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Protein

Ig lambda-2 chain C regions

Gene

IGLC2

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

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Bence-Jones protein

Enzyme and pathway databases

BioCyciZFISH:G66-33682-MONOMER.
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-2 chain C regions
Gene namesi
Name:IGLC2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:5856. IGLC2.

Subcellular locationi

GO - Cellular componenti

  • blood microparticle Source: UniProtKB
  • external side of plasma membrane Source: GO_Central
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
  • immunoglobulin complex, circulating Source: GO_Central
  • plasma membrane Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Polymorphism and mutation databases

DMDMi298351714.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000394665‹1 – 106Ig lambda-2 chain C regionsAdd BLAST›106

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi28 ↔ 87PROSITE-ProRule annotation1 Publication
Disulfide bondi105Interchain (with heavy chain)PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiP0CG05.
PaxDbiP0CG05.
PeptideAtlasiP0CG05.
PRIDEiP0CG05.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

IntActiP0CG05. 2 interactors.
STRINGi9606.ENSP00000431254.

Structurei

Secondary structure

1106
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 12Combined sources5
Helixi16 – 20Combined sources5
Beta strandi24 – 36Combined sources13
Beta strandi39 – 44Combined sources6
Beta strandi47 – 49Combined sources3
Beta strandi53 – 55Combined sources3
Beta strandi62 – 64Combined sources3
Beta strandi66 – 74Combined sources9
Helixi76 – 81Combined sources6
Beta strandi85 – 91Combined sources7
Beta strandi94 – 100Combined sources7
Helixi102 – 104Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JVKX-ray1.94B1-105[»]
1LILX-ray2.65A/B1-106[»]
1ZVOX-ray-A/B2-106[»]
2JB5X-ray2.80L1-104[»]
2JB6X-ray2.85A/L1-104[»]
3C2AX-ray2.10L/M2-105[»]
3TV3X-ray1.29L1-106[»]
3TWCX-ray1.65L1-106[»]
3TYGX-ray3.25L1-106[»]
4EOWX-ray1.97L1-106[»]
4LLDX-ray1.19B1-105[»]
4LLMX-ray1.75B1-105[»]
4LLQX-ray1.42B1-105[»]
4LLUX-ray2.16B/D1-105[»]
4LLWX-ray1.95B/D1-105[»]
4LLYX-ray1.60B/D1-105[»]
4O58X-ray2.75L1-106[»]
4O5IX-ray6.50N/P/R/T/V/X1-106[»]
5IQ7X-ray3.29L1-104[»]
5IQ9X-ray2.40B/L1-102[»]
ProteinModelPortaliP0CG05.
SMRiP0CG05.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0CG05.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini7 – 101Ig-likeAdd BLAST95

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin C region, Immunoglobulin domain

Phylogenomic databases

eggNOGiENOG410J0XA. Eukaryota.
ENOG410YZ00. LUCA.
InParanoidiP0CG05.
PhylomeDBiP0CG05.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR003597. Ig_C1-set.
[Graphical view]
PfamiPF07654. C1-set. 1 hit.
[Graphical view]
SMARTiSM00407. IGc1. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
PS00290. IG_MHC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0CG05-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
GQPKAAPSVT LFPPSSEELQ ANKATLVCLI SDFYPGAVTV AWKADSSPVK
60 70 80 90 100
AGVETTTPSK QSNNKYAASS YLSLTPEQWK SHRSYSCQVT HEGSTVEKTV

APTECS
Length:106
Mass (Da):11,294
Last modified:June 15, 2010 - v1
Checksum:iE5DB72BBE65F4577
GO

Sequence cautioni

The sequence AAA59107 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAA20015 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAA20026 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAA20028 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAA36049 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAB38569 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence EAW59547 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence EAW59549 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J00253 Genomic DNA. Translation: AAA59107.1. Different initiation.
X51754 Genomic DNA. Translation: CAB38569.1. Different initiation.
X51755 Genomic DNA. Translation: CAA36049.1. Different initiation.
D87017 Genomic DNA. Translation: BAA20015.1. Different initiation.
D87023 Genomic DNA. Translation: BAA20026.1. Different initiation.
D87023 Genomic DNA. Translation: BAA20028.1. Different initiation.
CH471095 Genomic DNA. Translation: EAW59547.1. Different initiation.
CH471095 Genomic DNA. Translation: EAW59549.1. Different initiation.
PIRiA92057. L2HU.

