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   27-MAR-2024, entry version 165.
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   EMDB; EMD-14885; -.
DR   EMDB; EMD-22156; -.
DR   EMDB; EMD-32442; -.
DR   EMDB; EMD-32448; -.
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   Ensembl; ENST00000620395.2; ENSP00000482937.2; ENSG00000278196.3.
DR   AGR; HGNC:5895; -.
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   InParanoid; P01709; -.
DR   OMA; RSETKTC; -.
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-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; 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 91 other cell types or 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; 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:SF437; IMMUNOGLOBULIN LAMBDA VARIABLE 2-8; 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   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
//