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Immunoglobulin lambda constant 7 (Ig lambda-7 chain C region)

 IGLC7_HUMAN             Reviewed;         106 AA.
A0M8Q6; A0A075B6L1;
20-APR-2010, integrated into UniProtKB/Swiss-Prot.
15-MAR-2017, sequence version 3.
27-SEP-2017, entry version 86.
RecName: Full=Immunoglobulin lambda constant 7 {ECO:0000303|PubMed:11872955, ECO:0000303|Ref.6};
AltName: Full=Ig lambda-7 chain C region;
Name=IGLC7 {ECO:0000303|PubMed:11872955, ECO:0000303|Ref.6};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (IMGT ALLELE IGLC7*01).
PubMed=2115572; DOI=10.1084/jem.172.2.609;
Vasicek T.J., Leder P.;
"Structure and expression of the human immunoglobulin lambda genes.";
J. Exp. Med. 172:609-620(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (IMGT ALLELE IGLC7*01).
PubMed=9074928; DOI=10.1101/gr.7.3.250;
Kawasaki K., Minoshima S., Nakato E., Shibuya K., Shintani A.,
Schmeits J.L., Wang J., Shimizu N.;
"One-megabase sequence analysis of the human immunoglobulin lambda
gene locus.";
Genome Res. 7:250-261(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE IGLC7*03).
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
Khan A.S., Lane L., Tilahun Y., Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE IGLC7*01).
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NOMEMCLATURE.
PubMed=11872955;
Lefranc M.P.;
"Nomenclature of the human immunoglobulin lambda (IGL) genes.";
Exp. Clin. Immunogenet. 18:242-254(2001).
[6]
NOMENCLATURE.
Lefranc M.P., Lefranc G.;
"The Immunoglobulin FactsBook.";
(In) Lefranc M.P., Lefranc G. (eds.);
The Immunoglobulin FactsBook., pp.1-458, Academic Press, London.
(2001).
[7]
SEROLOGICAL ISOTYPE.
Lefranc M.-P., Lefranc G.;
"Immunoglobulin lambda (IGL) genes of human and mouse.";
(In) Honjo T., Alt F.W., Neuberger M. (eds.);
Molecular Biology of B Cells, pp.37-59, Elsevier Academic Press,
London (2004).
[8]
REVIEW ON SOMATIC HYPERMUTATION.
PubMed=17576170; DOI=10.1146/annurev.genet.41.110306.130340;
Teng G., Papavasiliou F.N.;
"Immunoglobulin somatic hypermutation.";
Annu. Rev. Genet. 41:107-120(2007).
[9]
REVIEW ON IMMUNOGLOBULINS.
PubMed=20176268; DOI=10.1016/j.jaci.2009.09.046;
Schroeder H.W. Jr., Cavacini L.;
"Structure and function of immunoglobulins.";
J. Allergy Clin. Immunol. 125:S41-S52(2010).
[10]
REVIEW ON FUNCTION.
PubMed=22158414; DOI=10.1038/nri3128;
McHeyzer-Williams M., Okitsu S., Wang N., McHeyzer-Williams L.;
"Molecular programming of B cell memory.";
Nat. Rev. Immunol. 12:24-34(2012).
-!- FUNCTION: Constant region of immunoglobulin heavy chains.
Immunoglobulins, also known as antibodies, are membrane-bound or
secreted glycoproteins produced by B lymphocytes. In the
recognition phase of humoral immunity, the membrane-bound
immunoglobulins serve as receptors which, upon binding of a
specific antigen, trigger the clonal expansion and differentiation
of B lymphocytes into immunoglobulins-secreting plasma cells.
Secreted immunoglobulins mediate the effector phase of humoral
immunity, which results in the elimination of bound antigens
(PubMed:22158414, PubMed:20176268). The antigen binding site is
formed by the variable domain of one heavy chain, together with
that of its associated light chain. Thus, each immunoglobulin has
two antigen binding sites with remarkable affinity for a
particular antigen. The variable domains are assembled by a
process called V-(D)-J rearrangement and can then be subjected to
somatic hypermutations which, after exposure to antigen and
selection, allow affinity maturation for a particular antigen
(PubMed:17576170, PubMed:20176268). {ECO:0000303|PubMed:17576170,
ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
-!- SUBUNIT: Immunoglobulins are composed of two identical heavy
chains and two identical light chains; disulfide-linked.
{ECO:0000303|PubMed:20176268}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268,
ECO:0000303|PubMed:22158414}. Cell membrane
{ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
-!- POLYMORPHISM: There are several alleles. The sequence shown is
that of IMGT allele IGLC7*03. {ECO:0000305}.
