Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Immunoglobulin lambda variable 3-1

Gene

IGLV3-1

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:17576170, PubMed:20176268).4 Publications

Caution

For an example of a full-length immunoglobulin lambda light chain see AC P0DOX8.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-DBIGLV3-1

Names & Taxonomyi

Protein namesi
Recommended name:
Immunoglobulin lambda variable 3-12 Publications
Alternative name(s):
Ig lambda chain V-IV region Bau1 Publication
Ig lambda chain V-IV region MOL1 Publication
Ig lambda chain V-IV region X1 Publication
Gene namesi
Name:IGLV3-12 Publications
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

EuPathDBiHostDB:ENSG00000211673.2
HGNCiHGNC:5896 IGLV3-1
neXtProtiNX_P01715

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

OpenTargetsiENSG00000211673

Polymorphism and mutation databases

DMDMi126566
126567
126570

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 203 PublicationsAdd BLAST20
ChainiPRO_000005984421 – 115Immunoglobulin lambda variable 3-13 PublicationsAdd BLAST95

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi41 ↔ 106PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PeptideAtlasiP01715
PRIDEiP01715
ProteomicsDBi51443
51444
51943

Expressioni

Gene expression databases

BgeeiENSG00000211673 Expressed in 83 organ(s), highest expression level in adrenal gland

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliP01715
SMRiP01715
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini21 – ›115Ig-likePROSITE-ProRule annotationAdd BLAST›95

Keywords - Domaini

Immunoglobulin domain, Immunoglobulin V region, Signal

Phylogenomic databases

GeneTreeiENSGT00900000140816
HOVERGENiHBG018013
OMAiMARITCR
PhylomeDBiP01715

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.

P01715-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAWIPLFLGV LAYCTGSVAS YELTQPPSVS VSPGQTASIT CSGDKLGDKY
60 70 80 90 100
ACWYQQKPGQ SPVLVIYQDS KRPSGIPERF SGSNSGNTAT LTISGTQAMD
110
EADYYCQAWD SSTAH
Length:115
Mass (Da):12,296
Last modified:November 2, 2016 - v2
Checksum:i04ECCC92731F7847
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti22E → D AA sequence (PubMed:4883841).Curated1
Sequence conflicti22E → G AA sequence (PubMed:4435717).Curated1
Sequence conflicti29V → L AA sequence (PubMed:4435717).Curated1
Sequence conflicti38 – 40SIT → TIS AA sequence (PubMed:3103603).Curated3
Sequence conflicti48 – 52DKYAC → ESYYD AA sequence (PubMed:3103603).Curated5
Sequence conflicti48 – 51DKYA → EQYV AA sequence (PubMed:4435717).Curated4
Sequence conflicti50 – 51YA → DV AA sequence (PubMed:4883841).Curated2
Sequence conflicti57K → R AA sequence (PubMed:4883841).Curated1
Sequence conflicti57K → S AA sequence (PubMed:3103603).Curated1
Sequence conflicti63V → L AA sequence (PubMed:3103603).Curated1
Sequence conflicti68 – 70QDS → EGD AA sequence (PubMed:3103603).Curated3
Sequence conflicti68Q → H AA sequence (PubMed:4435717).Curated1
Sequence conflicti70 – 73SKRP → NQRS AA sequence (PubMed:4883841).Curated4
Sequence conflicti87N → T AA sequence (PubMed:4435717).Curated1
Sequence conflicti97 – 98QA → ES AA sequence (PubMed:3103603).Curated2
Sequence conflicti110D → N AA sequence (PubMed:3103603).Curated1
Sequence conflicti112 – 115STAH → MSVV AA sequence (PubMed:4883841).Curated4
Sequence conflicti112 – 115STAH → YTVI AA sequence (PubMed:4435717).Curated4
Sequence conflicti113 – 115TAH → SVL AA sequence (PubMed:3103603).Curated3
Non-terminal residuei1151

Polymorphismi

There are several alleles. The sequence shown is that of IMGT allele IGLV3-1*01.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC245028 Genomic DNA No translation available.
PIRiA01981 L4HUBU
A01982 L4HUX
A26019 L4HUML

Genome annotation databases

EnsembliENST00000390319; ENSP00000374854; ENSG00000211673

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiLV301_HUMAN
AccessioniPrimary (citable) accession number: P01715
Secondary accession number(s): A0A075B6K7, P01716, P06889
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 2, 2016
Last modified: September 12, 2018
This is version 111 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

Complete proteome, Direct protein sequencing, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again