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Protein

Immunoglobulin kappa variable 1-39

Gene

IGKV1-39

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

Functioni

V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition. 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:20176268, PubMed:22158414). 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:20176268, PubMed:17576170).3 Publications

GO - Molecular functioni

  • antigen binding Source: UniProtKB
  • serine-type endopeptidase activity Source: Reactome

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Adaptive 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-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-983695. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.

Names & Taxonomyi

Protein namesi
Recommended name:
Immunoglobulin kappa variable 1-392 Publications
Alternative name(s):
Ig kappa chain V-I region DEE1 Publication
Ig kappa chain V-I region Hau1 Publication
Ig kappa chain V-I region Mev1 Publication
Ig kappa chain V-I region OU1 Publication
Ig kappa chain V-I region Walker1 Publication
Gene namesi
Name:IGKV1-392 Publications
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:5740. IGKV1-39.

Subcellular locationi

GO - Cellular componenti

  • blood microparticle Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: UniProtKB
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Organism-specific databases

OpenTargetsiENSG00000242371.
ENSG00000251546.
ENSG00000282120.

Polymorphism and mutation databases

DMDMi125761.
125764.
125770.
125776.
125779.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 224 PublicationsAdd BLAST22
ChainiPRO_000005974123 – 117Immunoglobulin kappa variable 1-394 PublicationsAdd BLAST95

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi45 ↔ 110PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PeptideAtlasiP01597.
PRIDEiP01597.

Interactioni

Subunit structurei

Immunoglobulins are composed of two identical heavy chains and two identical light chains, linked by disulfide bonds.1 Publication

Structurei

Secondary structure

1117
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 7Combined sources4
Beta strandi9 – 13Combined sources5
Beta strandi19 – 27Combined sources9
Beta strandi33 – 38Combined sources6
Beta strandi45 – 49Combined sources5
Turni50 – 52Combined sources3
Beta strandi62 – 67Combined sources6
Beta strandi70 – 77Combined sources8
Helixi80 – 82Combined sources3
Beta strandi84 – 90Combined sources7
Beta strandi92 – 95Combined sources4
Beta strandi102 – 105Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DGXmodel-L23-117[»]
1F6LX-ray2.80L23-117[»]
3UPAX-ray1.80A/B23-117[»]
ProteinModelPortaliP01597.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01600.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini24 – ›117Ig-likePROSITE-ProRule annotationAdd BLAST›94

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni23 – 45Framework-11 PublicationAdd BLAST23
Regioni46 – 56Complementarity-determining-11 PublicationAdd BLAST11
Regioni57 – 71Framework-21 PublicationAdd BLAST15
Regioni72 – 78Complementarity-determining-21 Publication7
Regioni79 – 110Framework-31 PublicationAdd BLAST32
Regioni111 – ›117Complementarity-determining-31 Publication›7

Sequence similaritiesi

Contains 1 Ig-like (immunoglobulin-like) domain.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Immunoglobulin V region, Signal

Phylogenomic databases

HOVERGENiHBG018013.
OMAiQAGHTLC.
PhylomeDBiP01597.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
[Graphical view]
PfamiPF07686. V-set. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
SM00406. IGv. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P01597-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDMRVPAQLL GLLLLWLRGA RCDIQMTQSP SSLSASVGDR VTITCRASQS
60 70 80 90 100
ISSYLNWYQQ KPGKAPKLLI YAASSLQSGV PSRFSGSGSG TDFTLTISSL
110
QPEDFATYYC QQSYSTP
Length:117
Mass (Da):12,737
Last modified:November 2, 2016 - v2
Checksum:iED1DC5B0055AB9D4
GO

