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Protein

Ig lambda chain V-II region MGC

Gene
N/A
Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Bence-Jones protein

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:
Ig lambda chain V-II region MGC
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

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

Pathology & Biotechi

Polymorphism and mutation databases

DMDMi126559.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – ›111›111Ig lambda chain V-II region MGCPRO_0000059835Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11Pyrrolidone carboxylic acid1 Publication
Disulfide bondi22 ↔ 90PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Proteomic databases

PRIDEiP01709.

Interactioni

Protein-protein interaction databases

MINTiMINT-1504417.

Structurei

Secondary structure

1
111
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 136Combined sources
Beta strandi18 – 236Combined sources
Turni26 – 316Combined sources
Beta strandi35 – 406Combined sources
Beta strandi42 – 443Combined sources
Beta strandi47 – 515Combined sources
Turni52 – 543Combined sources
Beta strandi58 – 603Combined sources
Beta strandi64 – 696Combined sources
Beta strandi72 – 776Combined sources
Helixi82 – 843Combined sources
Beta strandi86 – 938Combined sources
Beta strandi95 – 973Combined sources
Beta strandi99 – 1024Combined sources
Beta strandi105 – 1106Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A8JX-ray2.70H/L2-111[»]
1DCLX-ray2.30A/B2-111[»]
1MCWX-ray3.50M2-111[»]
2MCGX-ray2.001/22-111[»]
3MCGX-ray2.001/22-111[»]
4UNTX-ray2.70A/B/C/D/E/F/G/H1-110[»]
4UNUX-ray0.95A/B1-110[»]
4UNVX-ray1.60A1-110[»]
5ACLX-ray1.49A1-110[»]
5ACMX-ray1.05A/B1-110[»]
ProteinModelPortaliP01709.
SMRiP01709. Positions 2-110.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01709.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 108108Ig-likeAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Immunoglobulin V region

Phylogenomic databases

HOVERGENiHBG018013.
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.

P01709-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
QSALTQPPSA SGSLGQSVTI SCTGTSSDVG GYNYVSWYQQ HAGKAPKVII
60 70 80 90 100
YEVNKRPSGV PDRFSGSKSG NTASLTVSGL QAEDEADYYC SSYEGSDNFV
110
FGTGTKVTVL G
Length:111
Mass (Da):11,558
Last modified:July 21, 1986 - v1
Checksum:i7CC1D6E2FA3377BA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei111 – 1111

Sequence databases

PIRiA90381. L2HUMC.

Cross-referencesi

Sequence databases

PIRiA90381. L2HUMC.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A8JX-ray2.70H/L2-111[»]
1DCLX-ray2.30A/B2-111[»]
1MCWX-ray3.50M2-111[»]
2MCGX-ray2.001/22-111[»]
3MCGX-ray2.001/22-111[»]
4UNTX-ray2.70A/B/C/D/E/F/G/H1-110[»]
4UNUX-ray0.95A/B1-110[»]
4UNVX-ray1.60A1-110[»]
5ACLX-ray1.49A1-110[»]
5ACMX-ray1.05A/B1-110[»]
ProteinModelPortaliP01709.
SMRiP01709. Positions 2-110.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1504417.

Polymorphism and mutation databases

DMDMi126559.

Proteomic databases

PRIDEiP01709.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG018013.
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...

Publicationsi

  1. "Primary structure of the Mcg lambda chain."
    Fett J.W., Deutsch H.F.
    Biochemistry 13:4102-4114(1974) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, PYROGLUTAMATE FORMATION AT GLN-1.
  2. Cited for: LAMBDA CHAIN GENES.
  3. "Rotational allomerism and divergent evolution of domains in immunoglobulin light chains."
    Edmundson A.B., Ely K.R., Abola E.E., Schiffer M., Panagiotopoulos N.
    Biochemistry 14:3953-3961(1975)
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
  4. "Three-dimensional structure of a light chain dimer crystallized in water. Conformational flexibility of a molecule in two crystal forms."
    Ely K.R., Herron J.N., Harker M., Edmundson A.B.
    J. Mol. Biol. 210:601-615(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).

Entry informationi

Entry nameiLV206_HUMAN
AccessioniPrimary (citable) accession number: P01709
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 8, 2016
This is version 117 of the entry and version 1 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

Miscellaneous

This is a Bence-Jones protein.
The MCG-type C region appears to be correlated with a very unusual V-region substitution, 103-Thr above for Gly, suggesting that the V-C joining mechanism is not always random.
The C region of this chain has the Kern+ and Mcg+ markers.

Keywords - Technical termi

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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.