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P0CG05

- LAC2_HUMAN

UniProt

P0CG05 - LAC2_HUMAN

Protein

Ig lambda-2 chain C regions

Gene

IGLC2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. Functioni

    GO - Molecular functioni

    1. antigen binding Source: UniProtKB-KW

    GO - Biological processi

    1. complement activation Source: Reactome
    2. complement activation, classical pathway Source: Reactome
    3. Fc-epsilon receptor signaling pathway Source: Reactome
    4. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
    5. innate immune response Source: Reactome
    6. regulation of immune response Source: Reactome

    Keywords - Molecular functioni

    Bence-Jones protein

    Enzyme and pathway databases

    ReactomeiREACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
    REACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
    REACT_160158. Role of phospholipids in phagocytosis.
    REACT_160163. Scavenging of heme from plasma.
    REACT_160274. FCGR activation.
    REACT_163701. FCERI mediated MAPK activation.
    REACT_163769. Role of LAT2/NTAL/LAB on calcium mobilization.
    REACT_163834. FCERI mediated Ca+2 mobilization.
    REACT_163936. Fc epsilon receptor (FCERI) signaling.
    REACT_163994. FCERI mediated NF-kB activation.
    REACT_7956. Classical antibody-mediated complement activation.
    REACT_8024. Initial triggering of complement.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ig lambda-2 chain C regions
    Gene namesi
    Name:IGLC2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Unplaced

    Organism-specific databases

    HGNCiHGNC:5856. IGLC2.

    Subcellular locationi

    GO - Cellular componenti

    1. blood microparticle Source: UniProt
    2. extracellular region Source: Reactome
    3. extracellular space Source: UniProt
    4. extracellular vesicular exosome Source: UniProt
    5. plasma membrane Source: Reactome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini‹1 – 106›106Ig lambda-2 chain C regionsPRO_0000394665Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi28 ↔ 871 PublicationPROSITE-ProRule annotation
    Disulfide bondi105 – 105Interchain (with heavy chain)1 PublicationPROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PRIDEiP0CG05.

    Interactioni

    Protein-protein interaction databases

    IntActiP0CG05. 1 interaction.

    Structurei

    Secondary structure

    1
    106
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi8 – 125
    Helixi16 – 205
    Beta strandi24 – 3613
    Beta strandi39 – 446
    Beta strandi47 – 493
    Beta strandi53 – 553
    Beta strandi62 – 643
    Beta strandi66 – 749
    Helixi76 – 816
    Beta strandi85 – 917
    Beta strandi94 – 1007
    Helixi102 – 1043

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP0CG05.
    SMRiP0CG05. Positions 2-102.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0CG05.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini7 – 10195Ig-likeAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Immunoglobulin C region, Immunoglobulin domain

    Phylogenomic databases

    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]
    PROSITEiPS50835. IG_LIKE. 1 hit.
    PS00290. IG_MHC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0CG05-1 [UniParc]FASTAAdd to Basket

    « Hide

    GQPKAAPSVT LFPPSSEELQ ANKATLVCLI SDFYPGAVTV AWKADSSPVK    50
    AGVETTTPSK QSNNKYAASS YLSLTPEQWK SHRSYSCQVT HEGSTVEKTV 100
    APTECS 106
    Length:106
    Mass (Da):11,294
    Last modified:June 15, 2010 - v1
    Checksum:iE5DB72BBE65F4577
    GO

    Sequence cautioni

    The sequence AAA59107.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAA20015.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAA20026.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAA20028.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence CAA36049.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence CAB38569.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence EAW59547.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence EAW59549.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.

    Polymorphism databases

    DMDMi298351714.

    Cross-referencesi

    Web resourcesi

    IMGT/GENE-DB

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    PIRi A92057. L2HU.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JVK X-ray 1.94 B 1-105 [» ]
    1LIL X-ray 2.65 A/B 1-106 [» ]
    1ZVO X-ray - A/B 2-106 [» ]
    2JB5 X-ray 2.80 L 1-104 [» ]
    2JB6 X-ray 2.85 A/L 1-104 [» ]
    3C2A X-ray 2.10 L/M 2-105 [» ]
    3TV3 X-ray 1.29 L 1-106 [» ]
    3TWC X-ray 1.65 L 1-106 [» ]
    3TYG X-ray 3.25 L 1-106 [» ]
    4EOW X-ray 1.97 L 1-106 [» ]
    4LLD X-ray 1.19 B 1-105 [» ]
    4LLM X-ray 1.75 B 1-105 [» ]
    4LLQ X-ray 1.42 B 1-105 [» ]
    4LLU X-ray 2.16 B/D 1-105 [» ]
    4LLW X-ray 1.95 B/D 1-105 [» ]
    4LLY X-ray 1.60 B/D 1-105 [» ]
    4O58 X-ray 2.75 L 1-106 [» ]
    4O5I X-ray 6.50 N/P/R/T/V/X 1-106 [» ]
    ProteinModelPortali P0CG05.
    SMRi P0CG05. Positions 2-102.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P0CG05. 1 interaction.

