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Protein

Immunoglobulin kappa variable 1-33

Gene

IGKV1-33

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

Functioni

V region of the variable domain of immunoglobulin light chains that participates in 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: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).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
  • identical protein binding Source: IntAct
  • serine-type endopeptidase activity Source: Reactome

GO - Biological processi

Keywordsi

Molecular functionBence-Jones protein
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-DBIGKV1-33

Names & Taxonomyi

Protein namesi
Recommended name:
Immunoglobulin kappa variable 1-332 Publications
Alternative name(s):
Ig kappa chain V-I region AU1 Publication
Ig kappa chain V-I region Ka1 Publication
Gene namesi
Name:IGKV1-332 Publications
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

EuPathDBiHostDB:ENSG00000239975.2
HostDB:ENSG00000242076.2
HGNCiHGNC:5737 IGKV1-33
neXtProtiNX_P01594

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

Polymorphism and mutation databases

DMDMi125758
125767

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 221 PublicationAdd BLAST22
ChainiPRO_000005973823 – 117Immunoglobulin kappa variable 1-33Sequence analysisAdd BLAST95

Amino acid modifications

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

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP01594

Expressioni

Gene expression databases

BgeeiENSG00000239975

Interactioni

Subunit structurei

Immunoglobulins are composed of two identical heavy chains and two identical light chains; disulfide-linked.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-15853604,EBI-15853604

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

DIPiDIP-58572N

Structurei

Secondary structure

1117
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi26 – 29Combined sources4
Beta strandi31 – 35Combined sources5
Beta strandi41 – 49Combined sources9
Beta strandi55 – 60Combined sources6
Beta strandi66 – 71Combined sources6
Turni72 – 74Combined sources3
Beta strandi84 – 89Combined sources6
Beta strandi92 – 99Combined sources8
Helixi102 – 104Combined sources3
Beta strandi106 – 112Combined sources7
Beta strandi114 – 117Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B0WX-ray1.80A/B/C23-117[»]
1JV5X-ray2.20A23-117[»]
1QP1X-ray2.06A/B/C23-117[»]
2Q20X-ray1.30A/B23-117[»]
3CDCX-ray1.53A/B23-117[»]
3CDFX-ray1.53A/B/C/D/E/F23-117[»]
3CDYX-ray2.43A/B23-117[»]
4K07X-ray2.83A/B/C/D/E/F/G/H/I/J20-117[»]
ProteinModelPortaliP01594
SMRiP01594
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01594

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-1Add BLAST23
Regioni46 – 56Complementarity-determining-1Add BLAST11
Regioni57 – 71Framework-2Add BLAST15
Regioni72 – 78Complementarity-determining-27
Regioni79 – 110Framework-3Add BLAST32
Regioni111 – ›117Complementarity-determining-3›7

Keywords - Domaini

Immunoglobulin domain, Immunoglobulin V region, Signal

Phylogenomic databases

GeneTreeiENSGT00910000144069
HOVERGENiHBG018013
OMAiWLPSARC
PhylomeDBiP01594

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.

P01594-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDMRVPAQLL GLLLLWLSGA RCDIQMTQSP SSLSASVGDR VTITCQASQD
60 70 80 90 100
ISNYLNWYQQ KPGKAPKLLI YDASNLETGV PSRFSGSGSG TDFTFTISSL
110
QPEDIATYYC QQYDNLP
Length:117
Mass (Da):12,848
Last modified:November 2, 2016 - v2
Checksum:iEE4F871C54A514FB
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti32S → T AA sequence (PubMed:818073).Curated1
Sequence conflicti35A → V AA sequence (PubMed:818073).Curated1
Sequence conflicti46Q → E AA sequence (PubMed:818073).Curated1
Sequence conflicti50 – 53DISN → TVLS AA sequence (PubMed:818073).Curated4
Sequence conflicti53N → D AA sequence (PubMed:5028201).Curated1
Sequence conflicti72D → A AA sequence (PubMed:818073).Curated1
Sequence conflicti75N → S AA sequence (PubMed:818073).Curated1
Sequence conflicti78T → S AA sequence (PubMed:5028201).Curated1
Sequence conflicti87S → G AA sequence (PubMed:5028201).Curated1
Sequence conflicti87S → Q AA sequence (PubMed:818073).Curated1
Sequence conflicti91 – 92TD → AH AA sequence (PubMed:5028201).Curated2
Sequence conflicti100L → V AA sequence (PubMed:818073).Curated1
Sequence conflicti105I → F AA sequence (PubMed:818073).Curated1
Sequence conflicti114 – 115DN → LD AA sequence (PubMed:818073).Curated2
Sequence conflicti115N → Y AA sequence (PubMed:5028201).Curated1
Non-terminal residuei1171

Polymorphismi

There are several alleles. The sequence shown is that of IMGT allele IGKV1-33*01.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC244255 Genomic DNA No translation available.
PIRiA01869 K1HUKA
A91653 K1HUAU
S42265

Genome annotation databases

EnsembliENST00000473726; ENSP00000420020; ENSG00000242076
ENST00000632835; ENSP00000487732; ENSG00000282811
UCSCiuc061lra.1 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiKV133_HUMAN
AccessioniPrimary (citable) accession number: P01594
Secondary accession number(s): A0A087WZH9, P01603
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 2, 2016
Last modified: May 23, 2018
This is version 122 of the entry and version 2 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

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

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