IGKC_HUMAN
ID IGKC_HUMAN Reviewed; 107 AA.
AC P01834; A0A075B6H6; A0A087X130;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Immunoglobulin kappa constant {ECO:0000303|PubMed:11549845, ECO:0000303|Ref.13};
DE AltName: Full=Ig kappa chain C region {ECO:0000305};
DE AltName: Full=Ig kappa chain C region AG {ECO:0000305|PubMed:4893682};
DE AltName: Full=Ig kappa chain C region CUM {ECO:0000305|PubMed:5586923};
DE AltName: Full=Ig kappa chain C region EU {ECO:0000305|PubMed:5489770};
DE AltName: Full=Ig kappa chain C region OU {ECO:0000305|PubMed:5447531};
DE AltName: Full=Ig kappa chain C region ROY {ECO:0000305|Ref.3};
DE AltName: Full=Ig kappa chain C region TI {ECO:0000305|PubMed:5027703};
GN Name=IGKC {ECO:0000303|PubMed:11549845, ECO:0000303|Ref.13};
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=5586923;
RA Hilschmann N.;
RT "The complete amino acid sequence of Bence Jones protein Cum (kappa-
RT type).";
RL Hoppe-Seyler's Z. Physiol. Chem. 348:1718-1722(1967).
RN [2]
RP PROTEIN SEQUENCE.
RX PubMed=4893682; DOI=10.1016/s0021-9258(18)83405-6;
RA Titani K., Shinoda T., Putnam F.W.;
RT "The amino acid sequence of a kappa type Bence-Jones protein. 3. The
RT complete sequence and the location of the disulfide bridges.";
RL J. Biol. Chem. 244:3550-3560(1969).
RN [3]
RP PROTEIN SEQUENCE, AND VARIANT LEU-84.
RA Hilschmann N., Barnikol H.U., Hess M., Langer B., Ponstingl H.,
RA Steinmetz-Kayne M., Suter L., Watanabe S.;
RL (In) Franek F., Shugar D. (eds.);
RL Gamma globulins: structure and function, pp.57-74, Academic Press, New York
RL (1969).
RN [4]
RP PROTEIN SEQUENCE.
RX PubMed=5489770; DOI=10.1021/bi00818a007;
RA Gottlieb P.D., Cunningham B.A., Rutishauser U., Edelman G.M.;
RT "The covalent structure of a human gamma G-immunoglobulin. VI. Amino acid
RT sequence of the light chain.";
RL Biochemistry 9:3155-3161(1970).
RN [5]
RP PROTEIN SEQUENCE.
RX PubMed=5447531; DOI=10.1126/science.169.3940.56;
RA Kohler H., Shimizu A., Paul C., Putnam F.W.;
RT "Macroglobulin structure: variable sequence of light and heavy chains.";
RL Science 169:56-59(1970).
RN [6]
RP PROTEIN SEQUENCE.
RX PubMed=5027703;
RA Suter L., Barnikol H.U., Watanabe S., Hilschmann N.;
RT "Rule of antibody structure. The primary structure of a monoclonal
RT immunoglobulin L-chain of kappa-type, subgroup 3 (Bence-Jones protein Ti).
RT IV. The complete amino acid sequence and its significance for the mechanism
RT of antibody production.";
RL Hoppe-Seyler's Z. Physiol. Chem. 353:189-208(1972).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (IMGT ALLELE IGKC*01).
RX PubMed=6775818; DOI=10.1016/0092-8674(80)90168-3;
RA Hieter P.A., Max E.E., Seidman J.G., Maizel J.V. Jr., Leder P.;
RT "Cloned human and mouse kappa immunoglobulin constant and J region genes
RT conserve homology in functional segments.";
RL Cell 22:197-207(1980).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE IGKC*01).
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [9]
RP PROTEIN SEQUENCE OF 2-34; 38-41 AND 62-80.
