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Immunoglobulin lambda variable 6-57



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


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:17576170, PubMed:20176268).4 Publications

GO - Molecular functioni

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

GO - Biological processi


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


Names & Taxonomyi

Protein namesi
Recommended name:
Immunoglobulin lambda variable 6-572 Publications
Alternative name(s):
Ig lambda chain V-VI region AR1 Publication
Ig lambda chain V-VI region EB41 Publication
Ig lambda chain V-VI region NIG-481 Publication
Ig lambda chain V-VI region SUT1 Publication
Ig lambda chain V-VI region WLT1 Publication
Gene namesi
Name:IGLV6-572 Publications
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:5927. IGLV6-57.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • plasma membrane Source: Reactome

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Organism-specific databases


Polymorphism and mutation databases


PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 194 PublicationsAdd BLAST19
ChainiPRO_000005985020 – 117Immunoglobulin lambda variable 6-574 PublicationsAdd BLAST98

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi41 ↔ 110PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases



Subunit structurei

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


Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi27 – 31Combined sources5
Beta strandi37 – 46Combined sources10
Helixi48 – 50Combined sources3
Beta strandi54 – 58Combined sources5
Beta strandi65 – 69Combined sources5
Turni70 – 72Combined sources3
Beta strandi82 – 87Combined sources6
Turni88 – 91Combined sources4
Beta strandi92 – 97Combined sources6
Helixi102 – 104Combined sources3
Beta strandi106 – 114Combined sources9

3D structure databases

Select the link destinations:
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini20 – ›117Ig-likePROSITE-ProRule annotationAdd BLAST›98


Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni20 – 41Framework-11 PublicationAdd BLAST22
Regioni42 – 54Complementarity-determining-11 PublicationAdd BLAST13
Regioni55 – 69Framework-21 PublicationAdd BLAST15
Regioni70 – 76Complementarity-determining-21 Publication7
Regioni77 – 110Framework-31 PublicationAdd BLAST34
Regioni111 – ›117Complementarity-determining-31 Publication›7

Keywords - Domaini

Immunoglobulin domain, Immunoglobulin V region, Signal

Phylogenomic databases


Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiView protein in InterPro
IPR007110. Ig-like_dom.
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.


Sequence statusi: Complete.

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

P01721-1 [UniParc]FASTAAdd to basket

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60 70 80 90 100
Mass (Da):12,566
Last modified:November 2, 2016 - v2

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti16 – 17GS → DC (PubMed:3923440).Curated2
Sequence conflicti20N → D AA sequence (PubMed:6797401).Curated1
Sequence conflicti20N → D AA sequence (Ref. 6) Curated1
Sequence conflicti21F → L AA sequence (PubMed:118171).Curated1
Sequence conflicti24T → I AA sequence (PubMed:118171).Curated1
Sequence conflicti27H → L AA sequence (PubMed:4089539).Curated1
Sequence conflicti27H → P AA sequence (PubMed:118171).Curated1
Sequence conflicti31E → G AA sequence (PubMed:4089539).Curated1
Sequence conflicti34G → E AA sequence (PubMed:4089539).Curated1
Sequence conflicti38T → I AA sequence (Ref. 6) Curated1
Sequence conflicti39I → F AA sequence (PubMed:6797401).Curated1
Sequence conflicti39I → M AA sequence (PubMed:118171).Curated1
Sequence conflicti43 – 47GSSGS → RSDGT AA sequence (Ref. 6) Curated5
Sequence conflicti43 – 46GSSG → RTSD AA sequence (PubMed:118171).Curated4
Sequence conflicti44S → N (PubMed:3923440).Curated1
Sequence conflicti45S → G AA sequence (PubMed:6797401).Curated1
Sequence conflicti49A → G AA sequence (PubMed:4089539).Curated1
Sequence conflicti50 – 52SNY → DSF AA sequence (PubMed:6797401).Curated3
Sequence conflicti50 – 51SN → GY AA sequence (Ref. 6) Curated2
Sequence conflicti57Q → R AA sequence (PubMed:118171).Curated1
Sequence conflicti60 – 61PG → RV (PubMed:3923440).Curated2
Sequence conflicti62S → G AA sequence (PubMed:118171).Curated1
Sequence conflicti62S → R AA sequence (Ref. 6) Curated1
Sequence conflicti66T → I (PubMed:3923440).Curated1
Sequence conflicti66T → N AA sequence (PubMed:4089539).Curated1
Sequence conflicti67V → L AA sequence (PubMed:118171).Curated1
Sequence conflicti69Y → F AA sequence (Ref. 6) Curated1
Sequence conflicti70E → D AA sequence (PubMed:6797401).Curated1
Sequence conflicti70E → D AA sequence (PubMed:118171).Curated1
Sequence conflicti71D → N AA sequence (PubMed:4089539).Curated1
Sequence conflicti71D → T AA sequence (PubMed:118171).Curated1
Sequence conflicti72N → T AA sequence (Ref. 6) Curated1
Sequence conflicti76S → L (PubMed:3923440).Curated1
Sequence conflicti77G → E AA sequence (PubMed:4089539).Curated1
Sequence conflicti80D → N AA sequence (PubMed:118171).Curated1
Sequence conflicti86I → F AA sequence (PubMed:118171).Curated1
Sequence conflicti88 – 90SSS → DSA AA sequence (PubMed:6797401).Curated3
Sequence conflicti88S → R AA sequence (Ref. 6) Curated1
Sequence conflicti101 – 109KTEDEADYY → TNDDTAMYF AA sequence (PubMed:118171).Curated9
Sequence conflicti101K → Q AA sequence (Ref. 6) Curated1
Sequence conflicti113 – 116YDSS → FDNT (PubMed:3923440).Curated4
Sequence conflicti114 – 117DSSN → NSNH AA sequence (PubMed:6797401).Curated4
Sequence conflicti115 – 117SSN → NNN AA sequence (PubMed:4089539).Curated3
Sequence conflicti115 – 117SSN → RDH AA sequence (Ref. 6) Curated3
Non-terminal residuei1171


There are several alleles. The sequence shown is that of IMGT allele IGLV6-57*01.

Sequence databases

Select the link destinations:
Links Updated
AC245060 Genomic DNA. No translation available.
PIRiA01987. L6HUAR.
A01988. L6HUST.
A01989. L6HULT.
A01990. L6HUEB.
A01991. L6HU48.

Genome annotation databases

EnsembliENST00000390285; ENSP00000374820; ENSG00000211640.

Keywords - Coding sequence diversityi


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.

Entry informationi

Entry nameiLV657_HUMAN
AccessioniPrimary (citable) accession number: P01721
Secondary accession number(s): A0A075B6I2
, P01722, P06317, P06318, P06319
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 2, 2016
Last modified: July 5, 2017
This is version 95 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.



For an example of a full length immunoglobulin lambda light chain see AC P0DOX8.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome


  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references