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Protein

Immunoglobulin kappa variable 3-20

Gene

IGKV3-20

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 3-202 Publications
Alternative name(s):
Ig kappa chain V-III region B61 Publication
Ig kappa chain V-III region GOL1 Publication
Ig kappa chain V-III region HAH1 Publication
Ig kappa chain V-III region HIC1 Publication
Ig kappa chain V-III region IARC/BL411 Publication
Ig kappa chain V-III region NG91 Publication
Ig kappa chain V-III region SIE1 Publication
Ig kappa chain V-III region Ti1 Publication
Ig kappa chain V-III region WOL1 Publication
Gene namesi
Name:IGKV3-202 Publications
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:5817. IGKV3-20.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Organism-specific databases

OpenTargetsiENSG00000239951.
ENSG00000282402.

Polymorphism and mutation databases

DMDMi125795.
125797.
125799.
125801.
125803.
125807.
125817.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 204 PublicationsAdd BLAST20
ChainiPRO_000005976221 – 116Immunoglobulin kappa variable 3-204 PublicationsAdd BLAST96

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi43 ↔ 109PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PeptideAtlasiP01619.
PRIDEiP01619.

Expressioni

Gene expression databases

BgeeiENSG00000239951.

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

MINTiMINT-202307.

Structurei

Secondary structure

1116
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
Helixi30 – 32Combined sources3
Beta strandi34 – 39Combined sources6
Beta strandi46 – 50Combined sources5
Turni51 – 53Combined sources3
Beta strandi63 – 68Combined sources6
Beta strandi71 – 78Combined sources8
Helixi81 – 83Combined sources3
Beta strandi85 – 91Combined sources7
Beta strandi93 – 96Combined sources4
Beta strandi98 – 100Combined sources3
Beta strandi103 – 107Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DH5model-L21-116[»]
4LRNX-ray1.89L21-116[»]
4M62X-ray1.80L/M21-116[»]
4M8QX-ray2.89B/L21-116[»]
4OB5X-ray1.70L21-116[»]
4ODXX-ray3.10B/L21-116[»]
ProteinModelPortaliP01619.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini21 – ›116Ig-likePROSITE-ProRule annotationAdd BLAST›96

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni21 – 43Framework-11 PublicationAdd BLAST23
Regioni44 – 55Complementarity-determining-11 PublicationAdd BLAST12
Regioni56 – 70Framework-21 PublicationAdd BLAST15
Regioni71 – 77Complementarity-determining-21 Publication7
Regioni78 – 109Framework-31 PublicationAdd BLAST32
Regioni110 – ›116Complementarity-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

GeneTreeiENSGT00780000121852.
HOVERGENiHBG018013.
OMAiTVIQLEI.
PhylomeDBiP01619.

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.

P01619-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
METPAQLLFL LLLWLPDTTG EIVLTQSPGT LSLSPGERAT LSCRASQSVS
60 70 80 90 100
SSYLAWYQQK PGQAPRLLIY GASSRATGIP DRFSGSGSGT DFTLTISRLE
110
PEDFAVYYCQ QYGSSP
Length:116
Mass (Da):12,557
Last modified:November 2, 2016 - v2
Checksum:iFAC198A8B24553DD
GO

