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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

Organism-specific databases

DisGeNETi3502.

Polymorphism and mutation databases

DMDMi193806361.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001535801 – 377Ig gamma-3 chain C regionAdd BLAST377

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi27 ↔ 83
Disulfide bondi111Interchain (with heavy chain dimer)
Disulfide bondi114Interchain (with heavy chain dimer)
Disulfide bondi120Interchain (with heavy chain dimer)
Disulfide bondi126Interchain (with heavy chain dimer)
Disulfide bondi129Interchain (with heavy chain dimer)
Disulfide bondi135Interchain (with heavy chain dimer)
Disulfide bondi141Interchain (with heavy chain dimer)
Disulfide bondi144Interchain (with heavy chain dimer)
Disulfide bondi150Interchain (with heavy chain dimer)
Disulfide bondi156Interchain (with heavy chain dimer)
Disulfide bondi159Interchain (with heavy chain dimer)
Glycosylationi227N-linked (GlcNAc...)2 Publications1
Glycosylationi322N-linked (GlcNAc...)1 Publication1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiP01860.
MaxQBiP01860.
PeptideAtlasiP01860.
PRIDEiP01860.

2D gel databases

UCD-2DPAGEP01860.

PTM databases

iPTMnetiP01860.
PhosphoSitePlusiP01860.

Interactioni

Subunit structurei

Homodimer.1 Publication

GO - Molecular functioni

Protein-protein interaction databases

IntActiP01860. 4 interactors.
MINTiMINT-1135282.

Structurei

Secondary structure

1377
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi169 – 173Combined sources5
Helixi177 – 181Combined sources5
Beta strandi188 – 196Combined sources9
Beta strandi204 – 209Combined sources6
Beta strandi212 – 214Combined sources3
Beta strandi230 – 237Combined sources8
Helixi240 – 244Combined sources5
Beta strandi249 – 254Combined sources6
Beta strandi262 – 266Combined sources5
Beta strandi277 – 281Combined sources5
Helixi285 – 289Combined sources5
Beta strandi290 – 305Combined sources16
Beta strandi308 – 313Combined sources6
Beta strandi321 – 323Combined sources3
Beta strandi334 – 343Combined sources10
Helixi344 – 348Combined sources5
Beta strandi353 – 358Combined sources6
Helixi363 – 365Combined sources3
Beta strandi366 – 371Combined sources6

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati116 – 130Add BLAST15
Repeati131 – 145Add BLAST15
Repeati146 – 160Add BLAST15

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 98CH1Add BLAST98
Regioni99 – 160HingeAdd BLAST62
Regioni161 – 270CH2Add BLAST110
Regioni271 – 376CH3Add BLAST106

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)DescriptionActionsGraphical viewLength
Natural variantiVAR_0686951 – 76Missing in variant WIS. Add BLAST76
Natural variantiVAR_06869677 – 98GTQTY…VDKRV → QMQGVNCTVSS in variant WIS. Add BLAST22
Natural variantiVAR_068697213E → Q in variant WIS. 1
Natural variantiVAR_003891221P → L in variant OMM. 1
Natural variantiVAR_068698224E → Q in variant WIS. 1
Natural variantiVAR_003892226Y → F in variant ZUC and WIS. 1
Natural variantiVAR_068699242D → N in variant WIS. 1
Natural variantiVAR_068700245N → D in variant WIS. 1
Natural variantiVAR_003893269T → A in variant OMM. 1
Natural variantiVAR_003894314S → N in variant OMM. 1
Natural variantiVAR_003895314Missing in variant ZUC. 1
Natural variantiVAR_003896366F → Y in variant OMM. 1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4WWIX-ray2.31D/E/F168-377[»]
4ZNCX-ray2.28D/E/F168-377[»]
ProteinModelPortaliP01860.
SMRiP01860.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP01860. 4 interactors.
MINTiMINT-1135282.

Protein family/group databases

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

PTM databases

iPTMnetiP01860.
PhosphoSitePlusiP01860.

Polymorphism and mutation databases

DMDMi193806361.

2D gel databases

UCD-2DPAGEP01860.

Proteomic databases

EPDiP01860.
MaxQBiP01860.
PeptideAtlasiP01860.
PRIDEiP01860.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

DisGeNETi3502.
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...

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: November 2, 2016
This is version 147 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.