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Protein

Ig gamma-3 chain C region

Gene

IGHG3

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...

Enzyme and pathway databases

ReactomeiR-HSA-166663. Initial triggering of complement.
R-HSA-173623. Classical antibody-mediated complement activation.
R-HSA-2029481. FCGR activation.
R-HSA-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-HSA-2029485. Role of phospholipids in phagocytosis.

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
Proteomesi
  • UP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:5527. IGHG3.

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
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Polymorphism and mutation databases

DMDMi193806361.

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

PRIDEiP01860.

2D gel databases

UCD-2DPAGEP01860.

Interactioni

Subunit structurei

Homodimer.1 Publication

GO - Molecular functioni

Protein-protein interaction databases

IntActiP01860. 4 interactions.
MINTiMINT-1135282.

Structurei

Secondary structure

1
377
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi169 – 1735Combined sources
Helixi177 – 1815Combined sources
Beta strandi188 – 1969Combined sources
Beta strandi204 – 2096Combined sources
Beta strandi212 – 2143Combined sources
Beta strandi230 – 2378Combined sources
Helixi240 – 2445Combined sources
Beta strandi249 – 2546Combined sources
Beta strandi262 – 2665Combined sources
Beta strandi277 – 2815Combined sources
Helixi285 – 2895Combined sources
Beta strandi290 – 30516Combined sources
Beta strandi308 – 3136Combined sources
Beta strandi321 – 3233Combined sources
Beta strandi334 – 34310Combined sources
Helixi344 – 3485Combined sources
Beta strandi353 – 3586Combined sources
Helixi363 – 3653Combined sources
Beta strandi366 – 3716Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4WWIX-ray2.31D/E/F168-377[»]
4ZNCX-ray2.28D/E/F168-377[»]
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

HOVERGENiHBG005814.
InParanoidiP01860.
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. 3 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 3 hits.
PROSITEiPS50835. IG_LIKE. 3 hits.
PS00290. IG_MHC. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P01860-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
ASTKGPSVFP LAPCSRSTSG GTAALGCLVK DYFPEPVTVS WNSGALTSGV
60 70 80 90 100
HTFPAVLQSS GLYSLSSVVT VPSSSLGTQT YTCNVNHKPS NTKVDKRVEL
110 120 130 140 150
KTPLGDTTHT CPRCPEPKSC DTPPPCPRCP EPKSCDTPPP CPRCPEPKSC
160 170 180 190 200
DTPPPCPRCP APELLGGPSV FLFPPKPKDT LMISRTPEVT CVVVDVSHED
210 220 230 240 250
PEVQFKWYVD GVEVHNAKTK PREEQYNSTF RVVSVLTVLH QDWLNGKEYK
260 270 280 290 300
CKVSNKALPA PIEKTISKTK GQPREPQVYT LPPSREEMTK NQVSLTCLVK
310 320 330 340 350
GFYPSDIAVE WESSGQPENN YNTTPPMLDS DGSFFLYSKL TVDKSRWQQG
360 370
NIFSCSVMHE ALHNRFTQKS LSLSPGK
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.3 Publications

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 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:
EMBLi
GenBanki
DDBJi
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.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

IMGT/GENE-DB

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4WWIX-ray2.31D/E/F168-377[»]
4ZNCX-ray2.28D/E/F168-377[»]
ProteinModelPortaliP01860.
SMRiP01860. Positions 1-377.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP01860. 4 interactions.
MINTiMINT-1135282.

Protein family/group databases

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

Polymorphism and mutation databases

DMDMi193806361.

2D gel databases

UCD-2DPAGEP01860.

Proteomic databases

PRIDEiP01860.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

GeneCardsiIGHG3.
HGNCiHGNC:5527. IGHG3.
MIMi147120. gene.
neXtProtiNX_P01860.
GenAtlasiSearch...

Phylogenomic databases

HOVERGENiHBG005814.
InParanoidiP01860.
PhylomeDBiP01860.

Enzyme and pathway databases

ReactomeiR-HSA-166663. Initial triggering of complement.
R-HSA-173623. Classical antibody-mediated complement activation.
R-HSA-2029481. FCGR activation.
R-HSA-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-HSA-2029485. Role of phospholipids in phagocytosis.

Miscellaneous databases

PROiP01860.
SOURCEiSearch...

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. 3 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 3 hits.
PROSITEiPS50835. IG_LIKE. 3 hits.
PS00290. IG_MHC. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
  10. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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: May 11, 2016
This is version 142 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

3D-structure, 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
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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.