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P01860

- IGHG3_HUMAN

UniProt

P01860 - IGHG3_HUMAN

Protein

Ig gamma-3 chain C region

Gene

IGHG3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 2 (01 Jul 2008)
      Previous versions | rss
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    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-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
    4. innate immune response Source: Reactome
    5. retina homeostasis Source: UniProt

    Enzyme and pathway databases

    ReactomeiREACT_160086. Regulation of actin dynamics for phagocytic cup formation.
    REACT_160158. Role of phospholipids in phagocytosis.
    REACT_160274. FCGR activation.
    REACT_7956. Classical antibody-mediated complement activation.
    REACT_8024. Initial triggering of complement.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ig gamma-3 chain C region
    Alternative name(s):
    HDC
    Heavy chain disease protein
    Gene namesi
    Name:IGHG3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Unplaced

    Organism-specific databases

    HGNCiHGNC:5527. IGHG3.

    Subcellular locationi

    GO - Cellular componenti

    1. blood microparticle Source: UniProt
    2. extracellular region Source: Reactome
    3. extracellular space Source: UniProt

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 377377Ig gamma-3 chain C regionPRO_0000153580Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi27 ↔ 83
    Disulfide bondi111 – 111Interchain (with heavy chain dimer)
    Disulfide bondi114 – 114Interchain (with heavy chain dimer)
    Disulfide bondi120 – 120Interchain (with heavy chain dimer)
    Disulfide bondi126 – 126Interchain (with heavy chain dimer)
    Disulfide bondi129 – 129Interchain (with heavy chain dimer)
    Disulfide bondi135 – 135Interchain (with heavy chain dimer)
    Disulfide bondi141 – 141Interchain (with heavy chain dimer)
    Disulfide bondi144 – 144Interchain (with heavy chain dimer)
    Disulfide bondi150 – 150Interchain (with heavy chain dimer)
    Disulfide bondi156 – 156Interchain (with heavy chain dimer)
    Disulfide bondi159 – 159Interchain (with heavy chain dimer)
    Glycosylationi227 – 2271N-linked (GlcNAc...)2 Publications
    Glycosylationi322 – 3221N-linked (GlcNAc...)1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP01860.
    PRIDEiP01860.

    2D gel databases

    UCD-2DPAGEP01860.

    Expressioni

    Gene expression databases

    GenevestigatoriP01860.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    MINTiMINT-1135282.
    STRINGi9606.ENSP00000374992.

    Structurei

    3D structure databases

    ProteinModelPortaliP01860.
    SMRiP01860. Positions 1-377.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati116 – 13015Add
    BLAST
    Repeati131 – 14515Add
    BLAST
    Repeati146 – 16015Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 9898CH1Add
    BLAST
    Regioni99 – 16062HingeAdd
    BLAST
    Regioni161 – 270110CH2Add
    BLAST
    Regioni271 – 376106CH3Add
    BLAST

    Keywords - Domaini

    Immunoglobulin C region, Immunoglobulin domain, Repeat

    Phylogenomic databases

    eggNOGiNOG313034.
    HOVERGENiHBG005814.
    PhylomeDBiP01860.

    Family and domain databases

    Gene3Di2.60.40.10. 3 hits.
    InterProiIPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003006. Ig/MHC_CS.
    IPR003597. Ig_C1-set.
    [Graphical view]
    PfamiPF07654. C1-set. 3 hits.
    [Graphical view]
    SMARTiSM00407. IGc1. 2 hits.
    [Graphical view]
    PROSITEiPS50835. IG_LIKE. 3 hits.
    PS00290. IG_MHC. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P01860-1 [UniParc]FASTAAdd to Basket

    « Hide

    ASTKGPSVFP LAPCSRSTSG GTAALGCLVK DYFPEPVTVS WNSGALTSGV    50
    HTFPAVLQSS GLYSLSSVVT VPSSSLGTQT YTCNVNHKPS NTKVDKRVEL 100
    KTPLGDTTHT CPRCPEPKSC DTPPPCPRCP EPKSCDTPPP CPRCPEPKSC 150
    DTPPPCPRCP APELLGGPSV FLFPPKPKDT LMISRTPEVT CVVVDVSHED 200
    PEVQFKWYVD GVEVHNAKTK PREEQYNSTF RVVSVLTVLH QDWLNGKEYK 250
    CKVSNKALPA PIEKTISKTK GQPREPQVYT LPPSREEMTK NQVSLTCLVK 300
    GFYPSDIAVE WESSGQPENN YNTTPPMLDS DGSFFLYSKL TVDKSRWQQG 350
    NIFSCSVMHE ALHNRFTQKS LSLSPGK 377
    Length:377
    Mass (Da):41,287
    Last modified:July 1, 2008 - v2
    Checksum:iFEB7F537953F807F
    GO

