IGLC7_HUMAN
ID IGLC7_HUMAN Reviewed; 106 AA.
AC A0M8Q6; A0A075B6L1;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 3.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Immunoglobulin lambda constant 7 {ECO:0000303|PubMed:11872955, ECO:0000303|Ref.6};
DE AltName: Full=Ig lambda-7 chain C region;
GN Name=IGLC7 {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 [GENOMIC DNA] (IMGT ALLELE IGLC7*01).
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (IMGT ALLELE IGLC7*01).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE IGLC7*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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE IGLC7*01).
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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).
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 IGLC7*03. {ECO:0000305}.
CC -!- MISCELLANEOUS: Displays the following serological isotype: Ke+, Oz- and
CC two of the three characteristic amino acids of Mgc-isotype: Ala-6 and
CC Ser-8 but instead of Thr-57 it displays Lys-57. Ke+ has Gly-46 and
CC Oz- has Arg-83. {ECO:0000303|Ref.7}.
CC -!- CAUTION: For an example of a full-length immunoglobulin lambda light
CC chain see AC P0DOX8. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA20016.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA36053.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=EAW59556.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X51755; CAA36053.1; ALT_INIT; Genomic_DNA.
DR EMBL; D87017; BAA20016.1; ALT_INIT; Genomic_DNA.
DR EMBL; AC245028; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471095; EAW59556.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; A0M8Q6; -.
DR SMR; A0M8Q6; -.
DR ComplexPortal; CPX-6910; IgD - Ig lambda 7 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6927; IgM - Ig lambda 7 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6935; IgG1 - Ig lambda 7 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6942; IgG2 - Ig lambda 7 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6948; IgG3 - Ig lambda 7 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6954; IgG4 - Ig lambda 7 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6961; IgA1 - Ig lambda 7 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6967; IgA2 - Ig lambda 7 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6974; IgE - Ig lambda 7 immunoglobulin complex, constant regions.
DR IntAct; A0M8Q6; 3.
DR IMGT_GENE-DB; IGLC7; -.
DR BioMuta; IGLC7; -.
DR EPD; A0M8Q6; -.
DR jPOST; A0M8Q6; -.
DR MassIVE; A0M8Q6; -.
DR PeptideAtlas; A0M8Q6; -.
DR PRIDE; A0M8Q6; -.
DR ProteomicsDB; 44; -.
DR UCSC; uc062ceh.1; human.
DR GeneCards; IGLC7; -.
DR HGNC; HGNC:5861; IGLC7.
DR neXtProt; NX_A0M8Q6; -.
DR InParanoid; A0M8Q6; -.
DR PhylomeDB; A0M8Q6; -.
DR PathwayCommons; A0M8Q6; -.
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; A0M8Q6; -.
DR ChiTaRS; IGLC7; human.
DR Pharos; A0M8Q6; Tdark.
DR PRO; PR:A0M8Q6; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; A0M8Q6; protein.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IC:ComplexPortal.
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: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 Adaptive immunity; Cell membrane; Disulfide bond; Immunity; Immunoglobulin;
KW Immunoglobulin domain; Membrane; Reference proteome; Secreted.
FT CHAIN <1..106
FT /note="Immunoglobulin lambda constant 7"
FT /id="PRO_0000393470"
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 34
FT /note="N -> Y (in IMGT ALLELE IGLC7*01)"
FT /id="VAR_077896"
FT NON_TER 1
SQ SEQUENCE 106 AA; 11254 MW; 372937A232ABE662 CRC64;
GQPKAAPSVT LFPPSSEELQ ANKATLVCLV SDFNPGAVTV AWKADGSPVK VGVETTKPSK
QSNNKYAASS YLSLTPEQWK SHRSYSCRVT HEGSTVEKTV APAECS
