IGLC3_HUMAN
ID IGLC3_HUMAN Reviewed; 106 AA.
AC P0DOY3; A0A075B6L0; A0M8Q4; P0CG05; P0CG06; P80423;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 1.
DT 03-AUG-2022, entry version 28.
DE RecName: Full=Immunoglobulin lambda constant 3 {ECO:0000303|PubMed:11872955, ECO:0000303|Ref.9};
DE AltName: Full=Ig lambda chain C region DOT {ECO:0000305|PubMed:7737190};
DE AltName: Full=Ig lambda chain C region NEWM {ECO:0000305|PubMed:4814727};
DE AltName: Full=Ig lambda-3 chain C regions {ECO:0000305};
GN Name=IGLC3 {ECO:0000303|PubMed:11872955, ECO:0000303|Ref.9};
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 [GENOMIC DNA] (IMGT ALLELE IGLC3*01).
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (IMGT ALLELE IGLC3*03).
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 PROTEIN SEQUENCE.
RX PubMed=7737190; DOI=10.1111/j.1432-1033.1995.tb20336.x;
RA Stoppini M., Bellotti V., Negri A., Merlini G., Garver F., Ferri G.;
RT "Characterization of the two unique human anti-flavin monoclonal
RT immunoglobulins.";
RL Eur. J. Biochem. 228:886-893(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8676895; DOI=10.1016/0161-5890(95)00153-0;
RA Pilkington G.R., Duan L., Zhu M., Keil W., Pomerantz R.J.;
RT "Recombinant human Fab antibody fragments to HIV-1 Rev and Tat regulatory
RT proteins: direct selection from a combinatorial phage display library.";
RL Mol. Immunol. 33:439-450(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (IMGT ALLELE IGLC3*04), AND VARIANT
RP ARG-83.
RX PubMed=9074928; DOI=10.1101/gr.7.3.250;
RA Kawasaki K., Minoshima S., Nakato E., Shibuya K., Shintani A.,
RA Schmeits J.L., Wang J., Shimizu N.;
RT "One-megabase sequence analysis of the human immunoglobulin lambda gene
RT locus.";
RL Genome Res. 7:250-261(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE IGLC3*03).
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 [7]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=4814727; DOI=10.1021/bi00703a037;
RA Chen B.L., Poljak R.J.;
RT "Amino acid sequence of the (lambda) light chain of a human myeloma
RT immunoglobulin (IgG New).";
RL Biochemistry 13:1295-1302(1974).
RN [8]
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 [9]
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 [10]
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 [11]
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 [12]
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 [13]
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 [14]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=4215080; DOI=10.1073/pnas.71.9.3440;
RA Poljak R.J., Amzel L.M., Avey H.P., Chen B.L., Phizackerley R.P., Saul F.;
RT "The three-dimensional structure of the fab' fragment of a human myeloma
RT immunoglobulin at 2.0-A resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 71:3440-3444(1974).
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 IGLC3*03. {ECO:0000305}.
CC -!- MISCELLANEOUS: Alleles IGLC3*01, IGLC3*02, and IGLC3*03 display the
CC following serological isotype: Mcg-, Kern- and Oz+. The Mcg-isotype
CC marker is characterized by Ala-6, Ser-8 and Thr-57; the Ke- marker by
CC Ser-46 and the Oz+ marker by Lys-83. Allele IGLC3*04 displays the
CC following serological isotype: Mcg-, Kern- and Oz-. The Mcg- isotype
CC marker is characterized by Ala-6, Ser-8 and Thr-57; the Ke- marker by
CC Ser-46 and the Oz- marker by Arg-83. {ECO:0000303|Ref.10}.
CC -!- CAUTION: For an example of a full-length immunoglobulin lambda light
CC chain see AC P0DOX8. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA59109.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAB36581.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA20015.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA20028.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA36051.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; J00254; AAA59109.1; ALT_INIT; Genomic_DNA.
DR EMBL; X51755; CAA36051.1; ALT_INIT; Genomic_DNA.
DR EMBL; L38562; AAB36581.1; ALT_INIT; mRNA.
DR EMBL; D87017; BAA20015.1; ALT_INIT; Genomic_DNA.
DR EMBL; D87023; BAA20028.1; ALT_INIT; Genomic_DNA.
DR EMBL; AC245028; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A92057; L2HU.
DR PDB; 1AQK; X-ray; 1.84 A; L=1-106.
DR PDB; 4O5L; X-ray; 1.50 A; L=1-106.
DR PDB; 4R26; X-ray; 2.50 A; L=2-106.
DR PDB; 4R2G; X-ray; 3.28 A; C/I/M/P=1-106.
DR PDB; 7FAB; X-ray; 2.00 A; L=2-106.
DR PDBsum; 1AQK; -.
DR PDBsum; 4O5L; -.
DR PDBsum; 4R26; -.
DR PDBsum; 4R2G; -.
DR PDBsum; 7FAB; -.
DR AlphaFoldDB; P0DOY3; -.
DR SMR; P0DOY3; -.
DR ComplexPortal; CPX-6908; IgD - Ig lambda 3 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6925; IgM - Ig lambda 3 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6933; IgG1 - Ig lambda 3 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6940; IgG2 - Ig lambda 3 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6946; IgG3 - Ig lambda 3 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6952; IgG4 - Ig lambda 3 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6959; IgA1 - Ig lambda 3 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6965; IgA2 - Ig lambda 3 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6972; IgE - Ig lambda 3 immunoglobulin complex, constant regions.
DR IntAct; P0DOY3; 2.
DR IMGT_GENE-DB; IGLC3; -.
DR BioMuta; IGLC3; -.
DR jPOST; P0DOY3; -.
DR MassIVE; P0DOY3; -.
DR PeptideAtlas; P0DOY3; -.
DR PRIDE; P0DOY3; -.
DR Ensembl; ENST00000390325.2; ENSP00000374857.2; ENSG00000211679.2.
DR GeneCards; IGLC3; -.
DR HGNC; HGNC:5857; IGLC3.
DR HPA; ENSG00000211679; Tissue enhanced (intestine, lymphoid tissue, stomach, urinary bladder).
DR neXtProt; NX_P0DOY3; -.
DR VEuPathDB; HostDB:ENSG00000211679; -.
DR PathwayCommons; P0DOY3; -.
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; P0DOY3; -.
DR ChiTaRS; IGLC3; human.
DR Pharos; P0DOY3; Tdark.
DR PRO; PR:P0DOY3; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P0DOY3; protein.
DR Bgee; ENSG00000211679; Expressed in duodenum and 93 other tissues.
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; IPI: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: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 3"
FT /id="PRO_0000394666"
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 VARIANT 83
FT /note="K -> R (in IMGT allele IGLC3*04)"
FT /id="VAR_077897"
FT NON_TER 1
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:4O5L"
FT HELIX 16..20
FT /evidence="ECO:0007829|PDB:4O5L"
FT STRAND 24..36
FT /evidence="ECO:0007829|PDB:4O5L"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:4O5L"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:4O5L"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:4O5L"
FT STRAND 64..74
FT /evidence="ECO:0007829|PDB:4O5L"
FT HELIX 76..81
FT /evidence="ECO:0007829|PDB:4O5L"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:4O5L"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:4O5L"
SQ SEQUENCE 106 AA; 11266 MW; 145272BBE65F4565 CRC64;
GQPKAAPSVT LFPPSSEELQ ANKATLVCLI SDFYPGAVTV AWKADSSPVK AGVETTTPSK
QSNNKYAASS YLSLTPEQWK SHKSYSCQVT HEGSTVEKTV APTECS
