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Protein

Immunoglobulin kappa variable 4-1

Gene

IGKV4-1

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

Functioni

V segment of the variable domain of immunoglobulins light chain that participates to the antigen recognition (PubMed:24600447). 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).4 Publications

Caution

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

GO - Molecular functioni

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

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-DBIGKV4-1

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

EuPathDBiHostDB:ENSG00000211598.2
HGNCiHGNC:5834 IGKV4-1
neXtProtiNX_P06312

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

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
ProteomicsDBi51426
51886
51887
51888
57737

Expressioni

Gene expression databases

BgeeiENSG00000211598
GenevisibleiP06312 HS

Interactioni

Subunit structurei

Immunoglobulins are composed of two identical heavy chains and two identical light chains; disulfide-linked.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 strandi24 – 27Combined sources4
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/B21-121[»]
1EEUX-ray1.60A/B21-121[»]
1EFQX-ray1.60A21-121[»]
1EK3X-ray1.90A/B21-121[»]
1LVEX-ray1.95A21-121[»]
1QACX-ray1.80A/B21-121[»]
2LVEX-ray2.70A21-121[»]
3LVEX-ray2.00A21-121[»]
4LVEX-ray2.30A/B21-121[»]
5LVEX-ray2.00A21-121[»]
ProteinModelPortaliP06312
SMRiP06312
ModBaseiSearch...
MobiDBiSearch...

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

Keywords - Domaini

Immunoglobulin domain, Immunoglobulin V region, Signal

Phylogenomic databases

GeneTreeiENSGT00920000148960
HOGENOMiHOG000059537
HOVERGENiHBG018013
InParanoidiP06312
OMAiRATINCK
PhylomeDBiP06312
TreeFamiTF352067

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
IPR003599 Ig_sub
IPR013106 Ig_V-set
PfamiView protein in Pfam
PF07686 V-set, 1 hit
SMARTiView protein in SMART
SM00409 IG, 1 hit
SM00406 IGv, 1 hit
SUPFAMiSSF48726 SSF48726, 1 hit
PROSITEiView protein in PROSITE
PS50835 IG_LIKE, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiKV401_HUMAN
AccessioniPrimary (citable) accession number: P06312
Secondary accession number(s): P01625
, P06313, P06314, P83593
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: June 20, 2018
This is version 138 of the entry and version 1 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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