Sequence cautioni

The sequence CAA77316 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 conflicti17 – 19DTT → VPS (PubMed:6419127).Curated3
Sequence conflicti38R → S in CAA77316 (PubMed:2997711).Curated1
Sequence conflicti40T → A AA sequence (PubMed:11946339).Curated1
Sequence conflicti46 – 52SQSVSSS → ALLSSRG AA sequence (PubMed:3086710).Curated7
Sequence conflicti49 – 52VSSS → LSGN AA sequence (PubMed:11946339).Curated4
Sequence conflicti51S → N AA sequence (PubMed:6794615).Curated1
Sequence conflicti51S → N AA sequence (PubMed:5027703).Curated1
Sequence conflicti52 – 53SY → N in CAA77316 (PubMed:2997711).Curated2
Sequence conflicti52S → G AA sequence (PubMed:6794615).Curated1
Sequence conflicti53Y → F AA sequence (PubMed:5027703).Curated1
Sequence conflicti55A → G AA sequence (PubMed:6794615).Curated1
Sequence conflicti61P → R in CAA77316 (PubMed:2997711).Curated1
Sequence conflicti64A → S in CAA77316 (PubMed:2997711).Curated1
Sequence conflicti69I → M AA sequence (PubMed:11946339).Curated1
Sequence conflicti69I → M AA sequence (PubMed:3086710).Curated1
Sequence conflicti70 – 71YG → RD in CAA77316 (PubMed:2997711).Curated2
Sequence conflicti71G → V AA sequence (PubMed:5027703).Curated1
Sequence conflicti72A → V AA sequence (PubMed:11946339).Curated1
Sequence conflicti73S → T (PubMed:6419127).Curated1
Sequence conflicti77T → N in CAA77316 (PubMed:2997711).Curated1
Sequence conflicti87G → A (PubMed:6419127).Curated1
Sequence conflicti90T → A AA sequence (PubMed:11946339).Curated1
Sequence conflicti95T → I in CAA77316 (PubMed:2997711).Curated1
Sequence conflicti102E → D AA sequence (PubMed:6794615).Curated1
Sequence conflicti113G → S in CAA77316 (PubMed:2997711).Curated1
Sequence conflicti114 – 116SSP → NSQ (PubMed:6419127).Curated3
Sequence conflicti114S → T (PubMed:3127527).Curated1
Sequence conflicti114S → T in CAA77316 (PubMed:2997711).Curated1
Sequence conflicti115 – 116SP → LG AA sequence (PubMed:6794615).Curated2
Non-terminal residuei1161

Polymorphismi

There are several alleles. The sequence shown is that of IMGT allele IGKV3-20*01.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z00021 Genomic DNA. Translation: CAA77316.1. Sequence problems.
AC245015 Genomic DNA. No translation available.
PIRiA01891. K3HUB6.
A01892. K3HUSI.
A01893. K3HUGO.
A01894. K3HUNG.
A01895. K3HUTI.
A01896. K3HUWL.
A01899. K3HU41.
C27594.
E30607.
PL0021. K3HUHI.
PL0022. K3HUHA.
UniGeneiHs.449609.
Hs.719895.

Genome annotation databases

EnsembliENST00000492167; ENSP00000418649; ENSG00000239951.
ENST00000632822; ENSP00000487628; ENSG00000282402.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

IMGT/GENE-DB

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z00021 Genomic DNA. Translation: CAA77316.1. Sequence problems.
AC245015 Genomic DNA. No translation available.
PIRiA01891. K3HUB6.
A01892. K3HUSI.
A01893. K3HUGO.
A01894. K3HUNG.
A01895. K3HUTI.
A01896. K3HUWL.
A01899. K3HU41.
C27594.
E30607.
PL0021. K3HUHI.
PL0022. K3HUHA.
UniGeneiHs.449609.
Hs.719895.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DH5model-L21-116[»]
4LRNX-ray1.89L21-116[»]
4M62X-ray1.80L/M21-116[»]
4M8QX-ray2.89B/L21-116[»]
4OB5X-ray1.70L21-116[»]
4ODXX-ray3.10B/L21-116[»]
ProteinModelPortaliP01619.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-202307.

Protein family/group databases

IMGTiSearch...
Search...

Polymorphism and mutation databases

DMDMi125795.
125797.
125799.
125801.
125803.
125807.
125817.

Proteomic databases

PeptideAtlasiP01619.
PRIDEiP01619.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000492167; ENSP00000418649; ENSG00000239951.
ENST00000632822; ENSP00000487628; ENSG00000282402.

Organism-specific databases

GeneCardsiIGKV3-20.
H-InvDBHIX0029811.
HGNCiHGNC:5817. IGKV3-20.
OpenTargetsiENSG00000239951.
ENSG00000282402.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00780000121852.
HOVERGENiHBG018013.
OMAiTVIQLEI.
PhylomeDBiP01619.

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.

Gene expression databases

BgeeiENSG00000239951.

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 nameiKV320_HUMAN
AccessioniPrimary (citable) accession number: P01619
Secondary accession number(s): A0A0B4J1Z6
, P01620, P01621, P01622, P01623, P04206, P06311, P18135, P18136
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 2, 2016
Last modified: November 30, 2016
This is version 88 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.