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Protein

Immunoglobulin kappa constant

Gene

IGKC

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).3 Publications

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processAdaptive immunity, Immunity

Enzyme and pathway databases

ReactomeiR-HSA-166663. Initial triggering of complement.
R-HSA-173623. Classical antibody-mediated complement activation.
R-HSA-198933. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
R-HSA-202733. Cell surface interactions at the vascular wall.
R-HSA-2029481. FCGR activation.
R-HSA-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-HSA-2029485. Role of phospholipids in phagocytosis.
R-HSA-2168880. Scavenging of heme from plasma.
R-HSA-2454202. Fc epsilon receptor (FCERI) signaling.
R-HSA-2730905. Role of LAT2/NTAL/LAB on calcium mobilization.
R-HSA-2871796. FCERI mediated MAPK activation.
R-HSA-2871809. FCERI mediated Ca+2 mobilization.
R-HSA-2871837. FCERI mediated NF-kB activation.
R-HSA-5690714. CD22 mediated BCR regulation.
R-HSA-977606. Regulation of Complement cascade.
R-HSA-983695. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.

Names & Taxonomyi

Protein namesi
Recommended name:
Immunoglobulin kappa constant2 Publications
Alternative name(s):
Ig kappa chain C regionCurated
Ig kappa chain C region AG1 Publication
Ig kappa chain C region CUM1 Publication
Ig kappa chain C region EU1 Publication
Ig kappa chain C region OU1 Publication
Ig kappa chain C region ROY1 Publication
Ig kappa chain C region TI1 Publication
Gene namesi
Name:IGKC2 Publications
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:5716. IGKC.

Subcellular locationi

GO - Cellular componenti

  • blood microparticle Source: UniProtKB
  • external side of plasma membrane Source: GO_Central
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
  • immunoglobulin complex, circulating Source: GO_Central
  • plasma membrane Source: Reactome

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Involvement in diseasei

Immunoglobulin kappa light chain deficiency (IGKCD)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disease characterized by the complete absence of immunoglobulin kappa chains.
See also OMIM:614102
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06640341W → R in IGKCD. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi3514.
MalaCardsiIGKC.
MIMi614102. phenotype.
Orphaneti183675. Recurrent infections associated with rare immunoglobulin isotypes deficiency.

Chemistry databases

DrugBankiDB07416. (2S)-2-(BUTYRYLOXY)-3-HYDROXYPROPYL NONANOATE.
DB08562. 4-(4-STYRYL-PHENYLCARBAMOYL)-BUTYRIC ACID.
DB04688. ECGONINE METHYL ESTER.
DB08413. METHYL-PHOSPHONIC ACID MONO-(4-NITRO-PHENYL) ESTER.
DB08289. N-(PARA-GLUTARAMIDOPHENYL-ETHYL)-PIPERIDINIUM-N-OXIDE.
DB07893. PHENYL[1-(N-SUCCINYLAMINO)PENTYL]PHOSPHONATE.
DB01851. Tetrabutylammonium Ion.
DB08647. TRAZEOLIDE.

Polymorphism and mutation databases

DMDMi125145.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000153596‹1 – 107Immunoglobulin kappa constantAdd BLAST›107

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi27 ↔ 87PROSITE-ProRule annotation1 Publication
Disulfide bondi107Interchain (with a heavy chain)1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

EPDiP01834.
PeptideAtlasiP01834.
PRIDEiP01834.

2D gel databases

UCD-2DPAGEiP01834.

PTM databases

iPTMnetiP01834.
PhosphoSitePlusiP01834.
SwissPalmiP01834.

Expressioni

Gene expression databases

BgeeiENSG00000211592.
CleanExiHS_IGKC.

Interactioni

Subunit structurei

Immunoglobulins are composed of two identical heavy chains and two identical light chains; disulfide-linked.1 Publication

GO - Molecular functioni

Protein-protein interaction databases

IntActiP01834. 39 interactors.
MINTiMINT-159227.

