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Protein

Immunoglobulin lambda variable 6-57

Gene

IGLV6-57

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 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
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:5927. IGLV6-57.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Polymorphism and mutation databases

DMDMi126572.
126573.
126574.
126575.
126576.

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

PeptideAtlasiP01721.
PRIDEiP01721.

Interactioni

Subunit structurei

Immunoglobulins are composed of two identical heavy chains and two identical light chains, linked by disulfide bonds.1 Publication

Structurei

Secondary structure

1117
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 12Combined sources5
Beta strandi18 – 27Combined sources10
Helixi29 – 31Combined sources3
Beta strandi35 – 39Combined sources5
Beta strandi46 – 50Combined sources5
Turni51 – 53Combined sources3
Beta strandi63 – 68Combined sources6
Turni69 – 72Combined sources4
Beta strandi73 – 78Combined sources6
Helixi83 – 85Combined sources3
Beta strandi87 – 95Combined sources9
Beta strandi100 – 102Combined sources3
Beta strandi106 – 110Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CD0X-ray1.90A/B21-117[»]
1PEWX-ray1.60A/B21-117[»]
2CD0X-ray1.80A/B21-117[»]
ProteinModelPortaliP01721.
SMRiP01721.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06317.

Family & Domainsi

Domains and Repeats

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

Region

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

Sequence similaritiesi

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

Keywords - Domaini

Immunoglobulin domain, Immunoglobulin V region, Signal

Phylogenomic databases

HOVERGENiHBG018013.
OMAiHGEVRQN.
PhylomeDBiP01721.

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.

P01721-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAWAPLLLTL LAHCTGSWAN FMLTQPHSVS ESPGKTVTIS CTGSSGSIAS
60 70 80 90 100
NYVQWYQQRP GSAPTTVIYE DNQRPSGVPD RFSGSIDSSS NSASLTISGL
110
KTEDEADYYC QSYDSSN
Length:117
Mass (Da):12,566
Last modified:November 2, 2016 - v2
Checksum:i1FA030C806D9F49F
GO

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

Polymorphismi

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

Polymorphism

Cross-referencesi

Web resourcesi

IMGT/GENE-DB

Sequence databases

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CD0X-ray1.90A/B21-117[»]
1PEWX-ray1.60A/B21-117[»]
2CD0X-ray1.80A/B21-117[»]
ProteinModelPortaliP01721.
SMRiP01721.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

IMGTiSearch...

Polymorphism and mutation databases

DMDMi126572.
126573.
126574.
126575.
126576.

Proteomic databases

PeptideAtlasiP01721.
PRIDEiP01721.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000390285; ENSP00000374820; ENSG00000211640.

Organism-specific databases

HGNCiHGNC:5927. IGLV6-57.
GenAtlasiSearch...

Phylogenomic databases

HOVERGENiHBG018013.
OMAiHGEVRQN.
PhylomeDBiP01721.

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

EvolutionaryTraceiP06317.

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 nameiLV657_HUMAN
AccessioniPrimary (citable) accession number: P01721
Secondary accession number(s): A0A075B6I2
, P01722, P06317, P06318, P06319
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 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.