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Protein

Immunoglobulin kappa constant

Gene

IGKC

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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

Caution

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

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

Protein family/group databases

IMGT/GENE-DBIGKC

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

EuPathDBiHostDB:ENSG00000211592.7
HGNCiHGNC:5716 IGKC
MIMi147200 gene
neXtProtiNX_P01834

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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
ProteomicsDBi51490

2D gel databases

UCD-2DPAGEiP01834

PTM databases

CarbonylDBiP01834
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
MINTiP01834

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[»]
5VEBX-ray2.34B/L1-107[»]
5VIYelectron microscopy6.20G/I1-107[»]
6AU5X-ray2.48A/C1-106[»]
6AXPX-ray2.48A/C1-106[»]
6AYNX-ray2.48A/C1-106[»]
6AZKX-ray2.48A/C1-106[»]
6AZLX-ray2.48A/C1-106[»]
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
IPR036179 Ig-like_dom_sf
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

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 20, 2018
This is version 178 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

Keywords - Technical termi

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

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