Structurei

Secondary structure

1107
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 11Combined sources5
Helixi15 – 18Combined sources4
Turni19 – 21Combined sources3
Beta strandi22 – 35Combined sources14
Beta strandi37 – 45Combined sources9
Beta strandi46 – 48Combined sources3
Beta strandi50 – 56Combined sources7
Turni61 – 63Combined sources3
Beta strandi66 – 75Combined sources10
Helixi76 – 79Combined sources4
Beta strandi83 – 91Combined sources9
Beta strandi94 – 96Combined sources3
Beta strandi98 – 103Combined sources6
Turni104 – 106Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A4JX-ray2.10A/L2-105[»]
1A4KX-ray2.40A/L2-105[»]
1CLYX-ray2.50L2-107[»]
1D5BX-ray2.80A/L2-104[»]
1D5IX-ray2.00L2-104[»]
1D6VX-ray2.00L2-104[»]
1DFBX-ray2.70L2-107[»]
1GAFX-ray1.95L2-107[»]
1HEZX-ray2.70A/C2-107[»]
1HKLX-ray2.68L2-107[»]
1HZHX-ray2.70L/M2-107[»]
1I7ZX-ray2.30A/C2-107[»]
1MIMX-ray2.60L2-106[»]
1N0XX-ray1.80L/M2-107[»]
1OM3X-ray2.20L/M2-106[»]
1OP3X-ray1.75K/L2-106[»]
1OP5X-ray3.00K/L2-106[»]
1UCBX-ray2.50L2-107[»]
2NY7X-ray2.30L2-107[»]
2O5XX-ray2.05L2-107[»]
2O5YX-ray2.85L2-107[»]
2O5ZX-ray2.40L2-107[»]
2QQKX-ray2.75L2-107[»]
2QQLX-ray3.10L2-107[»]
2QQNX-ray2.20L2-107[»]
2QSCX-ray2.80L2-107[»]
2R56X-ray2.80L/M2-104[»]
2RFXX-ray2.50C94-102[»]
2VXQX-ray1.90L2-107[»]
3B2UX-ray2.58D/G/K/L/O/R/U/X2-105[»]
3B2VX-ray3.30L2-105[»]
3BDYX-ray2.60L2-107[»]
3BE1X-ray2.90L2-107[»]
3BKYX-ray2.61L2-107[»]
3BN9X-ray2.17C/E2-107[»]
3BQUX-ray3.00A2-107[»]
3C08X-ray2.15L2-106[»]
3C09X-ray3.20B/L2-106[»]
3CFJX-ray2.60A/C/E/L2-107[»]
3CFKX-ray2.60A/C/E/G/J/L/M/O2-107[»]
3CSYX-ray3.40B/D/F/H2-104[»]
3D0LX-ray2.35A2-106[»]
3D85X-ray1.90A2-107[»]
3DVGX-ray2.60A2-107[»]
3DVNX-ray2.70A/L2-107[»]
3EYFX-ray2.30A/C2-107[»]
3EYOX-ray2.50A/C2-107[»]
3EYQX-ray2.40C2-107[»]
3IU3X-ray2.90B/D/L2-106[»]
3O11X-ray2.80A/L2-107[»]
3QCTX-ray2.15L3-106[»]
3QCUX-ray1.98L/M3-106[»]
3QCVX-ray2.51L/M3-106[»]
3RU8X-ray2.07L2-107[»]
3U0WX-ray2.00L2-107[»]
3U7WX-ray2.60L2-107[»]
3U7YX-ray2.45L2-107[»]
3VH8X-ray1.80C/F94-102[»]
3WUWX-ray2.00C94-102[»]
3X11X-ray2.15C94-102[»]
3X12X-ray1.80C94-102[»]
4D3CX-ray2.62L2-107[»]
4D9RX-ray2.42D/L3-107[»]
4HIXX-ray2.20L2-107[»]
4NM4X-ray2.65L/M2-107[»]
4NM8X-ray4.00L/M/N2-107[»]
4XMPX-ray1.78L2-107[»]
4XNYX-ray2.30L2-107[»]
4XNZX-ray3.39C/F/L2-107[»]
4XXDX-ray2.41A/D2-107[»]
4YDVX-ray2.70A/L2-107[»]
5B38X-ray2.30C94-102[»]
5B39X-ray2.50C94-102[»]
5ESVX-ray3.10B/D/L2-107[»]
5ESZX-ray4.19B/L2-107[»]
ProteinModelPortaliP01834.
SMRiP01834.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01834.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini6 – 103Ig-likePROSITE-ProRule annotationAdd BLAST98

Keywords - Domaini

Immunoglobulin C region, Immunoglobulin domain

Phylogenomic databases

HOGENOMiHOG000059537.
HOVERGENiHBG039526.
InParanoidiP01834.
PhylomeDBiP01834.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiView protein in InterPro
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR003597. Ig_C1-set.
PfamiView protein in Pfam
PF07654. C1-set. 1 hit.
SMARTiView protein in SMART
SM00407. IGc1. 1 hit.
SUPFAMiSSF48726. SSF48726. 1 hit.
PROSITEiView protein in PROSITE
PS50835. IG_LIKE. 1 hit.
PS00290. IG_MHC. 1 hit.