RC TISSUE=Abdominal adipose tissue;
RX PubMed=9588180; DOI=10.1006/bbrc.1998.8515;
RA Olsen K.E., Sletten K., Westermark P.;
RT "Extended analysis of AL-amyloid protein from abdominal wall subcutaneous
RT fat biopsy: kappa IV immunoglobulin light chain.";
RL Biochem. Biophys. Res. Commun. 245:713-716(1998).
RN [10]
RP PROTEIN SEQUENCE OF 67-107, AND 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 [11]
RP DISULFIDE BONDS.
RX PubMed=4923144; DOI=10.1021/bi00818a011;
RA Gall W.E., Edelman G.M.;
RT "The covalent structure of a human gamma G-immunoglobulin. X. Intrachain
RT disulfide bonds.";
RL Biochemistry 9:3188-3196(1970).
RN [12]
RP NOMEMCLATURE.
RX PubMed=11549845; DOI=10.1159/000049195;
RA Lefranc M.P.;
RT "Nomenclature of the human immunoglobulin kappa (IGK) genes.";
RL Exp. Clin. Immunogenet. 18:161-174(2001).
RN [13]
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 [14]
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 [15]
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 [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [17]
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 [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [19]
RP VARIANT IGKCD ARG-41.
RX PubMed=3931219; DOI=10.1126/science.3931219;
RA Stavnezer-Nordgren J., Kekish O., Zegers B.J.;
RT "Molecular defects in a human immunoglobulin kappa chain deficiency.";
RL Science 230:458-461(1985).
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 IGKC*01. {ECO:0000305}.
CC -!- DISEASE: Immunoglobulin kappa light chain deficiency (IGKCD)
CC [MIM:614102]: A disease characterized by the complete absence of
CC immunoglobulin kappa chains. {ECO:0000269|PubMed:3931219}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- CAUTION: For an example of a full-length immunoglobulin kappa light
CC chain see AC P0DOX7. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA58989.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; J00241; AAA58989.1; ALT_INIT; Genomic_DNA.
DR EMBL; AC244205; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; B90562; K3HU.
DR PDB; 1A4J; X-ray; 2.10 A; A/L=2-105.
DR PDB; 1A4K; X-ray; 2.40 A; A/L=2-105.
DR PDB; 1CLY; X-ray; 2.50 A; L=2-107.
DR PDB; 1D5B; X-ray; 2.80 A; A/L=2-104.
DR PDB; 1D5I; X-ray; 2.00 A; L=2-104.
DR PDB; 1D6V; X-ray; 2.00 A; L=2-104.
DR PDB; 1DFB; X-ray; 2.70 A; L=2-107.
DR PDB; 1GAF; X-ray; 1.95 A; L=2-107.
DR PDB; 1HEZ; X-ray; 2.70 A; A/C=2-107.
DR PDB; 1HKL; X-ray; 2.68 A; L=2-107.
DR PDB; 1HZH; X-ray; 2.70 A; L/M=2-107.
DR PDB; 1I7Z; X-ray; 2.30 A; A/C=2-107.
DR PDB; 1MIM; X-ray; 2.60 A; L=2-106.
DR PDB; 1N0X; X-ray; 1.80 A; L/M=2-107.
DR PDB; 1UCB; X-ray; 2.50 A; L=2-107.
DR PDB; 2NY7; X-ray; 2.30 A; L=2-107.
DR PDB; 2O5X; X-ray; 2.05 A; L=2-107.
DR PDB; 2O5Y; X-ray; 2.85 A; L=2-107.
DR PDB; 2O5Z; X-ray; 2.40 A; L=2-107.
DR PDB; 2QQK; X-ray; 2.75 A; L=2-107.
DR PDB; 2QQL; X-ray; 3.10 A; L=2-107.
DR PDB; 2QQN; X-ray; 2.20 A; L=2-107.
DR PDB; 2QSC; X-ray; 2.80 A; L=2-107.
DR PDB; 2R56; X-ray; 2.80 A; L/M=2-104.
DR PDB; 2RFX; X-ray; 2.50 A; C=94-102.
