LV144_HUMAN
ID LV144_HUMAN Reviewed; 117 AA.
AC P01699; A0A0B4J1U1; A0A0G2JQC2; A0A0U1RVH6; P06887;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2016, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Immunoglobulin lambda variable 1-44 {ECO:0000303|PubMed:11872955, ECO:0000303|Ref.5};
DE AltName: Full=Ig lambda chain V-I region MEM {ECO:0000305|PubMed:2410269};
DE AltName: Full=Ig lambda chain V-I region VOR {ECO:0000305|PubMed:809332};
DE Flags: Precursor;
GN Name=IGLV1-44 {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 IGLV1-44*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 20-117, AND PYROGLUTAMATE FORMATION AT GLN-20.
RX PubMed=809332;
RA Engelhard M., Hilschmann N.;
RT "Pattern of antibody structure. The amino acid sequence of a monoclonal
RT immunoglobulin L-chain of lambda-type, subgroup I (Bence-Jones-protein
RT Vor.). A contribution to the elucidation of the origin of antibody
RT specificity.";
RL Hoppe-Seyler's Z. Physiol. Chem. 356:1413-1444(1975).
RN [3]
RP PROTEIN SEQUENCE OF 20-117, AND PYROGLUTAMATE FORMATION AT GLN-20.
RX PubMed=2410269; DOI=10.1111/j.1432-1033.1985.tb09027.x;
RA Mihaesco E., Roy J.P., Congy N., Peran-Rivat L., Mihaesco C.;
RT "The amino acid sequence of a lambda light chain presenting abnormal
RT physicochemical and antigenic features.";
RL Eur. J. Biochem. 150:349-357(1985).
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).
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 IGLV1-44*01.
CC -!- CAUTION: For an example of a full-length immunoglobulin lambda light
CC chain see AC P0DOX8. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC245291; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A01962; L1HUVO.
DR PIR; A25479; L1HUMM.
DR AlphaFoldDB; P01699; -.
DR PCDDB; P01699; -.
DR SMR; P01699; -.
DR IMGT_GENE-DB; IGLV1-44; -.
DR BioMuta; IGLV1-44; -.
DR DMDM; 126537; -.
DR jPOST; P01699; -.
DR MassIVE; P01699; -.
DR PeptideAtlas; P01699; -.
DR PRIDE; P01699; -.
DR Ensembl; ENST00000390297.3; ENSP00000374832.3; ENSG00000211651.3.
DR Ensembl; ENST00000628287.1; ENSP00000485735.1; ENSG00000274854.2.
DR GeneCards; IGLV1-44; -.
DR HGNC; HGNC:5879; IGLV1-44.
DR HPA; ENSG00000211651; Tissue enhanced (intestine, lymphoid tissue, stomach).
DR neXtProt; NX_P01699; -.
DR OpenTargets; ENSG00000211651; -.
DR VEuPathDB; HostDB:ENSG00000211651; -.
DR GeneTree; ENSGT00940000154293; -.
DR OMA; EADYFCH; -.
DR PhylomeDB; P01699; -.
DR PathwayCommons; P01699; -.
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; IGLV1-44; human.
DR Pharos; P01699; Tdark.
DR PRO; PR:P01699; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P01699; protein.
DR Bgee; ENSG00000211651; Expressed in rectum and 93 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 Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:2410269,
FT ECO:0000269|PubMed:809332"
FT CHAIN 20..117
FT /note="Immunoglobulin lambda variable 1-44"
FT /evidence="ECO:0000269|PubMed:2410269,
FT ECO:0000269|PubMed:809332"
FT /id="PRO_0000059822"
FT DOMAIN 20..>117
FT /note="Ig-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REGION 24..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 20
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:2410269,
FT ECO:0000269|PubMed:809332"
FT DISULFID 41..108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 35
FT /note="Q -> G (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 44..47
FT /note="SSSN -> GNFD (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="I -> V (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 50..52
FT /note="SNT -> RNS (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 52..54
FT /note="TVN -> ZPAY (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 58..59
FT /note="QL -> VH (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="K -> R (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 70..71
FT /note="SN -> NY (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 71..72
FT /note="NN -> SD (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="P -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 84..86
FT /note="GSK -> ASR (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="D -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="Y -> F (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="A -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="N -> D (in Ref. 2; AA sequence and 3; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 117
SQ SEQUENCE 117 AA; 12201 MW; 5302215AD2E70E7C CRC64;
MASFPLLLTL LTHCAGSWAQ SVLTQPPSAS GTPGQRVTIS CSGSSSNIGS NTVNWYQQLP
GTAPKLLIYS NNQRPSGVPD RFSGSKSGTS ASLAISGLQS EDEADYYCAA WDDSLNG
