LV214_HUMAN
ID LV214_HUMAN Reviewed; 120 AA.
AC P01704; A0A075B6K1; P01711; P04209;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2016, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Immunoglobulin lambda variable 2-14 {ECO:0000303|PubMed:11872955, ECO:0000303|Ref.6};
DE AltName: Full=Ig lambda chain V-II region NIG-84 {ECO:0000305|PubMed:3922791};
DE AltName: Full=Ig lambda chain V-II region TOG {ECO:0000305|PubMed:500108};
DE AltName: Full=Ig lambda chain V-II region VIL {ECO:0000305|PubMed:5087637};
DE Flags: Precursor;
GN Name=IGLV2-14 {ECO:0000303|PubMed:11872955, ECO:0000303|Ref.6};
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 IGLV2-14*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 20-120.
RX PubMed=5087637;
RA Ponstingl H., Hilschmann N.;
RT "Structural rule of antibodies. Complete primary structure of a monoclonal
RT immunoglobin L chain of the lambda type, subgroup II (Bence Jones protein
RT VIL).";
RL Hoppe-Seyler's Z. Physiol. Chem. 352:859-877(1971).
RN [3]
RP PROTEIN SEQUENCE OF 20-120, AND PYROGLUTAMATE FORMATION AT GLN-20.
RX PubMed=500108; DOI=10.1016/0161-5890(79)90068-3;
RA Nabeshima Y., Ikenaka T.;
RT "Primary structure of cryo Bence-Jones protein (Tog) from the urine of a
RT patient with IgD myeloma.";
RL Mol. Immunol. 16:439-444(1979).
RN [4]
RP PROTEIN SEQUENCE OF 20-120.
RX PubMed=3922791; DOI=10.1016/0014-5793(85)80757-2;
RA Tonoike H., Kametani F., Hoshi A., Shinoda T., Isobe T.;
RT "Amino acid sequence of an amyloidogenic Bence Jones protein in myeloma-
RT associated systemic amyloidosis.";
RL FEBS Lett. 185:139-141(1985).
RN [5]
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 [6]
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 [7]
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 [8]
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 [9]
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 [10]
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 IGLV2-14*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; A01969; L2HUTG.
DR PIR; A01971; L2HUNG.
DR PIR; A01977; L2HUVL.
DR PDB; 5C2B; X-ray; 1.40 A; L=20-111.
DR PDB; 5C6W; X-ray; 1.54 A; H/J=20-120.
DR PDB; 5CBA; X-ray; 2.50 A; B/D=20-111.
DR PDB; 5CBE; X-ray; 2.40 A; B/D=20-109.
DR PDB; 6SM1; X-ray; 1.55 A; A=20-118.
DR PDBsum; 5C2B; -.
DR PDBsum; 5C6W; -.
DR PDBsum; 5CBA; -.
DR PDBsum; 5CBE; -.
DR PDBsum; 6SM1; -.
DR AlphaFoldDB; P01704; -.
DR SMR; P01704; -.
DR IMGT_GENE-DB; IGLV2-14; -.
DR BioMuta; IGLV2-14; -.
DR DMDM; 126552; -.
DR jPOST; P01704; -.
DR MassIVE; P01704; -.
DR PeptideAtlas; P01704; -.
DR PRIDE; P01704; -.
DR Ensembl; ENST00000390312.2; ENSP00000374847.2; ENSG00000211666.2.
DR GeneCards; IGLV2-14; -.
DR HGNC; HGNC:5888; IGLV2-14.
DR HPA; ENSG00000211666; Tissue enhanced (intestine, lymphoid tissue, stomach).
DR neXtProt; NX_P01704; -.
DR OpenTargets; ENSG00000211666; -.
DR VEuPathDB; HostDB:ENSG00000211666; -.
DR GeneTree; ENSGT00940000154179; -.
DR OMA; QKITITC; -.
DR PhylomeDB; P01704; -.
DR PathwayCommons; P01704; -.
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 ChiTaRS; IGLV2-14; human.
DR Pharos; P01704; Tdark.
DR PRO; PR:P01704; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P01704; protein.
DR Bgee; ENSG00000211666; Expressed in duodenum and 96 other tissues.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
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:3922791,
FT ECO:0000269|PubMed:500108, ECO:0000269|PubMed:5087637"
FT CHAIN 20..120
FT /note="Immunoglobulin lambda variable 2-14"
FT /evidence="ECO:0000269|PubMed:3922791,
FT ECO:0000269|PubMed:500108, ECO:0000269|PubMed:5087637"
FT /id="PRO_0000059830"
FT DOMAIN 20..119
FT /note="Ig-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT MOD_RES 20
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:500108"
FT DISULFID 41..109
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 20
FT /note="Q -> H (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 31
FT /note="G -> A (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="P -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 45..52
FT /note="SSDVGGYN -> TNDIGSYS (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="S -> T (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 52..53
FT /note="NY -> DF (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="Y -> F (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="H -> Y (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="K -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 67..74
FT /note="LMIYEVSN -> VLIFDVNS (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 68..70
FT /note="MIY -> IIS (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="M -> L (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 71..74
FT /note="EVSN -> DVNS (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="S -> R (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="V -> I (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="N -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="N -> H (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="G -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 106..108
FT /note="DYY -> HYF (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 112..120
FT /note="YTSSSTLHS -> FTTTNSRAV (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 113..120
FT /note="TSSSTLHS -> RTSGTIIF (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 116..120
FT /note="STLHS -> NSVVF (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 120
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:5C6W"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:5C6W"
FT TURN 45..50
FT /evidence="ECO:0007829|PDB:5C6W"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:5C6W"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:5C6W"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:5C6W"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:5C6W"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:5C6W"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:5C6W"
FT STRAND 105..112
FT /evidence="ECO:0007829|PDB:5C6W"
SQ SEQUENCE 120 AA; 12597 MW; 76569E85B25B5611 CRC64;
MAWALLLLTL LTQGTGSWAQ SALTQPASVS GSPGQSITIS CTGTSSDVGG YNYVSWYQQH
PGKAPKLMIY EVSNRPSGVS NRFSGSKSGN TASLTISGLQ AEDEADYYCS SYTSSSTLHS
