LV208_HUMAN
ID LV208_HUMAN Reviewed; 118 AA.
AC P01709; A0A087WZW9; P01710;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2016, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Immunoglobulin lambda variable 2-8 {ECO:0000303|PubMed:11872955, ECO:0000303|Ref.5};
DE AltName: Full=Ig lambda chain V-II region BO {ECO:0000305|PubMed:5532228};
DE AltName: Full=Ig lambda chain V-II region MGC {ECO:0000305|PubMed:4415202};
DE Flags: Precursor;
GN Name=IGLV2-8 {ECO:0000303|PubMed:11872955, ECO:0000303|Ref.5};
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 IGLV2-8*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 20-118, AND PYROGLUTAMATE FORMATION AT GLN-20.
RX PubMed=5532228; DOI=10.1016/s0021-9258(19)63819-6;
RA Wikler M., Putnam F.W.;
RT "Amino acid sequence of human lambda chains. 3. Tryptic peptides,
RT chymotryptic peptides, and sequence of protein Bo.";
RL J. Biol. Chem. 245:4488-4507(1970).
RN [3]
RP PROTEIN SEQUENCE OF 20-118, AND PYROGLUTAMATE FORMATION AT GLN-20.
RX PubMed=4415202; DOI=10.1021/bi00717a007;
RA Fett J.W., Deutsch H.F.;
RT "Primary structure of the Mcg lambda chain.";
RL Biochemistry 13:4102-4114(1974).
RN [4]
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 [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. (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 Rise
RT of Immunoinformatics.";
RL Front. Immunol. 5:22-22(2014).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 21-118.
RX PubMed=2515285; DOI=10.1016/0022-2836(89)90135-6;
RA Ely K.R., Herron J.N., Harker M., Edmundson A.B.;
RT "Three-dimensional structure of a light chain dimer crystallized in water.
RT Conformational flexibility of a molecule in two crystal forms.";
RL J. Mol. Biol. 210:601-615(1989).
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 IGLV2-8*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; AC245028; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A01976; L2HUBO.
DR PIR; A90381; L2HUMC.
DR PDB; 1A8J; X-ray; 2.70 A; H/L=21-118.
DR PDB; 1DCL; X-ray; 2.30 A; A/B=21-118.
DR PDB; 1MCW; X-ray; 3.50 A; M=21-118.
DR PDB; 2MCG; X-ray; 2.00 A; 1/2=21-118.
DR PDB; 3MCG; X-ray; 2.00 A; 1/2=21-118.
DR PDB; 4UNT; X-ray; 2.70 A; A/B/C/D/E/F/G/H=20-118.
DR PDB; 4UNU; X-ray; 0.95 A; A/B=20-118.
DR PDB; 4UNV; X-ray; 1.60 A; A=20-118.
DR PDB; 5ACL; X-ray; 1.49 A; A=20-118.
DR PDB; 5ACM; X-ray; 1.05 A; A/B=20-118.
DR PDBsum; 1A8J; -.
DR PDBsum; 1DCL; -.
DR PDBsum; 1MCW; -.
DR PDBsum; 2MCG; -.
DR PDBsum; 3MCG; -.
DR PDBsum; 4UNT; -.
DR PDBsum; 4UNU; -.
DR PDBsum; 4UNV; -.
DR PDBsum; 5ACL; -.
DR PDBsum; 5ACM; -.
DR AlphaFoldDB; P01709; -.
DR SMR; P01709; -.
DR MINT; P01709; -.
DR DrugBank; DB03088; Pidolic acid.
DR IMGT_GENE-DB; IGLV2-8; -.
DR BioMuta; IGLV2-8; -.
DR DMDM; 126560; -.
DR jPOST; P01709; -.
DR MassIVE; P01709; -.
DR PeptideAtlas; P01709; -.
DR PRIDE; P01709; -.
DR Ensembl; ENST00000620395.2; ENSP00000482937.2; ENSG00000278196.3.
DR GeneCards; IGLV2-8; -.
DR HGNC; HGNC:5895; IGLV2-8.
DR HPA; ENSG00000278196; Tissue enhanced (intestine, lymphoid tissue).
DR neXtProt; NX_P01709; -.
DR OpenTargets; ENSG00000278196; -.
DR VEuPathDB; HostDB:ENSG00000278196; -.
DR GeneTree; ENSGT00940000154179; -.
DR OMA; YYCSSPR; -.
DR PathwayCommons; P01709; -.
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 SignaLink; P01709; -.
DR ChiTaRS; IGLV2-8; human.
DR EvolutionaryTrace; P01709; -.
DR Pharos; P01709; Tdark.
DR PRO; PR:P01709; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P01709; protein.
DR Bgee; ENSG00000278196; Expressed in duodenum and 90 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 3D-structure; 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:4415202,
FT ECO:0000269|PubMed:5532228"
FT CHAIN 20..118
FT /note="Immunoglobulin lambda variable 2-8"
FT /evidence="ECO:0000269|PubMed:4415202,
FT ECO:0000269|PubMed:5532228"
FT /id="PRO_0000059835"
FT DOMAIN 20..>118
FT /note="Ig-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REGION 76..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 20
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:4415202,
FT ECO:0000269|PubMed:5532228"
FT DISULFID 41..109
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 33
FT /note="P -> L (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 50..52
FT /note="GYN -> DNK (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="P -> A (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="K -> R (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 67..68
FT /note="LM -> VI (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 68..70
FT /note="MIY -> VIF (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="S -> N (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="K -> Q (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="G -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="Q -> R (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 113..115
FT /note="AGS -> VDN (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="A -> E (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="N -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 118
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:4UNU"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:4UNU"
FT TURN 45..50
FT /evidence="ECO:0007829|PDB:4UNU"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:4UNU"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:1A8J"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:4UNU"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:4UNU"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:2MCG"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:4UNU"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:4UNU"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:4UNU"
FT STRAND 105..112
FT /evidence="ECO:0007829|PDB:4UNU"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:2MCG"
SQ SEQUENCE 118 AA; 12382 MW; B94EEE11F9DA8260 CRC64;
MAWALLLLTL LTQGTGSWAQ SALTQPPSAS GSPGQSVTIS CTGTSSDVGG YNYVSWYQQH
PGKAPKLMIY EVSKRPSGVP DRFSGSKSGN TASLTVSGLQ AEDEADYYCS SYAGSNNF
