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Immunoglobulin lambda constant 2 (Ig lambda chain C region Kern) (Ig lambda chain C region NIG-64) (Ig lambda chain C region SH) (Ig lambda chain C region X) (Ig lambda-2 chain C region)

 IGLC2_HUMAN             Reviewed;         106 AA.
P0DOY2; A0A075B6K9; A0M8Q4; P0CG05; P0CG06; P80423;
15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
15-MAR-2017, sequence version 1.
25-OCT-2017, entry version 8.
RecName: Full=Immunoglobulin lambda constant 2 {ECO:0000303|PubMed:11872955, ECO:0000303|Ref.11};
AltName: Full=Ig lambda chain C region Kern {ECO:0000305|PubMed:5549568};
AltName: Full=Ig lambda chain C region NIG-64 {ECO:0000305|PubMed:6404900};
AltName: Full=Ig lambda chain C region SH {ECO:0000305|PubMed:4909564};
AltName: Full=Ig lambda chain C region X {ECO:0000305|PubMed:4883841};
AltName: Full=Ig lambda-2 chain C region {ECO:0000305};
Name=IGLC2 {ECO:0000303|PubMed:11872955, ECO:0000303|Ref.11};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
PROTEIN SEQUENCE, AND DISULFIDE BONDS.
PubMed=4883841; DOI=10.1042/bj1100631;
Milstein C., Clegg J.B., Jarvis J.M.;
"Immunoglobulin lambda-chains. The complete amino acid sequence of a
Bence-Jones protein.";
Biochem. J. 110:631-652(1968).
[2]
PROTEIN SEQUENCE.
PubMed=4909564;
Titani K., Wikler M., Shinoda T., Putnam F.W.;
"The amino acid sequence of a lambda type Bence-Jones protein. 3. The
complete amino acid sequence and the location of the disulfide
bridges.";
J. Biol. Chem. 245:2171-2176(1970).
[3]
PROTEIN SEQUENCE.
PubMed=5549568;
Ponstingl H., Hess M., Hilschmann N.;
"Structural rule of antibodies. Primary structure of a monoclonal
immunoglobulin-L-chain of the lambda type, subgroup IV (Bence-Jones-
protein Kern). V. The complete amino acid sequence and its genetic
interpretation.";
Hoppe-Seyler's Z. Physiol. Chem. 352:247-266(1971).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (IMGT ALLELE IGLC2*01).
PubMed=6273747; DOI=10.1038/294536a0;
Hieter P.A., Hollis G.F., Korsmeyer S.J., Waldmann T.A., Leder P.;
"Clustered arrangement of immunoglobulin lambda constant region genes
in man.";
Nature 294:536-540(1981).
[5]
PROTEIN SEQUENCE.
PubMed=6404900;
Kametani F., Takayasu T., Suzuki S., Shinoda T., Okuyama T.,
Shimizu A.;
"Comparative studies on the structure of the light chains of human
immunoglobulins. IV. Assignment of a subsubgroup.";
J. Biochem. 93:421-429(1983).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (IMGT ALLELE IGLC2*02).
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).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (IMGT ALLELE IGLC2*02).
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).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE IGLC2*02).
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).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE IGLC2*02).
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.
[10]
NOMEMCLATURE.
PubMed=11872955;
Lefranc M.P.;
"Nomenclature of the human immunoglobulin lambda (IGL) genes.";
Exp. Clin. Immunogenet. 18:242-254(2001).
[11]
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).
[12]
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).
[13]
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).
[14]
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).
[15]
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 IGLC2*02. {ECO:0000305}.
-!- MISCELLANEOUS: Displays the following serological isotype: Mcg-,
Kern- and Oz-. The Mcg- isotype marker is characterized by Ala-6,
Ser-8 and Thr-57; the Ke- marker by Ser-46 and the Oz- marker by
Arg-83. {ECO:0000303|Ref.12}.
-!- CAUTION: For an example of a full-length immunoglobulin lambda
light chain see AC P0DOX8. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA59107.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAA20026.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAA36049.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAB38569.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=EAW59547.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=EAW59549.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; J00253; AAA59107.1; ALT_INIT; Genomic_DNA.
EMBL; X51754; CAB38569.1; ALT_INIT; Genomic_DNA.
EMBL; X51755; CAA36049.1; ALT_INIT; Genomic_DNA.
EMBL; D87023; BAA20026.1; ALT_INIT; Genomic_DNA.
EMBL; AC245028; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471095; EAW59547.1; ALT_INIT; Genomic_DNA.
EMBL; CH471095; EAW59549.1; ALT_INIT; Genomic_DNA.
PIR; A92057; L2HU.
PDB; 1JVK; X-ray; 1.94 A; B=1-105.
PDB; 1LIL; X-ray; 2.65 A; A/B=1-106.