    Protein family/group databases

    IMGTi Search...
    Search...
    Search...
    Search...
    Search...
    Search...
    Search...
    Search...

    Polymorphism databases

    DMDMi 298351714.

    Proteomic databases

    PRIDEi P0CG05.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    GeneCardsi GC22P023243.
    H-InvDB HIX0016285.
    HIX0197173.
    HGNCi HGNC:5856. IGLC2.
    neXtProti NX_P0CG05.
    GenAtlasi Search...

    Phylogenomic databases

    PhylomeDBi P0CG05.

    Enzyme and pathway databases

    Reactomei REACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
    REACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
    REACT_160158. Role of phospholipids in phagocytosis.
    REACT_160163. Scavenging of heme from plasma.
    REACT_160274. FCGR activation.
    REACT_163701. FCERI mediated MAPK activation.
    REACT_163769. Role of LAT2/NTAL/LAB on calcium mobilization.
    REACT_163834. FCERI mediated Ca+2 mobilization.
    REACT_163936. Fc epsilon receptor (FCERI) signaling.
    REACT_163994. FCERI mediated NF-kB activation.
    REACT_7956. Classical antibody-mediated complement activation.
    REACT_8024. Initial triggering of complement.

    Miscellaneous databases

    EvolutionaryTracei P0CG05.
    PROi P0CG05.

    Family and domain databases

    Gene3Di 2.60.40.10. 1 hit.
    InterProi IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003006. Ig/MHC_CS.
    IPR003597. Ig_C1-set.
    [Graphical view ]
    Pfami PF07654. C1-set. 1 hit.
    [Graphical view ]
    SMARTi SM00407. IGc1. 1 hit.
    [Graphical view ]
    PROSITEi PS50835. IG_LIKE. 1 hit.
    PS00290. IG_MHC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Immunoglobulin lambda-chains. The complete amino acid sequence of a Bence-Jones protein."
      Milstein C., Clegg J.B., Jarvis J.M.
      Biochem. J. 110:631-652(1968) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE (BENCE-JONES PROTEIN X), DISULFIDE BONDS.
    2. "The amino acid sequence of a lambda type Bence-Jones protein. 3. The complete amino acid sequence and the location of the disulfide bridges."
      Titani K., Wikler M., Shinoda T., Putnam F.W.
      J. Biol. Chem. 245:2171-2176(1970) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE (BENCE-JONES PROTEIN SH).
    3. "Structural rule of antibodies. Primary structure of a monoclonal immunoglobulin-L-chain of the lambda type, subgroup IV (Bence-Jones-protein Kern). V. The complete amino acid sequence and its genetic interpretation."
      Ponstingl H., Hess M., Hilschmann N.
      Hoppe-Seyler's Z. Physiol. Chem. 352:247-266(1971) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE (BENCE-JONES PROTEIN KERN).
    4. "Clustered arrangement of immunoglobulin lambda constant region genes in man."
      Hieter P.A., Hollis G.F., Korsmeyer S.J., Waldmann T.A., Leder P.
      Nature 294:536-540(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "Comparative studies on the structure of the light chains of human immunoglobulins. IV. Assignment of a subsubgroup."
      Kametani F., Takayasu T., Suzuki S., Shinoda T., Okuyama T., Shimizu A.
      J. Biochem. 93:421-429(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE (BENCE-JONES PROTEIN NIG-64).
    6. "Structure and expression of the human immunoglobulin lambda genes."
      Vasicek T.J., Leder P.
      J. Exp. Med. 172:609-620(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    7. "One-megabase sequence analysis of the human immunoglobulin lambda gene locus."
      Kawasaki K., Minoshima S., Nakato E., Shibuya K., Shintani A., Schmeits J.L., Wang J., Shimizu N.
      Genome Res. 7:250-261(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "Immunoglobulin lambda (IGL) genes of human and mouse."
      Lefranc M.-P., Lefranc G.
      (In) Honjo T., Alt F.W., Neuberger M. (eds.); Molecular Biology of B Cells, pp.37-59, Elsevier Academic Press, London (2004)
      Cited for: SEROLOGICAL ISOTYPE.

    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: October 1, 2014
    This is version 39 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

    External Data

    Dasty 3