-!- MISCELLANEOUS: Displays the following serological isotype: Ke+,
Oz- and two of the three characteristic amino acids of Mgc-
isotype: Ala-6 and Ser-8 but instead of Thr-57 it displays Lys-57.
Ke+ has Gly-46 and Oz- has Arg-83. {ECO:0000303|Ref.7}.
-!- CAUTION: For an example of a full-length immunoglobulin lambda
light chain see AC P0DOX8. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA20016.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAA36053.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=EAW59556.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; X51755; CAA36053.1; ALT_INIT; Genomic_DNA.
EMBL; D87017; BAA20016.1; ALT_INIT; Genomic_DNA.
EMBL; AC245028; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471095; EAW59556.1; ALT_INIT; Genomic_DNA.
ProteinModelPortal; A0M8Q6; -.
SMR; A0M8Q6; -.
IMGT_GENE-DB; IGLC7; -.
PRIDE; A0M8Q6; -.
EuPathDB; HostDB:ENSG00000211685.3; -.
GeneCards; IGLC7; -.
HGNC; HGNC:5861; IGLC7.
neXtProt; NX_A0M8Q6; -.
HOVERGEN; HBG017899; -.
InParanoid; A0M8Q6; -.
PhylomeDB; A0M8Q6; -.
Reactome; R-HSA-166663; Initial triggering of complement.
Reactome; R-HSA-173623; Classical antibody-mediated complement activation.
Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
Reactome; R-HSA-2029481; FCGR activation.
Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-HSA-2029485; Role of phospholipids in phagocytosis.
Reactome; R-HSA-2168880; Scavenging of heme from plasma.
Reactome; R-HSA-2454202; Fc epsilon receptor (FCERI) signaling.
Reactome; R-HSA-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
Reactome; R-HSA-2871796; FCERI mediated MAPK activation.
Reactome; R-HSA-2871809; FCERI mediated Ca+2 mobilization.
Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
Reactome; R-HSA-5690714; CD22 mediated BCR regulation.
Reactome; R-HSA-977606; Regulation of Complement cascade.
Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
PRO; PR:A0M8Q6; -.
Proteomes; UP000005640; Unplaced.
Bgee; ENSG00000211685; -.
GO; GO:0072562; C:blood microparticle; IBA:GO_Central.
GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0042571; C:immunoglobulin complex, circulating; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0003823; F:antigen binding; IBA:GO_Central.
GO; GO:0034987; F:immunoglobulin receptor binding; IBA:GO_Central.
GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
GO; GO:0050853; P:B cell receptor signaling pathway; IBA:GO_Central.
GO; GO:0006956; P:complement activation; TAS:Reactome.
GO; GO:0006958; P:complement activation, classical pathway; IBA:GO_Central.
GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0006911; P:phagocytosis, engulfment; IBA:GO_Central.
GO; GO:0006910; P:phagocytosis, recognition; IBA:GO_Central.
GO; GO:0050871; P:positive regulation of B cell activation; IBA:GO_Central.
GO; GO:0006898; P:receptor-mediated endocytosis; TAS:Reactome.
GO; GO:0030449; P:regulation of complement activation; TAS:Reactome.
GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
Gene3D; 2.60.40.10; -; 1.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003006; Ig/MHC_CS.
InterPro; IPR003597; Ig_C1-set.
Pfam; PF07654; C1-set; 1.
SMART; SM00407; IGc1; 1.
SUPFAM; SSF48726; SSF48726; 1.
PROSITE; PS50835; IG_LIKE; 1.
PROSITE; PS00290; IG_MHC; 1.
1: Evidence at protein level;
Adaptive immunity; Cell membrane; Complete proteome; Disulfide bond;
Immunity; Immunoglobulin C region; Immunoglobulin domain; Membrane;
Polymorphism; Reference proteome; Secreted.
CHAIN <1 106 Immunoglobulin lambda constant 7.
/FTId=PRO_0000393470.
DOMAIN 7 101 Ig-like. {ECO:0000255|PROSITE-
ProRule:PRU00114}.
DISULFID 28 87 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 105 105 Interchain (with heavy chain).
VARIANT 34 34 N -> Y (in IMGT ALLELE IGLC7*01).
/FTId=VAR_077896.
NON_TER 1 1
SEQUENCE 106 AA; 11254 MW; 372937A232ABE662 CRC64;
GQPKAAPSVT LFPPSSEELQ ANKATLVCLV SDFNPGAVTV AWKADGSPVK VGVETTKPSK
QSNNKYAASS YLSLTPEQWK SHRSYSCRVT HEGSTVEKTV APAECS


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