P01834 (IGKC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ig kappa chain C region

Gene names

Name:

IGKC

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	106 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Involvement in disease	Defects in IGKC are the cause of immunoglobulin kappa light chain deficiency (IGKCD) [MIM:614102]. IGKCD is a disease characterized by the complete absence of immunoglobulin kappa chains. Ref.10
Miscellaneous	The EU sequence has the INV (3) allotypic marker, Ala-45 and Val-83. The ROY sequence has the INV (1,2) allotypic marker, Ala-45 and Leu-83.
Sequence similarities	Contains 1 Ig-like (immunoglobulin-like) domain.

Ontologies

Keywords
Disease	Disease mutation
Domain	Immunoglobulin C region Immunoglobulin domain
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	complement activation, classical pathway Traceable author statement. Source: Reactome innate immune response Traceable author statement. Source: Reactome
Cellular component	extracellular region Traceable author statement. Source: Reactome
Molecular function	antigen binding Non-traceable author statement Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

‹1 – 106

›106

Ig kappa chain C region

PRO_0000153596

Regions

Domain

5 – 102

98

Ig-like

Amino acid modifications

Disulfide bond

26 ↔ 86

Ref.2

Disulfide bond

106

Interchain (with a heavy chain) Ref.2

Natural variations

Natural variant

40

1

W → R in IGKCD. Ref.10

VAR_066403

Natural variant

83

1

V → L in INV(1,2) marker.

VAR_003897

Experimental info

Sequence conflict

14

1

D → N AA sequence Ref.7

Sequence conflict

14

1

D → N AA sequence Ref.8

Sequence conflict

57

1

E → Q AA sequence Ref.5

Sequence conflict

57

1

E → Q AA sequence Ref.6

Non-terminal residue

1

1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

106

Helix Strand Turn

Details...

Beta strand

6 – 10

5

Helix

14 – 19

6

Beta strand

21 – 34

14

Beta strand

37 – 42

6

Beta strand

49 – 55

7

Turn

60 – 62

3

Beta strand

65 – 74

10

Helix

75 – 80

6

Beta strand

83 – 89

7

Beta strand

97 – 102

6

Sequences

	Sequence		Length	Mass (Da)
	P01834 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 51984D1FDD372CE8	FASTA	106	11,609
	10 20 30 40 50 60 TVAAPSVFIF PPSDEQLKSG TASVVCLLNN FYPREAKVQW KVDNALQSGN SQESVTEQDS 70 80 90 100 KDSTYSLSST LTLSKADYEK HKVYACEVTH QGLSSPVTKS FNRGEC

References

[1]	"The covalent structure of a human gamma G-immunoglobulin. VI. Amino acid sequence of the light chain." Gottlieb P.D., Cunningham B.A., Rutishauser U., Edelman G.M. Biochemistry 9:3155-3161(1970) [PubMed: 5489770] [Abstract] Cited for: PROTEIN SEQUENCE (MYELOMA PROTEIN EU).
[2]	"The covalent structure of a human gamma G-immunoglobulin. X. Intrachain disulfide bonds." Gall W.E., Edelman G.M. Biochemistry 9:3188-3196(1970) [PubMed: 4923144] [Abstract] Cited for: DISULFIDE BONDS.
[3]	"Rule of antibody structure. The primary structure of a monoclonal immunoglobulin L-chain of kappa-type, subgroup 3 (Bence-Jones protein Ti). IV. The complete amino acid sequence and its significance for the mechanism of antibody production." Suter L., Barnikol H.U., Watanabe S., Hilschmann N. Hoppe-Seyler's Z. Physiol. Chem. 353:189-208(1972) [PubMed: 5027703] [Abstract] Cited for: PROTEIN SEQUENCE (BENCE-JONES PROTEIN TI).
[4]	"Cloned human and mouse kappa immunoglobulin constant and J region genes conserve homology in functional segments." Hieter P.A., Max E.E., Seidman J.G., Maizel J.V. Jr., Leder P. Cell 22:197-207(1980) [PubMed: 6775818] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	Hilschmann N., Barnikol H.U., Hess M., Langer B., Ponstingl H., Steinmetz-Kayne M., Suter L., Watanabe S. (In) Franek F., Shugar D. (eds.); Gamma globulins: structure and function, pp.57-74, Academic Press, New York (1969) Cited for: PROTEIN SEQUENCE (BENCE-JONES PROTEIN ROY).
[6]	"The complete amino acid sequence of Bence Jones protein Cum (kappa-type)." Hilschmann N. Hoppe-Seyler's Z. Physiol. Chem. 348:1718-1722(1967) [PubMed: 5586923] [Abstract] Cited for: PROTEIN SEQUENCE (BENCE-JONES PROTEIN CUM).
[7]	"The amino acid sequence of a kappa type Bence-Jones protein. 3. The complete sequence and the location of the disulfide bridges." Titani K., Shinoda T., Putnam F.W. J. Biol. Chem. 244:3550-3560(1969) [PubMed: 4893682] [Abstract] Cited for: PROTEIN SEQUENCE (BENCE-JONES PROTEIN AG).
[8]	"Macroglobulin structure: variable sequence of light and heavy chains." Kohler H., Shimizu A., Paul C., Putnam F.W. Science 169:56-59(1970) [PubMed: 5447531] [Abstract] Cited for: PROTEIN SEQUENCE (WALDENSTROM'S MACROGLOBULIN OU).
[9]	"Extended analysis of AL-amyloid protein from abdominal wall subcutaneous fat biopsy: kappa IV immunoglobulin light chain." Olsen K.E., Sletten K., Westermark P. Biochem. Biophys. Res. Commun. 245:713-716(1998) [PubMed: 9588180] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-33; 38-41 AND 62-80. Tissue: Abdominal adipose tissue.
[10]	"Molecular defects in a human immunoglobulin kappa chain deficiency." Stavnezer-Nordgren J., Kekish O., Zegers B.J. Science 230:458-461(1985) [PubMed: 3931219] [Abstract] Cited for: VARIANT IGKCD ARG-40.
+	Additional computationally mapped references.

