LV327_HUMAN
ID LV327_HUMAN Reviewed; 113 AA.
AC P01718; A0A075B6J3;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2016, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Immunoglobulin lambda variable 3-27 {ECO:0000303|PubMed:11872955, ECO:0000303|Ref.4};
DE AltName: Full=Ig lambda chain V-IV region Kern {ECO:0000305|PubMed:5549568};
DE Flags: Precursor;
GN Name=IGLV3-27 {ECO:0000303|PubMed:11872955, ECO:0000303|Ref.4};
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 [LARGE SCALE GENOMIC DNA] (IMGT ALLELE IGLV3-27*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 [2]
RP PROTEIN SEQUENCE OF 21-113.
RX PubMed=5549568;
RA Ponstingl H., Hess M., Hilschmann N.;
RT "Structural rule of antibodies. Primary structure of a monoclonal
RT immunoglobulin-L-chain of the lambda type, subgroup IV (Bence-Jones-protein
RT Kern). V. The complete amino acid sequence and its genetic
RT interpretation.";
RL Hoppe-Seyler's Z. Physiol. Chem. 352:247-266(1971).
RN [3]
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 [4]
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 [5]
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 [6]
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 [7]
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 [8]
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 IGLV3-27*01.
CC -!- CAUTION: For an example of a full-length immunoglobulin lambda light
CC chain see AC P0DOX8. {ECO:0000305}.
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DR EMBL; AC244250; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A01984; L4HUKN.
DR AlphaFoldDB; P01718; -.
DR SMR; P01718; -.
DR IMGT_GENE-DB; IGLV3-27; -.
DR BioMuta; IGLV3-27; -.
DR jPOST; P01718; -.
DR MassIVE; P01718; -.
DR PeptideAtlas; P01718; -.
DR PRIDE; P01718; -.
DR TopDownProteomics; P01718; -.
DR Ensembl; ENST00000390304.2; ENSP00000374839.2; ENSG00000211658.2.
DR GeneCards; IGLV3-27; -.
DR HGNC; HGNC:5910; IGLV3-27.
DR HPA; ENSG00000211658; Tissue enriched (lymphoid).
DR neXtProt; NX_P01718; -.
DR OpenTargets; ENSG00000211658; -.
DR VEuPathDB; HostDB:ENSG00000211658; -.
DR GeneTree; ENSGT00940000153120; -.
DR OMA; ITCQGGI; -.
DR PhylomeDB; P01718; -.
DR PathwayCommons; P01718; -.
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-977606; Regulation of Complement cascade.
DR Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR Pharos; P01718; Tdark.
DR PRO; PR:P01718; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P01718; protein.
DR Bgee; ENSG00000211658; Expressed in lymph node and 82 other tissues.
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; -; 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; Direct protein sequencing;
KW Disulfide bond; Immunity; Immunoglobulin; Immunoglobulin domain; Membrane;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:5549568"
FT CHAIN 21..113
FT /note="Immunoglobulin lambda variable 3-27"
FT /evidence="ECO:0000269|PubMed:5549568"
FT /id="PRO_0000059847"
FT DOMAIN 21..>113
FT /note="Ig-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 41..106
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 22
FT /note="E -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 27
FT /note="S -> P (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 38
FT /note="R -> V (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 45..52
FT /note="VLAKKYAR -> NLEKTFVS (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="K -> R (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 61..63
FT /note="APV -> SPL (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 68..69
FT /note="KD -> HT (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="G -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 87..89
FT /note="TTV -> ATA (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 98..99
FT /note="VE -> SV (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 105..113
FT /note="YCYSAADNN -> FCQTWDTITA (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 113
SQ SEQUENCE 113 AA; 12165 MW; 2C653D17B5D75F7F CRC64;
MAWIPLLLPL LILCTVSVAS YELTQPSSVS VSPGQTARIT CSGDVLAKKY ARWFQQKPGQ
APVLVIYKDS ERPSGIPERF SGSSSGTTVT LTISGAQVED EADYYCYSAA DNN
