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Protein

Immunoglobulin kappa variable 4-1

Gene

IGKV4-1

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

Functioni

V segment of the variable domain of immunoglobulins light chain that participates to 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: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: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

BioCyciZFISH:ENSG00000153586-MONOMER.
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 4-12 Publications
Alternative name(s):
Ig kappa chain V-IV region B171 Publication
Ig kappa chain V-IV region JI1 Publication
Ig kappa chain V-IV region Len1 Publication
Ig kappa chain V-IV region STH1 Publication
Gene namesi
Name:IGKV4-12 Publications
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:5834. IGKV4-1.

Subcellular locationi

GO - Cellular componenti

  • blood microparticle 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

OpenTargetsiENSG00000211598.

Chemistry databases

DrugBankiDB02325. Isopropyl Alcohol.

Polymorphism and mutation databases

DMDMi125830.
125833.
125834.
1730075.
31340182.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 202 PublicationsAdd BLAST20
ChainiPRO_000001518121 – 121Immunoglobulin kappa variable 4-12 PublicationsAdd BLAST101

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi43 ↔ 114PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PeptideAtlasiP06312.
PRIDEiP06312.

Expressioni

Gene expression databases

BgeeiENSG00000211598.
GenevisibleiP06312. HS.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiP06312. 1 interactor.

Structurei

Secondary structure

1121
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi25 – 27Combined sources3
Beta strandi29 – 33Combined sources5
Beta strandi39 – 47Combined sources9
Turni52 – 55Combined sources4
Beta strandi59 – 64Combined sources6
Beta strandi71 – 75Combined sources5
Turni76 – 78Combined sources3
Beta strandi88 – 93Combined sources6
Beta strandi96 – 103Combined sources8
Helixi106 – 108Combined sources3
Beta strandi110 – 116Combined sources7
Beta strandi118 – 121Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DH6model-L1-114[»]
1EEQX-ray1.50A/B1-114[»]
1EEUX-ray1.60A/B1-114[»]
1EFQX-ray1.60A1-114[»]
1EK3X-ray1.90A/B1-114[»]
1LVEX-ray1.95A1-114[»]
1QACX-ray1.80A/B1-114[»]
2LVEX-ray2.70A1-114[»]
3LVEX-ray2.00A1-114[»]
4LVEX-ray2.30A/B1-114[»]
5LVEX-ray2.00A1-114[»]
ProteinModelPortaliP06312.
SMRiP06312.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01625.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini21 – ›121Ig-likePROSITE-ProRule annotationAdd BLAST›101

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni21 – 43Framework-11 PublicationAdd BLAST23
Regioni44 – 60Complementarity-determining-11 PublicationAdd BLAST17
Regioni61 – 75Framework-21 PublicationAdd BLAST15
Regioni76 – 82Complementarity-determining-21 Publication7
Regioni83 – 114Framework-31 PublicationAdd BLAST32
Regioni115 – 121Complementarity-determining-31 Publication7

Sequence similaritiesi

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

Keywords - Domaini

Immunoglobulin domain, Immunoglobulin V region, Signal

Phylogenomic databases

GeneTreeiENSGT00860000133683.
HOGENOMiHOG000059537.
HOVERGENiHBG018013.
InParanoidiP06312.
OMAiSWASTRE.
PhylomeDBiP06312.
TreeFamiTF352067.

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.

P06312-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVLQTQVFIS LLLWISGAYG DIVMTQSPDS LAVSLGERAT INCKSSQSVL
60 70 80 90 100
YSSNNKNYLA WYQQKPGQPP KLLIYWASTR ESGVPDRFSG SGSGTDFTLT
110 120
ISSLQAEDVA VYYCQQYYST P
Length:121
Mass (Da):13,380
Last modified:January 1, 1988 - v1
Checksum:i9586AD4188D33974
GO

