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6  structures 62  species 4  interactions 67  sequences 2  architectures

Family: IFNGR1 (PF07140)

Summary: Interferon gamma receptor (IFNGR1)

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This is the Wikipedia entry entitled "Interferon gamma receptor (IFNGR1) family". More...

Interferon gamma receptor (IFNGR1) family Edit Wikipedia article

Interferon gamma receptor (IFNGR1)
PDB 1fyh EBI.jpg
1:1 complex between an interferon gamma single-chain variant and its receptor
Identifiers
Symbol IFNGR1
Pfam PF07140
Pfam clan CL0159
InterPro IPR021126
SCOP 1fg9
SUPERFAMILY 1fg9

In molecular biology, the interferon gamma receptor (IFNGR1) family is a family of proteins which includes several eukaryotic and viral interferon gamma receptor proteins.

Members of this family include:

References

  1. ^ Sogabe S, Stuart F, Henke C, Bridges A, Williams G, Birch A, Winkler FK, Robinson JA (November 1997). "Neutralizing epitopes on the extracellular interferon gamma receptor (IFNgammaR) alpha-chain characterized by homolog scanning mutagenesis and X-ray crystal structure of the A6 fab-IFNgammaR1-108 complex". J. Mol. Biol. 273 (4): 882–97. doi:10.1006/jmbi.1997.1336. PMID 9367779. 
  2. ^ Alcami A, Smith GL (March 2002). "The vaccinia virus soluble interferon-gamma receptor is a homodimer". J. Gen. Virol. 83 (Pt 3): 545–9. PMID 11842249. 

This article incorporates text from the public domain Pfam and InterPro IPR021126

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Interferon gamma receptor (IFNGR1) Provide feedback

This family consists of several eukaryotic and viral interferon gamma receptor proteins. Molecular interactions among cytokines and cytokine receptors in eukaryotes form the basis of many cell-signaling pathways relevant to immune function. Human interferon-gamma (IFN-gamma) signals through a multimeric receptor complex consisting of two different but structurally related transmembrane chains: the high-affinity receptor-binding subunit (IFN-gammaRalpha) and a species specific accessory factor (AF-1 or IFN-gammaRbeta). The vaccinia viral interferon gamma receptor has been shown to be secreted from infected cells during early infection [2]. The structure has been halved such that the N-terminus of this family is now represented by Tissue_fac PF01108.

Literature references

  1. Thiel DJ, le Du MH, Walter RL, D'Arcy A, Chene C, Fountoulakis M, Garotta G, Winkler FK, Ealick SE; , Structure Fold Des 2000;8:927-936.: Observation of an unexpected third receptor molecule in the crystal structure of human interferon-gamma receptor complex. PUBMED:10986460 EPMC:10986460

  2. Alcami A, Smith GL; , J Gen Virol. 2002;83:545-549.: The vaccinia virus soluble interferon-gamma receptor is a homodimer. PUBMED:11842249 EPMC:11842249


Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR021126

Interferon (INF)-gamma is a dimeric glycoprotein produced by activated T cells and natural killer cells. Although originally isolated based on its antiviral activity, INF-gamma also displays powerful anti-proliferative and immuno-modulatory activities, which are essential for developing appropriate cellular defences against a variety of infectious agents. The first step in eliciting these responses is the specific high affinity interaction of INF- gamma with its cell-surface receptor (INF-gammaRalpha); the complex then interacts with at least one of a family of additional species-specific accessory factors (AF-1 or INF-gammabeta), which convey different cellular responses. One such response is the association and phosphorylation of two protein tyrosine kinases (Jak-1 and Jak-2), which in turn stimulate nuclear transcription activators [PUBMED:7617032].

  • The human INF-gammaR, is a member of the hematopoietic cytokine receptor superfamily. It is expressed in a membrane-bound form in many cell types, and is over-expressed in tumour cells. It comprises an extracellular portion of 229 residues, a single transmembrane region, and a cytoplasmic domain of 221 residues. As with other members of its superfamily, the cytokine-binding sites are formed by a small set of closely-spaced surface loops that extend from a beta-sheet core, much like antigen-binding sites on antibodies. The extracellular INF-gammaR monomer comprises two domains (domain D1 from residue 14-102, and domain D2 from residue 114-221), each resembling an Ig fold with fibronectin type III topology [PUBMED:9367779].
  • The vaccinia virus interferon (IFN)-gamma receptor (IFN-gammaR) is a 43 kDa soluble glycoprotein that is secreted from infected cells early during infection. IFN-gammaR from vaccinia virus, cowpox virus and camelpox virus exist naturally as homodimers, whereas the cellular IFN-gammaR dimerizes only upon binding the homodimeric IFN-gamma. The existence of the virus protein as a dimer in the absence of ligand may provide an advantage to the virus in efficient binding and inhibition of IFN-gamma in solution [PUBMED:11842249].

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan E-set (CL0159), which has the following description:

This clan includes a diverse range of domains that have an Ig-like fold and appear to be distantly related to each other. The clan includes: PKD domains, cadherins and several families of bacterial Ig-like domains as well as viral tail fibre proteins. it also includes several Fibronectin type III domain-containing families.

