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Protein

Immunoglobulin lambda variable 2-8

Gene

IGLV2-8

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:17576170, PubMed:20176268).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 lambda variable 2-82 Publications
Alternative name(s):
Ig lambda chain V-II region BO1 Publication
Ig lambda chain V-II region MGC1 Publication
Gene namesi
Name:IGLV2-82 Publications
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:5895. IGLV2-8.

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: UniProtKB
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Polymorphism and mutation databases

DMDMi126559.
126560.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 192 PublicationsAdd BLAST19
ChainiPRO_000005983520 – 118Immunoglobulin lambda variable 2-82 PublicationsAdd BLAST99

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei20Pyrrolidone carboxylic acid2 Publications1
Disulfide bondi41 ↔ 109PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Proteomic databases

PeptideAtlasiP01709.
PRIDEiP01709.

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-1504417.

Structurei

Secondary structure

1118
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 13Combined sources6
Beta strandi18 – 23Combined sources6
Turni26 – 31Combined sources6
Beta strandi35 – 40Combined sources6
Beta strandi42 – 44Combined sources3
Beta strandi47 – 51Combined sources5
Turni52 – 54Combined sources3
Beta strandi58 – 60Combined sources3
Beta strandi64 – 69Combined sources6
Beta strandi72 – 77Combined sources6
Helixi82 – 84Combined sources3
Beta strandi86 – 93Combined sources8
Beta strandi95 – 97Combined sources3
Beta strandi99 – 102Combined sources4
Beta strandi105 – 110Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A8JX-ray2.70H/L21-118[»]
1DCLX-ray2.30A/B21-118[»]
1MCWX-ray3.50M21-118[»]
2MCGX-ray2.001/221-118[»]
3MCGX-ray2.001/221-118[»]
4UNTX-ray2.70A/B/C/D/E/F/G/H20-118[»]
4UNUX-ray0.95A/B20-118[»]
4UNVX-ray1.60A20-118[»]
5ACLX-ray1.49A20-118[»]
5ACMX-ray1.05A/B20-118[»]
ProteinModelPortaliP01709.
SMRiP01709.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01709.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini20 – ›118Ig-likePROSITE-ProRule annotationAdd BLAST›99

Sequence similaritiesi

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

Keywords - Domaini

Immunoglobulin domain, Immunoglobulin V region, Signal

Phylogenomic databases

HOVERGENiHBG018013.
OMAiICMEVPP.
PhylomeDBiP01709.

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.

P01709-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAWALLLLTL LTQGTGSWAQ SALTQPPSAS GSPGQSVTIS CTGTSSDVGG
60 70 80 90 100
YNYVSWYQQH PGKAPKLMIY EVSKRPSGVP DRFSGSKSGN TASLTVSGLQ
110
AEDEADYYCS SYAGSNNF
Length:118
Mass (Da):12,382
Last modified:November 2, 2016 - v2
Checksum:iB94EEE11F9DA8260
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti33P → L AA sequence (PubMed:4415202).Curated1
Sequence conflicti50 – 52GYN → DNK AA sequence (PubMed:5532228).Curated3
Sequence conflicti61P → A AA sequence (PubMed:4415202).Curated1
Sequence conflicti63K → R AA sequence (PubMed:5532228).Curated1
Sequence conflicti67 – 68LM → VI AA sequence (PubMed:4415202).Curated2
Sequence conflicti68 – 70MIY → VIF AA sequence (PubMed:5532228).Curated3
Sequence conflicti73S → N AA sequence (PubMed:4415202).Curated1
Sequence conflicti74K → Q AA sequence (PubMed:5532228).Curated1
Sequence conflicti89G → D AA sequence (PubMed:5532228).Curated1
Sequence conflicti100Q → R AA sequence (PubMed:5532228).Curated1
Sequence conflicti113 – 115AGS → VDN AA sequence (PubMed:5532228).Curated3
Sequence conflicti113A → E AA sequence (PubMed:4415202).Curated1
Sequence conflicti116N → D AA sequence (PubMed:4415202).Curated1
Non-terminal residuei1181

Polymorphismi

There are several alleles. The sequence shown is that of IMGT allele IGLV2-8*01.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC245028 Genomic DNA. No translation available.
PIRiA01976. L2HUBO.
A90381. L2HUMC.

Genome annotation databases

EnsembliENST00000620395; ENSP00000482937; ENSG00000278196.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

IMGT/GENE-DB

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC245028 Genomic DNA. No translation available.
PIRiA01976. L2HUBO.
A90381. L2HUMC.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A8JX-ray2.70H/L21-118[»]
1DCLX-ray2.30A/B21-118[»]
1MCWX-ray3.50M21-118[»]
2MCGX-ray2.001/221-118[»]
3MCGX-ray2.001/221-118[»]
4UNTX-ray2.70A/B/C/D/E/F/G/H20-118[»]
4UNUX-ray0.95A/B20-118[»]
4UNVX-ray1.60A20-118[»]
5ACLX-ray1.49A20-118[»]
5ACMX-ray1.05A/B20-118[»]
ProteinModelPortaliP01709.
SMRiP01709.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1504417.

Protein family/group databases

IMGTiSearch...

Polymorphism and mutation databases

DMDMi126559.
126560.

Proteomic databases

PeptideAtlasiP01709.
PRIDEiP01709.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000620395; ENSP00000482937; ENSG00000278196.

Organism-specific databases

HGNCiHGNC:5895. IGLV2-8.
GenAtlasiSearch...

Phylogenomic databases

HOVERGENiHBG018013.
OMAiICMEVPP.
PhylomeDBiP01709.

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.

Miscellaneous databases

EvolutionaryTraceiP01709.

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 nameiLV208_HUMAN
AccessioniPrimary (citable) accession number: P01709
Secondary accession number(s): A0A087WZW9, P01710
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 2, 2016
Last modified: November 30, 2016
This is version 121 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 22
    Human chromosome 22: 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.