Sequence cautioni

The sequence CAA26733 differs from that shown. Chimeric DNA corresponding to regions V and J of immunoglobulin kappa light chain.Curated
The sequence CAA77317 differs from that shown. Chimeric DNA corresponding to regions V and J of immunoglobulin kappa light chain.Curated
The sequence CAA77318 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti32A → V AA sequence (PubMed:9588180).Curated1
Sequence conflicti44K → R AA sequence (PubMed:9588180).Curated1
Sequence conflicti49V → I in CAA26733 (PubMed:2997713).Curated1
Sequence conflicti54N → D in CAA26733 (PubMed:2997713).Curated1
Sequence conflicti55N → S AA sequence (PubMed:50995).Curated1
Sequence conflicti69P → A AA sequence (PubMed:9588180).Curated1
Sequence conflicti74 – 75IY → FS AA sequence (PubMed:9588180).Curated2
Sequence conflicti102 – 103SS → PG AA sequence (PubMed:9588180).Curated2
Sequence conflicti118 – 120YST → DTI in CAA77317 (PubMed:2997712).Curated3
Sequence conflicti119 – 120ST → NL in CAA26733 (PubMed:2997713).Curated2
Sequence conflicti119 – 120ST → RI AA sequence (PubMed:9588180).Curated2
Non-terminal residuei1211

Polymorphismi

There are several alleles. The sequence shown is that of IMGT allele IGKV4-1*01.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z00022 Genomic DNA. Translation: CAA77317.1. Sequence problems.
Z00023 Genomic DNA. Translation: CAA77318.1. Sequence problems.
X02990 mRNA. Translation: CAA26733.1. Sequence problems.
AC244205 Genomic DNA. No translation available.
PIRiA01902. K4HU.
A01903. K4HULN.
A01904. K4HUJI.
A01905. K4HU17.
PH0869.
S30523.
S34002.
S34003.

Genome annotation databases

EnsembliENST00000390243; ENSP00000374778; ENSG00000211598.
UCSCiuc061lqi.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

IMGT/GENE-DB

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z00022 Genomic DNA. Translation: CAA77317.1. Sequence problems.
Z00023 Genomic DNA. Translation: CAA77318.1. Sequence problems.
X02990 mRNA. Translation: CAA26733.1. Sequence problems.
AC244205 Genomic DNA. No translation available.
PIRiA01902. K4HU.
A01903. K4HULN.
A01904. K4HUJI.
A01905. K4HU17.
PH0869.
S30523.
S34002.
S34003.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DH6model-L1-114[»]
1EEQX-ray1.50A/B1-114[»]
1EEUX-ray1.60A/B1-114[»]
1EFQX-ray1.60A1-114[»]
1EK3X-ray1.90A/B1-114[»]
1LVEX-ray1.95A1-114[»]
1QACX-ray1.80A/B1-114[»]
2LVEX-ray2.70A1-114[»]
3LVEX-ray2.00A1-114[»]
4LVEX-ray2.30A/B1-114[»]
5LVEX-ray2.00A1-114[»]
ProteinModelPortaliP06312.
SMRiP06312.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP06312. 1 interactor.

Chemistry databases

DrugBankiDB02325. Isopropyl Alcohol.

Protein family/group databases

IMGTiSearch...
Search...
Search...
Search...

Polymorphism and mutation databases

DMDMi125830.
125833.
125834.
1730075.
31340182.

Proteomic databases

PeptideAtlasiP06312.
PRIDEiP06312.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000390243; ENSP00000374778; ENSG00000211598.
UCSCiuc061lqi.1. human.

Organism-specific databases

GeneCardsiIGKV4-1.
H-InvDBHIX0029781.
HGNCiHGNC:5834. IGKV4-1.
OpenTargetsiENSG00000211598.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00860000133683.
HOGENOMiHOG000059537.
HOVERGENiHBG018013.
InParanoidiP06312.
OMAiSWASTRE.
PhylomeDBiP06312.
TreeFamiTF352067.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000153586-MONOMER.
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

EvolutionaryTraceiP01625.
PROiP06312.

Gene expression databases

BgeeiENSG00000211598.
GenevisibleiP06312. HS.

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 nameiKV401_HUMAN
AccessioniPrimary (citable) accession number: P06312
Secondary accession number(s): P01625
, P06313, P06314, P83593
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: November 30, 2016
This is version 125 of the entry and version 1 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.