Sequencei

Sequence statusi: Complete.

P01834-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
RTVAAPSVFI FPPSDEQLKS GTASVVCLLN NFYPREAKVQ WKVDNALQSG
60 70 80 90 100
NSQESVTEQD SKDSTYSLSS TLTLSKADYE KHKVYACEVT HQGLSSPVTK

SFNRGEC
Length:107
Mass (Da):11,765
Last modified:March 15, 2017 - v2
Checksum:iB97BEEBBA4D0B291
GO

Sequence cautioni

The sequence AAA58989 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11
Sequence conflicti15D → N AA sequence (PubMed:4893682).Curated1
Sequence conflicti15D → N AA sequence (PubMed:5447531).Curated1
Sequence conflicti58E → Q AA sequence (Ref. 3) Curated1
Sequence conflicti58E → Q AA sequence (PubMed:5586923).Curated1

Polymorphismi

There are several alleles. The sequence shown is that of IMGT allele IGKC*01.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06640341W → R in IGKCD. 1 Publication1
Natural variantiVAR_00389784V → L1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J00241 Genomic DNA. Translation: AAA58989.1. Different initiation.
AC244205 Genomic DNA. No translation available.
PIRiB90562. K3HU.
UniGeneiHs.449609.

Genome annotation databases

UCSCiuc061lpy.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J00241 Genomic DNA. Translation: AAA58989.1. Different initiation.
AC244205 Genomic DNA. No translation available.
PIRiB90562. K3HU.
UniGeneiHs.449609.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A4JX-ray2.10A/L2-105[»]
1A4KX-ray2.40A/L2-105[»]
1CLYX-ray2.50L2-107[»]
1D5BX-ray2.80A/L2-104[»]
1D5IX-ray2.00L2-104[»]
1D6VX-ray2.00L2-104[»]
1DFBX-ray2.70L2-107[»]
1GAFX-ray1.95L2-107[»]
1HEZX-ray2.70A/C2-107[»]
1HKLX-ray2.68L2-107[»]
1HZHX-ray2.70L/M2-107[»]
1I7ZX-ray2.30A/C2-107[»]
1MIMX-ray2.60L2-106[»]
1N0XX-ray1.80L/M2-107[»]
1OM3X-ray2.20L/M2-106[»]
1OP3X-ray1.75K/L2-106[»]
1OP5X-ray3.00K/L2-106[»]
1UCBX-ray2.50L2-107[»]
2NY7X-ray2.30L2-107[»]
2O5XX-ray2.05L2-107[»]
2O5YX-ray2.85L2-107[»]
2O5ZX-ray2.40L2-107[»]
2QQKX-ray2.75L2-107[»]
2QQLX-ray3.10L2-107[»]
2QQNX-ray2.20L2-107[»]
2QSCX-ray2.80L2-107[»]
2R56X-ray2.80L/M2-104[»]
2RFXX-ray2.50C94-102[»]
2VXQX-ray1.90L2-107[»]
3B2UX-ray2.58D/G/K/L/O/R/U/X2-105[»]
3B2VX-ray3.30L2-105[»]
3BDYX-ray2.60L2-107[»]
3BE1X-ray2.90L2-107[»]
3BKYX-ray2.61L2-107[»]
3BN9X-ray2.17C/E2-107[»]
3BQUX-ray3.00A2-107[»]
3C08X-ray2.15L2-106[»]
3C09X-ray3.20B/L2-106[»]
3CFJX-ray2.60A/C/E/L2-107[»]
3CFKX-ray2.60A/C/E/G/J/L/M/O2-107[»]
3CSYX-ray3.40B/D/F/H2-104[»]
3D0LX-ray2.35A2-106[»]
3D85X-ray1.90A2-107[»]
3DVGX-ray2.60A2-107[»]
3DVNX-ray2.70A/L2-107[»]
3EYFX-ray2.30A/C2-107[»]
3EYOX-ray2.50A/C2-107[»]
3EYQX-ray2.40C2-107[»]
3IU3X-ray2.90B/D/L2-106[»]
3O11X-ray2.80A/L2-107[»]
3QCTX-ray2.15L3-106[»]
3QCUX-ray1.98L/M3-106[»]
3QCVX-ray2.51L/M3-106[»]
3RU8X-ray2.07L2-107[»]
3U0WX-ray2.00L2-107[»]
3U7WX-ray2.60L2-107[»]
3U7YX-ray2.45L2-107[»]
3VH8X-ray1.80C/F94-102[»]
3WUWX-ray2.00C94-102[»]
3X11X-ray2.15C94-102[»]
3X12X-ray1.80C94-102[»]
4D3CX-ray2.62L2-107[»]
4D9RX-ray2.42D/L3-107[»]
4HIXX-ray2.20L2-107[»]
4NM4X-ray2.65L/M2-107[»]
4NM8X-ray4.00L/M/N2-107[»]
4XMPX-ray1.78L2-107[»]
4XNYX-ray2.30L2-107[»]
4XNZX-ray3.39C/F/L2-107[»]
4XXDX-ray2.41A/D2-107[»]
4YDVX-ray2.70A/L2-107[»]
5B38X-ray2.30C94-102[»]
5B39X-ray2.50C94-102[»]
5ESVX-ray3.10B/D/L2-107[»]
5ESZX-ray4.19B/L2-107[»]
ProteinModelPortaliP01834.
SMRiP01834.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP01834. 39 interactors.
MINTiMINT-159227.