    Polymorphismi

    The IGHG3 gene shows a structural polymorphism characterized by different hinge lengths. Variant WIS is lacking most of the V region and all of the CH1 region. It has an extra interchain disulfide bond at position 7 in addition to the 11 normally present in the hinge region. Variant ZUC lacks most of the V region, all of the CH1 region, and part of the hinge. Variant OMM may represent an allelic form or another gamma chain subclass.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1 – 7676Missing in variant WIS.
    VAR_068695Add
    BLAST
    Natural varianti77 – 9822GTQTY…VDKRV → QMQGVNCTVSS in variant WIS.
    VAR_068696Add
    BLAST
    Natural varianti213 – 2131E → Q in variant WIS.
    VAR_068697
    Natural varianti214 – 2141V → B in variant ZUC.
    VAR_003890
    Natural varianti221 – 2211P → L in variant OMM.
    VAR_003891
    Natural varianti224 – 2241E → Q in variant WIS.
    VAR_068698
    Natural varianti226 – 2261Y → F in variant ZUC and WIS.
    VAR_003892
    Natural varianti242 – 2421D → N in variant WIS.
    VAR_068699
    Natural varianti245 – 2451N → D in variant WIS.
    VAR_068700
    Natural varianti269 – 2691T → A in variant OMM.
    VAR_003893
    Natural varianti314 – 3141S → N in variant OMM.
    VAR_003894
    Natural varianti314 – 3141Missing in variant ZUC.
    VAR_003895
    Natural varianti366 – 3661F → Y in variant OMM.
    VAR_003896

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03604 Genomic DNA. Translation: CAA27268.1.
    AL122127 Genomic DNA. No translation available.
    J00231 mRNA. Translation: AAA52805.1. Sequence problems.
    PIRiA23511.
    A90442. G3HUWI.
    UniGeneiHs.510635.

    Polymorphism databases

    DMDMi193806361.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    IMGT/GENE-DB

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03604 Genomic DNA. Translation: CAA27268.1 .
    AL122127 Genomic DNA. No translation available.
    J00231 mRNA. Translation: AAA52805.1 . Sequence problems.
    PIRi A23511.
    A90442. G3HUWI.
    UniGenei Hs.510635.

    3D structure databases

    ProteinModelPortali P01860.
    SMRi P01860. Positions 1-377.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-1135282.
    STRINGi 9606.ENSP00000374992.

    Protein family/group databases

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

    Polymorphism databases

    DMDMi 193806361.

    2D gel databases

    UCD-2DPAGE P01860.

    Proteomic databases

    PaxDbi P01860.
    PRIDEi P01860.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    GeneCardsi GC14M106231.
    HGNCi HGNC:5527. IGHG3.
    MIMi 147120. gene.
    neXtProti NX_P01860.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG313034.
    HOVERGENi HBG005814.
    PhylomeDBi P01860.

    Enzyme and pathway databases

    Reactomei REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
    REACT_160158. Role of phospholipids in phagocytosis.
    REACT_160274. FCGR activation.
    REACT_7956. Classical antibody-mediated complement activation.
    REACT_8024. Initial triggering of complement.

    Miscellaneous databases

    PROi P01860.
    SOURCEi Search...

    Gene expression databases

    Genevestigatori P01860.

    Family and domain databases

    Gene3Di 2.60.40.10. 3 hits.
    InterProi IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003006. Ig/MHC_CS.
    IPR003597. Ig_C1-set.
    [Graphical view ]
    Pfami PF07654. C1-set. 3 hits.
    [Graphical view ]
    SMARTi SM00407. IGc1. 2 hits.
    [Graphical view ]
    PROSITEi PS50835. IG_LIKE. 3 hits.
    PS00290. IG_MHC. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence of a human immunoglobulin gamma 3 heavy chain constant region gene: comparison with the other human C gamma genes."
      Huck S., Fort P., Crawford D.H., Lefranc M.-P., Lefranc G.
      Nucleic Acids Res. 14:1779-1789(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The DNA sequence and analysis of human chromosome 14."
      Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
      , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
      Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "Primary structure of human gamma 3 immunoglobulin deletion mutant: gamma 3 heavy-chain disease protein Wis."
      Frangione B., Rosenwasser E., Prelli F., Franklin E.C.
      Biochemistry 19:4304-4308(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE (VARIANT WIS), SUBUNIT.
    4. "Primary structure of the 'hinge' region of human IgG3. Probable quadruplication of a 15-amino acid residue basic unit."
      Michaelsen T.E., Frangione B., Franklin E.C.
      J. Biol. Chem. 252:883-889(1977) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION TO 146-376 (VARIANT WIS/VARIANT ZUC).
    5. "The amino acid sequence of 'heavy chain disease' protein ZUC. Structure of the Fc fragment of immunoglobulin G3."
      Wolfenstein-Todel C., Frangione B., Prelli F., Franklin E.C.
      Biochem. Biophys. Res. Commun. 71:907-914(1976) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION TO 59-289 (VARIANT WIS/VARIANT ZUC).
    6. "Gamma heavy chain disease in man: cDNA sequence supports partial gene deletion model."
      Alexander A., Steinmetz M., Barritault D., Frangione B., Franklin E.C., Hood L., Buxbaum J.N.
      Proc. Natl. Acad. Sci. U.S.A. 79:3260-3264(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 99-377 (VARIANT OMM).
    7. "Structure of human immunoglobulin gamma genes: implications for evolution of a gene family."
      Takahashi N., Ueda S., Obata M., Nikaido T., Nakai S., Honjo T.
      Cell 29:671-679(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 48-59.
    8. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-227 AND ASN-322.
      Tissue: Plasma.
    9. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-227.
      Tissue: Liver.

    Entry informationi

    Entry nameiIGHG3_HUMAN
    AccessioniPrimary (citable) accession number: P01860
    Secondary accession number(s): A2NU35
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 1, 2008
    Last modified: October 1, 2014
    This is version 128 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

    Miscellaneous

    The hinge region in gamma-3 chains is about 4 times as long as in other gamma chains and contains 3 identical 15-residue segments preceded by a similar 17-residue segment (12-28).

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

    External Data

    Dasty 3