DR PDB; 2VXQ; X-ray; 1.90 A; L=2-107.
DR PDB; 3B2U; X-ray; 2.58 A; D/G/K/L/O/R/U/X=2-105.
DR PDB; 3B2V; X-ray; 3.30 A; L=2-105.
DR PDB; 3BDY; X-ray; 2.60 A; L=2-107.
DR PDB; 3BE1; X-ray; 2.90 A; L=2-107.
DR PDB; 3BKY; X-ray; 2.61 A; L=2-107.
DR PDB; 3BN9; X-ray; 2.17 A; C/E=2-107.
DR PDB; 3BQU; X-ray; 3.00 A; A=2-107.
DR PDB; 3C08; X-ray; 2.15 A; L=2-106.
DR PDB; 3C09; X-ray; 3.20 A; B/L=2-106.
DR PDB; 3CFJ; X-ray; 2.60 A; A/C/E/L=2-107.
DR PDB; 3CFK; X-ray; 2.60 A; A/C/E/G/J/L/M/O=2-107.
DR PDB; 3CSY; X-ray; 3.40 A; B/D/F/H=2-104.
DR PDB; 3D0L; X-ray; 2.35 A; A=2-106.
DR PDB; 3D85; X-ray; 1.90 A; A=2-107.
DR PDB; 3DVG; X-ray; 2.60 A; A=2-107.
DR PDB; 3DVN; X-ray; 2.70 A; A/L=2-107.
DR PDB; 3EYF; X-ray; 2.30 A; A/C=2-107.
DR PDB; 3EYO; X-ray; 2.50 A; A/C=2-107.
DR PDB; 3EYQ; X-ray; 2.40 A; C=2-107.
DR PDB; 3IU3; X-ray; 2.90 A; B/D/L=2-106.
DR PDB; 3O11; X-ray; 2.80 A; A/L=2-107.
DR PDB; 3QCT; X-ray; 2.15 A; L=3-106.
DR PDB; 3QCU; X-ray; 1.98 A; L/M=3-106.
DR PDB; 3QCV; X-ray; 2.51 A; L/M=3-106.
DR PDB; 3RU8; X-ray; 2.07 A; L=2-107.
DR PDB; 3U0W; X-ray; 2.00 A; L=2-107.
DR PDB; 3U7W; X-ray; 2.60 A; L=2-107.
DR PDB; 3U7Y; X-ray; 2.45 A; L=2-107.
DR PDB; 3VH8; X-ray; 1.80 A; C/F=94-102.
DR PDB; 3WUW; X-ray; 2.00 A; C=94-102.
DR PDB; 3X11; X-ray; 2.15 A; C=94-102.
DR PDB; 3X12; X-ray; 1.80 A; C=94-102.
DR PDB; 4D3C; X-ray; 2.62 A; L=2-107.
DR PDB; 4D9R; X-ray; 2.42 A; D/L=3-107.
DR PDB; 4HIX; X-ray; 2.20 A; L=2-107.
DR PDB; 4NM4; X-ray; 2.65 A; L/M=2-107.
DR PDB; 4NM8; X-ray; 4.00 A; L/M/N=2-107.
DR PDB; 4XMP; X-ray; 1.78 A; L=2-107.
DR PDB; 4XNY; X-ray; 2.30 A; L=2-107.
DR PDB; 4XNZ; X-ray; 3.39 A; C/F/L=2-107.
DR PDB; 4XXD; X-ray; 2.41 A; A/D=2-107.
DR PDB; 4YDV; X-ray; 2.70 A; A/L=2-107.
DR PDB; 5B38; X-ray; 2.30 A; C=94-102.
DR PDB; 5B39; X-ray; 2.50 A; C=94-102.
DR PDB; 5C7K; X-ray; 4.60 A; F=1-107.
DR PDB; 5ESV; X-ray; 3.10 A; B/D/L=2-107.
DR PDB; 5ESZ; X-ray; 4.19 A; B/L=2-107.
DR PDB; 5EWI; X-ray; 1.60 A; L=1-107.