The clan contains the following 218 members:

A2M A2M_BRD A2M_recep Adeno_GP19K AlcCBM31 Alpha-amylase_N Alpha_adaptinC2 Alpha_E2_glycop Arch_flagellin Arylsulfotran_N ASF1_hist_chap ATG19_autophagy BACON Big_1 Big_10 Big_11 Big_2 Big_3 Big_3_2 Big_3_3 Big_3_5 Big_4 Big_5 Big_6 Big_7 Big_8 Big_9 Bile_Hydr_Trans BiPBP_C bMG1 bMG10 bMG3 bMG5 bMG6 BslA BsuPI Cadherin Cadherin-like Cadherin_2 Cadherin_3 Cadherin_4 Cadherin_5 Cadherin_pro CagX Calx-beta Candida_ALS_N CARDB CBM39 CBM_X2 CD45 CelD_N Ceramidse_alk_C CHB_HEX_C CHB_HEX_C_1 ChitinaseA_N ChiW_Ig_like CHU_C Coatamer_beta_C COP-gamma_platf CopC Cyc-maltodext_N Cytomega_US3 DsbC DUF11 DUF1410 DUF1425 DUF1929 DUF2271 DUF3244 DUF3327 DUF3416 DUF3458 DUF3501 DUF3823_C DUF3859 DUF3872 DUF4165 DUF4179 DUF4426 DUF4448 DUF4469 DUF4625 DUF4879 DUF4981 DUF4982 DUF5001 DUF5008 DUF5011 DUF5065 DUF5115 DUF525 DUF5643 DUF916 EB_dh ECD EpoR_lig-bind ERAP1_C EstA_Ig_like Filamin FixG_C Flavi_glycop_C FlgD_ig fn3 Fn3-like fn3_2 fn3_4 fn3_5 fn3_6 FN3_7 Fn3_assoc fn3_PAP GBS_Bsp-like Glucodextran_B Glyco_hydro2_C5 Glyco_hydro_2 Glyco_hydro_61 Gmad2 GMP_PDE_delta GPI-anchored Hanta_G1 He_PIG He_PIG_assoc HECW_N HemeBinding_Shp Hemocyanin_C Herpes_BLLF1 HYR IFNGR1 Ig_GlcNase Ig_mannosidase IL12p40_C Il13Ra_Ig IL17R_fnIII_D1 IL17R_fnIII_D2 IL2RB_N1 IL3Ra_N IL4Ra_N IL6Ra-bind Inhibitor_I42 Inhibitor_I71 Integrin_alpha2 Interfer-bind Invasin_D3 IRK_C IrmA Iron_transport LEA_2 Lep_receptor_Ig LIFR_N Lipase_bact_N LPMO_10 LRR_adjacent LTD Mannosidase_ig MG1 MG2 MG3 MG4 Mo-co_dimer N_BRCA1_IG Na_K-ATPase NEAT Neocarzinostat Neurexophilin NPCBM_assoc PapD_C PBP-Tp47_c Peptidase_C25_C Phlebovirus_G2 PhoD_N PKD PKD_2 PKD_3 Pollen_allerg_1 Pox_vIL-18BP Pur_ac_phosph_N Qn_am_d_aII Qn_am_d_aIII RabGGT_insert Reeler REJ RET_CLD1 RET_CLD3 RET_CLD4 RGI_lyase RHD_dimer Rho_GDI Rib SCAB-Ig SKICH SLAM SoxZ SprB SusE SVA SWM_repeat T2SS-T3SS_pil_N Tafi-CsgC TarS_C1 TcA_RBD TcfC TIG TIG_2 TIG_plexin Tissue_fac Top6b_C Transglut_C Transglut_N TRAP_beta Tuberculin UL16 Velvet WIF Wzt_C Y_Y_Y YBD ZirS_C Zona_pellucida

Alignments

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RP75
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NCBI
(367)
Meta
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RP15
(22)
RP35
(33)
RP55
(54)
RP75
(69)
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  Seed
(7)
Full
(67)
Representative proteomes UniProt
(213)
NCBI
(367)
Meta
(0)
RP15
(22)
RP35
(33)
RP55
(54)
RP75
(69)
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Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

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Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Pfam-B_15930 (release 10.0)
Previous IDs: none
Type: Family
Sequence Ontology: SO:0100021
Author: Moxon SJ
Number in seed: 7
Number in full: 67
Average length of the domain: 149.90 aa
Average identity of full alignment: 35 %
Average coverage of the sequence by the domain: 36.53 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 45638612 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.7 20.7
Trusted cut-off 22.5 22.5
Noise cut-off 20.3 19.4
Model length: 133
Family (HMM) version: 11
Download: download the raw HMM for this family

Species distribution

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Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence

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Interactions

There are 4 interactions for this family. More...

IFN-gamma Tissue_fac IFN-gamma IFNGR1

Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the IFNGR1 domain has been found. There are 6 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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