Cross-referencesi

Web resourcesi

IMGT/GENE-DB

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J00253 Genomic DNA. Translation: AAA59107.1. Different initiation.
X51754 Genomic DNA. Translation: CAB38569.1. Different initiation.
X51755 Genomic DNA. Translation: CAA36049.1. Different initiation.
D87017 Genomic DNA. Translation: BAA20015.1. Different initiation.
D87023 Genomic DNA. Translation: BAA20026.1. Different initiation.
D87023 Genomic DNA. Translation: BAA20028.1. Different initiation.
CH471095 Genomic DNA. Translation: EAW59547.1. Different initiation.
CH471095 Genomic DNA. Translation: EAW59549.1. Different initiation.
PIRiA92057. L2HU.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JVKX-ray1.94B1-105[»]
1LILX-ray2.65A/B1-106[»]
1ZVOX-ray-A/B2-106[»]
2JB5X-ray2.80L1-104[»]
2JB6X-ray2.85A/L1-104[»]
3C2AX-ray2.10L/M2-105[»]
3TV3X-ray1.29L1-106[»]
3TWCX-ray1.65L1-106[»]
3TYGX-ray3.25L1-106[»]
4EOWX-ray1.97L1-106[»]
4LLDX-ray1.19B1-105[»]
4LLMX-ray1.75B1-105[»]
4LLQX-ray1.42B1-105[»]
4LLUX-ray2.16B/D1-105[»]
4LLWX-ray1.95B/D1-105[»]
4LLYX-ray1.60B/D1-105[»]
4O58X-ray2.75L1-106[»]
4O5IX-ray6.50N/P/R/T/V/X1-106[»]
5IQ7X-ray3.29L1-104[»]
5IQ9X-ray2.40B/L1-102[»]
ProteinModelPortaliP0CG05.
SMRiP0CG05.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP0CG05. 2 interactors.
STRINGi9606.ENSP00000431254.

Protein family/group databases

IMGTiSearch...
Search...
Search...
Search...
Search...
Search...
Search...
Search...

Polymorphism and mutation databases

DMDMi298351714.

Proteomic databases

MaxQBiP0CG05.
PaxDbiP0CG05.
PeptideAtlasiP0CG05.
PRIDEiP0CG05.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

GeneCardsiIGLC2.
H-InvDBHIX0016285.
HIX0197173.
HGNCiHGNC:5856. IGLC2.
neXtProtiNX_P0CG05.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410J0XA. Eukaryota.
ENOG410YZ00. LUCA.
InParanoidiP0CG05.
PhylomeDBiP0CG05.

Enzyme and pathway databases

BioCyciZFISH:G66-33682-MONOMER.
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

EvolutionaryTraceiP0CG05.
PROiP0CG05.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR003597. Ig_C1-set.
[Graphical view]
PfamiPF07654. C1-set. 1 hit.
[Graphical view]
SMARTiSM00407. IGc1. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
PS00290. IG_MHC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLAC2_HUMAN
AccessioniPrimary (citable) accession number: P0CG05
Secondary accession number(s): A0M8Q4, P80423
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: June 15, 2010
Last modified: November 2, 2016
This is version 56 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

Displays the following serological isotype: Mcg-, Kern- and Oz-. The Mcg- isotype marker is characterized by Ala-6, Ser-8 and Thr-57; the Ke- marker by Ser-46 and the Oz- marker by Arg-83.

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.