DR PDB; 5VEB; X-ray; 2.34 A; B/L=1-107.
DR PDB; 5VIY; EM; 6.20 A; G/I=1-107.
DR PDB; 6AU5; X-ray; 2.48 A; A/C=1-106.
DR PDB; 6AXP; X-ray; 2.48 A; A/C=1-106.
DR PDB; 6AYN; X-ray; 2.48 A; A/C=1-106.
DR PDB; 6AZK; X-ray; 2.48 A; A/C=1-106.
DR PDB; 6AZL; X-ray; 2.48 A; A/C=1-106.
DR PDB; 6B9Y; X-ray; 2.14 A; A=1-107.
DR PDB; 6B9Z; X-ray; 1.82 A; A=1-107.
DR PDB; 6BAE; X-ray; 2.14 A; A=1-107.
DR PDB; 6BAH; X-ray; 1.90 A; A=1-107.
DR PDB; 6DCV; X-ray; 1.90 A; A/L=1-107.
DR PDB; 6DCW; X-ray; 2.00 A; L=1-107.
DR PDB; 6N2X; X-ray; 3.00 A; K/L=2-106.
DR PDB; 6N32; X-ray; 2.20 A; L/M=2-106.
DR PDB; 6N35; X-ray; 1.75 A; K/L=2-106.
DR PDB; 6OGE; EM; 4.36 A; B/D=1-107.
DR PDB; 6OKP; EM; 3.28 A; N/P/R=1-107.
DR PDB; 7CZY; EM; 3.30 A; K/N=1-107.
DR PDB; 7CZZ; EM; 3.20 A; K/M/N=1-107.
DR PDBsum; 1A4J; -.
DR PDBsum; 1A4K; -.
DR PDBsum; 1CLY; -.
DR PDBsum; 1D5B; -.
DR PDBsum; 1D5I; -.
DR PDBsum; 1D6V; -.
DR PDBsum; 1DFB; -.
DR PDBsum; 1GAF; -.
DR PDBsum; 1HEZ; -.
DR PDBsum; 1HKL; -.
DR PDBsum; 1HZH; -.
DR PDBsum; 1I7Z; -.
DR PDBsum; 1MIM; -.
DR PDBsum; 1N0X; -.
DR PDBsum; 1UCB; -.
DR PDBsum; 2NY7; -.
DR PDBsum; 2O5X; -.
DR PDBsum; 2O5Y; -.
DR PDBsum; 2O5Z; -.
DR PDBsum; 2QQK; -.
DR PDBsum; 2QQL; -.
DR PDBsum; 2QQN; -.
DR PDBsum; 2QSC; -.
DR PDBsum; 2R56; -.
DR PDBsum; 2RFX; -.
DR PDBsum; 2VXQ; -.
DR PDBsum; 3B2U; -.
DR PDBsum; 3B2V; -.
DR PDBsum; 3BDY; -.
DR PDBsum; 3BE1; -.
DR PDBsum; 3BKY; -.
DR PDBsum; 3BN9; -.
DR PDBsum; 3BQU; -.
DR PDBsum; 3C08; -.
DR PDBsum; 3C09; -.
DR PDBsum; 3CFJ; -.
DR PDBsum; 3CFK; -.
DR PDBsum; 3CSY; -.
DR PDBsum; 3D0L; -.
DR PDBsum; 3D85; -.
DR PDBsum; 3DVG; -.
DR PDBsum; 3DVN; -.
DR PDBsum; 3EYF; -.
DR PDBsum; 3EYO; -.
DR PDBsum; 3EYQ; -.
DR PDBsum; 3IU3; -.
DR PDBsum; 3O11; -.
DR PDBsum; 3QCT; -.
DR PDBsum; 3QCU; -.
DR PDBsum; 3QCV; -.
DR PDBsum; 3RU8; -.
DR PDBsum; 3U0W; -.
DR PDBsum; 3U7W; -.
DR PDBsum; 3U7Y; -.
DR PDBsum; 3VH8; -.