Sequence cautioni

The sequence CAA25477 differs from that shown. =Chimeric DNA. A chimeric DNA corresponding to regions V and J of immunoglobulin kappa light chain.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti24I → D AA sequence (PubMed:6816713).Curated1
Sequence conflicti42T → I AA sequence (PubMed:6816713).Curated1
Sequence conflicti48S → G AA sequence (PubMed:5124396).Curated1
Sequence conflicti50S → T AA sequence (PubMed:5447531).Curated1
Sequence conflicti51 – 53ISS → SVD AA sequence (PubMed:6816713).Curated3
Sequence conflicti51 – 53ISS → VNK AA sequence (PubMed:5124396).Curated3
Sequence conflicti53S → N in CAA25477 (PubMed:6091049).Curated1
Sequence conflicti56N → S AA sequence (PubMed:4097974).Curated1
Sequence conflicti67K → B AA sequence (PubMed:5447531).Curated1
Sequence conflicti67K → Q AA sequence (PubMed:4097974).Curated1
Sequence conflicti68L → V AA sequence (PubMed:5124396).Curated1
Sequence conflicti68L → V AA sequence (PubMed:4097974).Curated1
Sequence conflicti71Y → F AA sequence (PubMed:5124396).Curated1
Sequence conflicti71Y → F AA sequence (PubMed:6816713).Curated1
Sequence conflicti72 – 73AA → DT AA sequence (PubMed:6816713).Curated2
Sequence conflicti75 – 77SLQ → BLH AA sequence (PubMed:5447531).Curated3
Sequence conflicti75S → N AA sequence (PubMed:6816713).Curated1
Sequence conflicti77Q → K AA sequence (PubMed:5124396).Curated1
Sequence conflicti77Q → P AA sequence (PubMed:4097974).Curated1
Sequence conflicti81P → T in CAA25477 (PubMed:6091049).Curated1
Sequence conflicti87 – 88SG → GR AA sequence (PubMed:6816713).Curated2
Sequence conflicti95L → F AA sequence (PubMed:5447531).Curated1
Sequence conflicti99 – 101SLQ → GLL AA sequence (PubMed:5124396).Curated3
Sequence conflicti103E → D AA sequence (PubMed:6816713).Curated1
Sequence conflicti105F → S in CAA25477 (PubMed:6091049).Curated1
Sequence conflicti113 – 115SYS → NYI AA sequence (PubMed:4097974).Curated3
Sequence conflicti115S → T AA sequence (PubMed:5124396).Curated1
Sequence conflicti115S → T AA sequence (PubMed:6816713).Curated1
Sequence conflicti116T → N AA sequence (PubMed:6816713).Curated1
Sequence conflicti116T → S AA sequence (PubMed:5447531).Curated1
Sequence conflicti117P → L in CAA25477 (PubMed:6091049).Curated1
Non-terminal residuei1171

Polymorphismi

There are several alleles. The sequence shown is that of IMGT allele IGKV1-39*01.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00965 Genomic DNA. Translation: CAA25477.1. Sequence problems.
AC244255 Genomic DNA. No translation available.
PIRiA01865. K1HUDE.
A01868. K1HUHU.
A01872. K1HUOU.
A01879. K1HUMV.
A01883. K1HUWK.
A27594.
UniGeneiHs.449609.

Genome annotation databases

EnsembliENST00000498574; ENSP00000419058; ENSG00000242371.
ENST00000631411; ENSP00000488680; ENSG00000282120.

Cross-referencesi

Web resourcesi

IMGT/GENE-DB

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00965 Genomic DNA. Translation: CAA25477.1. Sequence problems.
AC244255 Genomic DNA. No translation available.
PIRiA01865. K1HUDE.
A01868. K1HUHU.
A01872. K1HUOU.
A01879. K1HUMV.
A01883. K1HUWK.
A27594.
UniGeneiHs.449609.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DGXmodel-L23-117[»]
1F6LX-ray2.80L23-117[»]
3UPAX-ray1.80A/B23-117[»]
ProteinModelPortaliP01597.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

IMGTiSearch...
Search...

Polymorphism and mutation databases

DMDMi125761.
125764.
125770.
125776.
125779.

Proteomic databases

PeptideAtlasiP01597.
PRIDEiP01597.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000498574; ENSP00000419058; ENSG00000242371.
ENST00000631411; ENSP00000488680; ENSG00000282120.

Organism-specific databases

HGNCiHGNC:5740. IGKV1-39.
OpenTargetsiENSG00000242371.
ENSG00000251546.
ENSG00000282120.
GenAtlasiSearch...

Phylogenomic databases

HOVERGENiHBG018013.
OMAiQAGHTLC.
PhylomeDBiP01597.

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-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-983695. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.

Miscellaneous databases

EvolutionaryTraceiP01600.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
[Graphical view]
PfamiPF07686. V-set. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
SM00406. IGv. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiKV139_HUMAN
AccessioniPrimary (citable) accession number: P01597
Secondary accession number(s): A0A0B4J1Z7
, A0A0C4DH57, A0A0U1RVJ5, P01600, P01606, P01612, P04431
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 2, 2016
Last modified: November 30, 2016
This is version 92 of the entry and version 2 of the sequence. [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

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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.