PDB; 1ZVO; X-ray; -; A/B=2-106.
PDB; 2JB5; X-ray; 2.80 A; L=1-104.
PDB; 2JB6; X-ray; 2.85 A; A/L=1-104.
PDB; 3C2A; X-ray; 2.10 A; L/M=2-105.
PDB; 3TV3; X-ray; 1.29 A; L=1-106.
PDB; 3TWC; X-ray; 1.65 A; L=1-106.
PDB; 3TYG; X-ray; 3.25 A; L=1-106.
PDB; 4EOW; X-ray; 1.97 A; L=1-106.
PDB; 4LLD; X-ray; 1.19 A; B=1-105.
PDB; 4LLM; X-ray; 1.75 A; B=1-105.
PDB; 4LLQ; X-ray; 1.42 A; B=1-105.
PDB; 4LLU; X-ray; 2.16 A; B/D=1-105.
PDB; 4LLW; X-ray; 1.95 A; B/D=1-105.
PDB; 4LLY; X-ray; 1.60 A; B/D=1-105.
PDB; 4O58; X-ray; 2.75 A; L=1-106.
PDB; 4O5I; X-ray; 6.50 A; N/P/R/T/V/X=1-106.
PDB; 5IQ7; X-ray; 3.29 A; L=1-104.
PDB; 5IQ9; X-ray; 2.40 A; B/L=1-102.
PDBsum; 1JVK; -.
PDBsum; 1LIL; -.
PDBsum; 1ZVO; -.
PDBsum; 2JB5; -.
PDBsum; 2JB6; -.
PDBsum; 3C2A; -.
PDBsum; 3TV3; -.
PDBsum; 3TWC; -.
PDBsum; 3TYG; -.
PDBsum; 4EOW; -.
PDBsum; 4LLD; -.
PDBsum; 4LLM; -.
PDBsum; 4LLQ; -.
PDBsum; 4LLU; -.
PDBsum; 4LLW; -.
PDBsum; 4LLY; -.
PDBsum; 4O58; -.
PDBsum; 4O5I; -.
PDBsum; 5IQ7; -.
PDBsum; 5IQ9; -.
SMR; P0DOY2; -.
IMGT_GENE-DB; IGLC2; -.
DMDM; 298351714; -.
MaxQB; P0DOY2; -.
PRIDE; P0CG05; -.
Ensembl; ENST00000390323; ENSP00000374856; ENSG00000211677.
EuPathDB; HostDB:ENSG00000211677.2; -.
GeneCards; IGLC2; -.
H-InvDB; HIX0016285; -.
H-InvDB; HIX0197173; -.
HGNC; HGNC:5856; IGLC2.
neXtProt; NX_P0DOY2; -.
eggNOG; ENOG410J0XA; Eukaryota.
eggNOG; ENOG410YZ00; LUCA.
InParanoid; P0CG05; -.
PhylomeDB; P0CG05; -.
PRO; PR:P0DOY2; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000211677; -.
GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0003823; F:antigen binding; IEA:UniProtKB-KW.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
Gene3D; 2.60.40.10; -; 1.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
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;
3D-structure; Adaptive immunity; Bence-Jones protein; Cell membrane;
Complete proteome; Direct protein sequencing; Disulfide bond;
Immunity; Immunoglobulin C region; Immunoglobulin domain; Membrane;
Polymorphism; Reference proteome; Secreted.
CHAIN <1 106 Immunoglobulin lambda constant 2.
/FTId=PRO_0000394665.
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).
{ECO:0000269|PubMed:4883841}.
NON_TER 1 1
STRAND 8 12 {ECO:0000244|PDB:4LLD}.
HELIX 16 20 {ECO:0000244|PDB:4LLD}.
STRAND 24 36 {ECO:0000244|PDB:4LLD}.
STRAND 39 44 {ECO:0000244|PDB:4LLD}.
STRAND 47 49 {ECO:0000244|PDB:4LLD}.
STRAND 53 55 {ECO:0000244|PDB:4LLD}.
STRAND 62 64 {ECO:0000244|PDB:4LLY}.
STRAND 66 74 {ECO:0000244|PDB:4LLD}.
HELIX 76 81 {ECO:0000244|PDB:4LLD}.
STRAND 85 91 {ECO:0000244|PDB:4LLD}.
STRAND 94 100 {ECO:0000244|PDB:4LLD}.
HELIX 102 104 {ECO:0000244|PDB:3C2A}.
SEQUENCE 106 AA; 11294 MW; E5DB72BBE65F4577 CRC64;
GQPKAAPSVT LFPPSSEELQ ANKATLVCLI SDFYPGAVTV AWKADSSPVK AGVETTTPSK
QSNNKYAASS YLSLTPEQWK SHRSYSCQVT HEGSTVEKTV APTECS


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