Web resources

IMGT/GENE-DB

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J00241 Genomic DNA. Translation: AAA58989.1.

IPI

IPI00979250.

PIR

K3HU. B90562.

UniGene

Hs.449621.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A4J	X-ray	2.10	A/L	1-104	[»]
1A4K	X-ray	2.40	A/L	1-104	[»]
1D5B	X-ray	2.80	A/L	1-103	[»]
1D5I	X-ray	2.00	L	1-103	[»]
1D6V	X-ray	2.00	L	1-103	[»]
1HEZ	X-ray	2.70	A/C	1-106	[»]
1HKL	X-ray	2.68	L	1-106	[»]
1I7Z	X-ray	2.30	A/C	1-106	[»]
1MIM	X-ray	2.60	L	1-105	[»]
1UCB	X-ray	2.50	L	1-106	[»]
2O5X	X-ray	2.05	L	1-106	[»]
2O5Y	X-ray	2.85	L	1-106	[»]
2O5Z	X-ray	2.40	L	1-106	[»]
2QQK	X-ray	2.75	L	1-106	[»]
2QQL	X-ray	3.10	L	1-106	[»]
2QQN	X-ray	2.20	L	1-106	[»]
2QSC	X-ray	2.80	L	1-106	[»]
2R56	X-ray	2.80	L/M	1-103	[»]
2VXQ	X-ray	1.90	L	1-106	[»]
3B2U	X-ray	2.58	D/G/K/L/O/R/U/X	1-104	[»]
3B2V	X-ray	3.30	L	1-104	[»]
3BDY	X-ray	2.60	L	1-106	[»]
3BE1	X-ray	2.90	L	1-106	[»]
3BKY	X-ray	2.61	L	1-106	[»]
3BN9	X-ray	2.17	C/E	1-106	[»]
3BQU	X-ray	3.00	A	1-106	[»]
3C08	X-ray	2.15	L	1-105	[»]
3C09	X-ray	3.20	B/L	1-105	[»]
3CFJ	X-ray	2.60	A/C/E/L	1-106	[»]
3CFK	X-ray	2.60	A/C/E/G/J/L/M/O	1-106	[»]
3CSY	X-ray	3.40	B/D/F/H	1-103	[»]
3D0L	X-ray	2.35	A	1-105	[»]
3D85	X-ray	1.90	A	1-106	[»]
3DVG	X-ray	2.60	A	1-106	[»]
3DVN	X-ray	2.70	A/L	1-106	[»]
3EYF	X-ray	2.30	A/C	1-106	[»]
3EYO	X-ray	2.50	A/C	1-106	[»]
3EYQ	X-ray	2.40	C	1-106	[»]
3U7W	X-ray	2.60	L	1-106	[»]
3U7Y	X-ray	2.45	L	1-106	[»]
3VH8	X-ray	1.80	C/F	93-101	[»]

ProteinModelPortal

P01834.

SMR

P01834. Positions 1-105.

ModBase

Search...

Protein-protein interaction databases

IntAct

P01834. 35 interactions.

MINT

MINT-159227.

STRING

P01834.

Protein family/group databases

IMGT

Search...

Polymorphism databases

DMDM

125145.

2D gel databases

Cornea-2DPAGE

P01834.

UCD-2DPAGE

P01834.

Proteomic databases

PRIDE

P01834.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000390237; ENSP00000374777; ENSG00000211592.
ENST00000429992; ENSP00000409413; ENSG00000251039.
ENST00000448155; ENSP00000406382; ENSG00000251546.

Organism-specific databases

GeneCards

GC02M089156.
GC02P089890.
GC02P089903.

H-InvDB

HIX0021121.
HIX0161619.
HIX0175869.

HGNC

HGNC:5716. IGKC.

MIM

147200. gene.
614102. phenotype.

neXtProt

NX_P01834.

Orphanet

183675. Recurrent infections associated with rare immunoglobulin isotypes deficiency.

GenAtlas

Search...

Phylogenomic databases

GeneTree

ENSGT00560000076683.

HOVERGEN

HBG039526.

InParanoid

P01834.

OrthoDB

EOG408N9K.
EOG412M6X.
EOG4XSKRF.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P01834.

Bgee

P01834.

CleanEx

HS_IGKC.

Genevestigator

P01834.

GermOnline

ENSG00000163245. Homo sapiens.

Family and domain databases

InterPro

IPR007110. Ig-like.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR003597. Ig_C1-set.
[Graphical view]

Gene3D

G3DSA:2.60.40.10. Ig-like_fold. 1 hit.

Pfam

PF07654. C1-set. 1 hit.
[Graphical view]

SMART

SM00407. IGc1. 1 hit.
[Graphical view]

PROSITE

PS50835. IG_LIKE. 1 hit.
PS00290. IG_MHC. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

SOURCE

Search...

Entry information

Entry name

IGKC_HUMAN

Accession

Primary (citable) accession number: P01834

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	January 25, 2012
This is version 120 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.