Chemistry databases

DrugBankiDB07416. (2S)-2-(BUTYRYLOXY)-3-HYDROXYPROPYL NONANOATE.
DB08562. 4-(4-STYRYL-PHENYLCARBAMOYL)-BUTYRIC ACID.
DB04688. ECGONINE METHYL ESTER.
DB08413. METHYL-PHOSPHONIC ACID MONO-(4-NITRO-PHENYL) ESTER.
DB08289. N-(PARA-GLUTARAMIDOPHENYL-ETHYL)-PIPERIDINIUM-N-OXIDE.
DB07893. PHENYL[1-(N-SUCCINYLAMINO)PENTYL]PHOSPHONATE.
DB01851. Tetrabutylammonium Ion.
DB08647. TRAZEOLIDE.

PTM databases

iPTMnetiP01834.
PhosphoSitePlusiP01834.
SwissPalmiP01834.

Polymorphism and mutation databases

DMDMi125145.

2D gel databases

UCD-2DPAGEiP01834.

Proteomic databases

EPDiP01834.
PeptideAtlasiP01834.
PRIDEiP01834.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiuc061lpy.1. human.

Organism-specific databases

DisGeNETi3514.
GeneCardsiIGKC.
H-InvDBiHIX0161619.
HGNCiHGNC:5716. IGKC.
MalaCardsiIGKC.
MIMi147200. gene.
614102. phenotype.
neXtProtiNX_P01834.
Orphaneti183675. Recurrent infections associated with rare immunoglobulin isotypes deficiency.
GenAtlasiSearch...

Phylogenomic databases

HOGENOMiHOG000059537.
HOVERGENiHBG039526.
InParanoidiP01834.
PhylomeDBiP01834.

Enzyme and pathway databases

ReactomeiR-HSA-166663. Initial triggering of complement.
R-HSA-173623. Classical antibody-mediated complement activation.
R-HSA-198933. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
R-HSA-202733. Cell surface interactions at the vascular wall.
R-HSA-2029481. FCGR activation.
R-HSA-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-HSA-2029485. Role of phospholipids in phagocytosis.
R-HSA-2168880. Scavenging of heme from plasma.
R-HSA-2454202. Fc epsilon receptor (FCERI) signaling.
R-HSA-2730905. Role of LAT2/NTAL/LAB on calcium mobilization.
R-HSA-2871796. FCERI mediated MAPK activation.
R-HSA-2871809. FCERI mediated Ca+2 mobilization.
R-HSA-2871837. FCERI mediated NF-kB activation.
R-HSA-5690714. CD22 mediated BCR regulation.
R-HSA-977606. Regulation of Complement cascade.
R-HSA-983695. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.

Miscellaneous databases

EvolutionaryTraceiP01834.
PROiPR:P01834.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000211592.
CleanExiHS_IGKC.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiView protein in InterPro
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR003597. Ig_C1-set.
PfamiView protein in Pfam
PF07654. C1-set. 1 hit.
SMARTiView protein in SMART
SM00407. IGc1. 1 hit.
SUPFAMiSSF48726. SSF48726. 1 hit.
PROSITEiView protein in PROSITE
PS50835. IG_LIKE. 1 hit.
PS00290. IG_MHC. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiIGKC_HUMAN
AccessioniPrimary (citable) accession number: P01834
Secondary accession number(s): A0A075B6H6, A0A087X130
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: March 15, 2017
Last modified: June 7, 2017
This is version 170 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Caution

For an example of a full length immunoglobulin kappa light chain see AC P0DOX7.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.