IGLC1_HUMAN
ID IGLC1_HUMAN Reviewed; 106 AA.
AC P0CG04; A0A075B6K8; A0M8Q4; P01842; P80423;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Immunoglobulin lambda constant 1 {ECO:0000303|PubMed:11872955, ECO:0000303|Ref.6};
DE AltName: Full=Ig lambda chain C region MGC {ECO:0000305|PubMed:4415202};
DE AltName: Full=Ig lambda-1 chain C region {ECO:0000305};
GN Name=IGLC1 {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 PROTEIN SEQUENCE.
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (IMGT ALLELE IGLC1*02).
RX PubMed=2115572; DOI=10.1084/jem.172.2.609;
RA Vasicek T.J., Leder P.;
RT "Structure and expression of the human immunoglobulin lambda genes.";
RL J. Exp. Med. 172:609-620(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE IGLC1*02).
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-106.
RX PubMed=6273747; DOI=10.1038/294536a0;
RA Hieter P.A., Hollis G.F., Korsmeyer S.J., Waldmann T.A., Leder P.;
RT "Clustered arrangement of immunoglobulin lambda constant region genes in
RT man.";
RL Nature 294:536-540(1981).
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 SEROLOGICAL ISOTYPE.
RA Lefranc M.-P., Lefranc G.;
RT "Immunoglobulin lambda (IGL) genes of human and mouse.";
RL (In) Honjo T., Alt F.W., Neuberger M. (eds.);
RL Molecular Biology of B Cells, pp.37-59, Elsevier Academic Press, London
RL (2004).
RN [8]
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 [9]
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 [10]
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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Tear;
RX PubMed=25946035; DOI=10.1021/acs.jproteome.5b00179;
RA Azkargorta M., Soria J., Ojeda C., Guzman F., Acera A., Iloro I.,
RA Suarez T., Elortza F.;
RT "Human basal tear peptidome characterization by CID, HCD, and ETD followed
RT by in silico and in vitro analyses for antimicrobial peptide
RT identification.";
RL J. Proteome Res. 14:2649-2658(2015).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RA Edmundson A.B., Ely K.R., Abola E.E., Schiffer M., Panagiotopoulos N.;
RT "Rotational allomerism and divergent evolution of domains in immunoglobulin
RT light chains.";
RL Biochemistry 14:3953-3961(1975).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
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: Constant region of immunoglobulin light chains.
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:22158414, PubMed:20176268). 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}.
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 IGLC1*02. {ECO:0000305}.
CC -!- CAUTION: For an example of a full-length immunoglobulin lambda light
CC chain see AC P0DOX8. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA36047.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X51755; CAA36047.1; ALT_INIT; Genomic_DNA.
DR EMBL; AC245028; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; J00252; AAA59106.1; -; Genomic_DNA.
DR PIR; A92057; L2HU.
DR PDB; 1ZVO; X-ray; -; A/B=9-106.
DR PDB; 2FB4; X-ray; 1.90 A; L=1-106.
DR PDB; 2IG2; X-ray; 3.00 A; L=1-106.
DR PDBsum; 1ZVO; -.
DR PDBsum; 2FB4; -.
DR PDBsum; 2IG2; -.
DR AlphaFoldDB; P0CG04; -.
DR SMR; P0CG04; -.
DR ComplexPortal; CPX-6906; IgD - Ig lambda 1 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6922; IgM - Ig lambda 1 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6931; IgG1 - Ig lambda 1 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6938; IgG2 - Ig lambda 1 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6944; IgG3 - Ig lambda 1 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6950; IgG4 - Ig lambda 1 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6956; IgA1 - Ig lambda 1 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6963; IgA2 - Ig lambda 1 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6970; IgE - Ig lambda 1 immunoglobulin complex, constant regions.
DR IntAct; P0CG04; 11.
DR MINT; P0CG04; -.
DR DrugBank; DB03088; Pidolic acid.
DR IMGT_GENE-DB; IGLC1; -.
DR GlyGen; P0CG04; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P0CG04; -.
DR BioMuta; IGLC1; -.
DR DMDM; 298351713; -.
DR jPOST; P0CG04; -.
DR MassIVE; P0CG04; -.
DR MaxQB; P0CG04; -.
DR PeptideAtlas; P0CG04; -.
DR PRIDE; P0CG04; -.
DR UCSC; uc062cdy.1; human.
DR GeneCards; IGLC1; -.
DR HGNC; HGNC:5855; IGLC1.
DR MIM; 147220; gene.
DR neXtProt; NX_P0CG04; -.
DR InParanoid; P0CG04; -.
DR PhylomeDB; P0CG04; -.
DR PathwayCommons; P0CG04; -.
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; P0CG04; -.
DR EvolutionaryTrace; P0CG04; -.
DR Pharos; P0CG04; Tdark.
DR PRO; PR:P0CG04; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; P0CG04; protein.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
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; HDA:UniProtKB.
DR GO; GO:0071745; C:IgA immunoglobulin complex; IC:ComplexPortal.
DR GO; GO:0071738; C:IgD immunoglobulin complex; IC:ComplexPortal.
DR GO; GO:0071742; C:IgE immunoglobulin complex; IC:ComplexPortal.
DR GO; GO:0071735; C:IgG immunoglobulin complex; IC:ComplexPortal.
DR GO; GO:0071753; C:IgM immunoglobulin complex; IC:ComplexPortal.
DR GO; GO:0042571; C:immunoglobulin complex, circulating; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0003823; F:antigen binding; IBA:GO_Central.
DR GO; GO:0034987; F:immunoglobulin receptor binding; IBA:GO_Central.
DR GO; GO:0002250; P:adaptive immune response; IC:ComplexPortal.
DR GO; GO:0050853; P:B cell receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0006958; P:complement activation, classical pathway; IBA:GO_Central.
DR GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
DR GO; GO:0006955; P:immune response; NAS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0006911; P:phagocytosis, engulfment; IBA:GO_Central.
DR GO; GO:0006910; P:phagocytosis, recognition; IBA:GO_Central.
DR GO; GO:0050871; P:positive regulation of B cell activation; 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; IPR003006; Ig/MHC_CS.
DR InterPro; IPR003597; Ig_C1-set.
DR Pfam; PF07654; C1-set; 1.
DR SMART; SM00407; IGc1; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS00290; IG_MHC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Bence-Jones protein; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Immunity; Immunoglobulin;
KW Immunoglobulin domain; Membrane; Reference proteome; Secreted.
FT CHAIN <1..106
FT /note="Immunoglobulin lambda constant 1"
FT /id="PRO_0000153607"
FT DOMAIN 7..101
FT /note="Ig-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 28..87
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 105
FT /note="Interchain (with heavy chain)"
FT NON_TER 1
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:2FB4"
FT HELIX 16..20
FT /evidence="ECO:0007829|PDB:2FB4"
FT STRAND 24..36
FT /evidence="ECO:0007829|PDB:2FB4"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:2FB4"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:2IG2"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:2FB4"
FT STRAND 64..74
FT /evidence="ECO:0007829|PDB:2FB4"
FT HELIX 76..81
FT /evidence="ECO:0007829|PDB:2FB4"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:2FB4"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:2FB4"
FT TURN 102..105
FT /evidence="ECO:0007829|PDB:2IG2"
SQ SEQUENCE 106 AA; 11348 MW; 4BA84D404ECA997E CRC64;
GQPKANPTVT LFPPSSEELQ ANKATLVCLI SDFYPGAVTV AWKADGSPVK AGVETTKPSK
QSNNKYAASS YLSLTPEQWK SHRSYSCQVT HEGSTVEKTV APTECS