DR PDBsum; 3WUW; -.
DR PDBsum; 3X11; -.
DR PDBsum; 3X12; -.
DR PDBsum; 4D3C; -.
DR PDBsum; 4D9R; -.
DR PDBsum; 4HIX; -.
DR PDBsum; 4NM4; -.
DR PDBsum; 4NM8; -.
DR PDBsum; 4XMP; -.
DR PDBsum; 4XNY; -.
DR PDBsum; 4XNZ; -.
DR PDBsum; 4XXD; -.
DR PDBsum; 4YDV; -.
DR PDBsum; 5B38; -.
DR PDBsum; 5B39; -.
DR PDBsum; 5C7K; -.
DR PDBsum; 5ESV; -.
DR PDBsum; 5ESZ; -.
DR PDBsum; 5EWI; -.
DR PDBsum; 5VEB; -.
DR PDBsum; 5VIY; -.
DR PDBsum; 6AU5; -.
DR PDBsum; 6AXP; -.
DR PDBsum; 6AYN; -.
DR PDBsum; 6AZK; -.
DR PDBsum; 6AZL; -.
DR PDBsum; 6B9Y; -.
DR PDBsum; 6B9Z; -.
DR PDBsum; 6BAE; -.
DR PDBsum; 6BAH; -.
DR PDBsum; 6DCV; -.
DR PDBsum; 6DCW; -.
DR PDBsum; 6N2X; -.
DR PDBsum; 6N32; -.
DR PDBsum; 6N35; -.
DR PDBsum; 6OGE; -.
DR PDBsum; 6OKP; -.
DR PDBsum; 7CZY; -.
DR PDBsum; 7CZZ; -.
DR AlphaFoldDB; P01834; -.
DR SMR; P01834; -.
DR ComplexPortal; CPX-6744; IgD - Ig kappa immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6911; IgM - Ig kappa immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6929; IgG1 - Ig kappa immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6936; IgG2 - Ig kappa immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6943; IgG3 - Ig kappa immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6949; IgG4 - Ig kappa immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6955; IgA1 - Ig kappa immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6962; IgA2 - Ig kappa immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6969; IgE - Ig kappa immunoglobulin complex, constant regions.
DR IntAct; P01834; 69.
DR MINT; P01834; -.
DR DrugBank; DB07909; (1S,2S,5S)2-(4-GLUTARIDYLBENZYL)-5-PHENYL-1-CYCLOHEXANOL.
DR DrugBank; DB07416; (2S)-2-(BUTYRYLOXY)-3-HYDROXYPROPYL NONANOATE.
DR DrugBank; DB07716; (4Z)-2,8:7,12:11,15:14,18:17,22-PENTAANHYDRO-4,5,6,9,10,13,19,20,21-NONADEOXY-D-ARABINO-D-ALLO-D-ALLO-DOCOSA-4,9,20-TRIENITOL.
DR DrugBank; DB07441; 3-{[(9-CYANO-9,10-DIHYDRO-10-METHYLACRIDIN-9-YL)CARBONYL]AMINO}PROPANOIC ACID.
DR DrugBank; DB08562; 4-(4-STYRYL-PHENYLCARBAMOYL)-BUTYRIC ACID.
DR DrugBank; DB07882; 4-{4-[2-(1A,7A-DIMETHYL-4-OXY-OCTAHYDRO-1-OXA-4-AZA-CYCLOPROPA[A]NAPHTHALEN-4-YL) -ACETYLAMINO]-PHENYLCARBAMOYL}-BUTYRIC ACID.
DR DrugBank; DB07784; [4-(4-ACETYLAMINO-PHENYL)-3,5-DIOXO-4-AZA-TRICYCLO[5.2.2.0 2,6]UNDEC-1-YLCARBAMOYLOXY]-ACETIC ACID.
DR DrugBank; DB07375; Etiocholanedione.
DR DrugBank; DB08413; METHYL-PHOSPHONIC ACID MONO-(4-NITRO-PHENYL) ESTER.
