NOT_ANNOTATED_CDS; Genomic_DNA.
PIR; A01963; L1HUHA.
PIR; A01967; L1HUWA.
PDB; 1ZVO; X-ray; -; A/B=20-115.
PDBsum; 1ZVO; -.
ProteinModelPortal; P01700; -.
SMR; P01700; -.
IntAct; P01700; 3.
IMGT_GENE-DB; IGLV1-47; -.
DMDM; 126539; -.
DMDM; 126547; -.
PeptideAtlas; P01700; -.
PRIDE; P01700; -.
Ensembl; ENST00000390294; ENSP00000374829; ENSG00000211648.
EuPathDB; HostDB:ENSG00000211648.2; -.
GeneCards; IGLV1-47; -.
HGNC; HGNC:5880; IGLV1-47.
neXtProt; NX_P01700; -.
OpenTargets; ENSG00000211648; -.
GeneTree; ENSGT00900000140816; -.
HOVERGEN; HBG018013; -.
OMA; CHSYDES; -.
PhylomeDB; P01700; -.
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:P01700; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000211648; -.
GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA: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; 2.60.40.10; -; 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.
PROSITE; PS50835; IG_LIKE; 1.
1: Evidence at protein level;
3D-structure; Adaptive immunity; Cell membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; Immunity;
Immunoglobulin domain; Immunoglobulin V region; Membrane;
Polymorphism; Pyrrolidone carboxylic acid; Reference proteome;
Secreted; Signal.
SIGNAL 1 19 {ECO:0000269|PubMed:5532227,
ECO:0000269|PubMed:6407018}.
CHAIN 20 117 Immunoglobulin lambda variable 1-47.
{ECO:0000269|PubMed:5532227,
ECO:0000269|PubMed:6407018}.
/FTId=PRO_0000059823.
DOMAIN 20 >117 Ig-like. {ECO:0000255|PROSITE-
ProRule:PRU00114}.
MOD_RES 20 20 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:5532227}.
DISULFID 41 108 {ECO:0000255|PROSITE-ProRule:PRU00114}.
CONFLICT 29 29 A -> V (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 42 42 S -> F (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 44 44 S -> G (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 48 50 IGS -> GTGN (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 50 51 SN -> RY (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 63 63 A -> T (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 70 73 SNNQ -> RDDK (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 70 71 SN -> KD (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 105 107 DYY -> HYH (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 113 114 DS -> YR (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 116 117 SG -> WV (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 117 117 G -> A (in Ref. 2; AA sequence).
{ECO:0000305}.
NON_TER 117 117
SEQUENCE 117 AA; 12284 MW; A80939A5F5AB2506 CRC64;
MAGFPLLLTL LTHCAGSWAQ SVLTQPPSAS GTPGQRVTIS CSGSSSNIGS NYVYWYQQLP
GTAPKLLIYS NNQRPSGVPD RFSGSKSGTS ASLAISGLRS EDEADYYCAA WDDSLSG


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