DR DrugBank; DB04688; Methylecgonine.
DR DrugBank; DB08289; N-(PARA-GLUTARAMIDOPHENYL-ETHYL)-PIPERIDINIUM-N-OXIDE.
DR DrugBank; DB07893; PHENYL[1-(N-SUCCINYLAMINO)PENTYL]PHOSPHONATE.
DR DrugBank; DB01851; Tetrabutylammonium Ion.
DR DrugBank; DB08647; Trazeolide.
DR IMGT_GENE-DB; IGKC; -.
DR CarbonylDB; P01834; -.
DR iPTMnet; P01834; -.
DR PhosphoSitePlus; P01834; -.
DR SwissPalm; P01834; -.
DR BioMuta; IGKC; -.
DR DMDM; 125145; -.
DR UCD-2DPAGE; P01834; -.
DR EPD; P01834; -.
DR jPOST; P01834; -.
DR MassIVE; P01834; -.
DR PeptideAtlas; P01834; -.
DR PRIDE; P01834; -.
DR ProteomicsDB; 51490; -.
DR ABCD; P01834; 2 sequenced antibodies.
DR UCSC; uc061lpw.1; human.
DR UCSC; uc061lpy.1; human.
DR GeneCards; IGKC; -.
DR HGNC; HGNC:5716; IGKC.
DR MalaCards; IGKC; -.
DR MIM; 147200; gene.
DR MIM; 614102; phenotype.
DR neXtProt; NX_P01834; -.
DR Orphanet; 183675; Recurrent infections associated with rare immunoglobulin isotypes deficiency.
DR InParanoid; P01834; -.
DR PhylomeDB; P01834; -.
DR PathwayCommons; P01834; -.
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; P01834; -.
DR ChiTaRS; IGKC; human.
DR EvolutionaryTrace; P01834; -.
DR Pharos; P01834; Tdark.
DR PRO; PR:P01834; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; P01834; 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; 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; IDA: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 GO; GO:0001895; P:retina homeostasis; HEP:UniProtKB.
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; Cell membrane; Direct protein sequencing;
KW Disease variant; Disulfide bond; Immunity; Immunoglobulin;
KW Immunoglobulin domain; Membrane; Reference proteome; Secreted.
FT CHAIN <1..107
FT /note="Immunoglobulin kappa constant"
FT /id="PRO_0000153596"
FT DOMAIN 6..103
FT /note="Ig-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 27..87
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:4923144"
FT DISULFID 107
FT /note="Interchain (with a heavy chain)"
FT /evidence="ECO:0000269|PubMed:4923144"
FT VARIANT 41
FT /note="W -> R (in IGKCD)"
FT /evidence="ECO:0000269|PubMed:3931219"
FT /id="VAR_066403"
FT VARIANT 84
FT /note="V -> L"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_003897"
FT CONFLICT 15
FT /note="D -> N (in Ref. 2; AA sequence and 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 58
FT /note="E -> Q (in Ref. 3; AA sequence and 1; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 1
FT STRAND 1..3
FT /evidence="ECO:0007829|PDB:7CZZ"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:5EWI"
FT HELIX 15..19
FT /evidence="ECO:0007829|PDB:5EWI"
FT STRAND 22..35
FT /evidence="ECO:0007829|PDB:5EWI"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:5EWI"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:1DFB"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:5EWI"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:5EWI"
FT STRAND 66..75
FT /evidence="ECO:0007829|PDB:5EWI"
FT HELIX 76..81
FT /evidence="ECO:0007829|PDB:5EWI"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:5EWI"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:5EWI"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:5EWI"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:1I7Z"
SQ SEQUENCE 107 AA; 11765 MW; B97BEEBBA4D0B291 CRC64;
RTVAAPSVFI FPPSDEQLKS GTASVVCLLN NFYPREAKVQ WKVDNALQSG NSQESVTEQD
SKDSTYSLSS TLTLSKADYE KHKVYACEVT HQGLSSPVTK SFNRGEC
