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InterPro: IPR007110 Immunoglobulin-like
Protein matches
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UniProtKB Matches: 23372 proteins |
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Accession
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IPR007110 Ig-like |
Type
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Domain |
Signatures
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InterPro Relationships
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Found in
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IPR000920 Myelin P0 protein
IPR001038 Glycoprotein C/ glycoprotein A
IPR001654 Marek's disease glycoprotein A
IPR003989 Vascular cell adhesion molecule-1
IPR004074 Interleukin-1 receptor, type I/II
IPR004076 Interleukin-1 receptor IL1R
IPR004077 Interleukin-1 receptor, type II
IPR004078 Interleukin-1 binding protein
IPR006704 CD47 integrin associated protein
IPR008056 Tapasin
IPR008096 Cytotoxic T-lymphocyte antigen 4
IPR009134 Tyrosine-protein kinase, vascular endothelial growth factor receptor (VEGFR), N-terminal
IPR009135 Tyrosine-protein kinase, vascular endothelial growth factor receptor 1 (VEGFR1), N-terminal
IPR009136 Tyrosine-protein kinase, vascular endothelial growth factor receptor 2 (VEGFR2)
IPR009137 Tyrosine-protein kinase, vascular endothelial growth factor receptor 3 (VEGFR3), N-terminal
IPR009151 Basigin
IPR011390 Insulin-like growth factor binding protein related protein (IGFBP-rP), MAC25
IPR013270 CD47 immunoglobulin-like
IPR013783 Immunoglobulin-like fold
IPR015468 CD8 alpha subunit
IPR015513 Semaphorin 3E
IPR015528 Interleukin-12 beta chain
IPR015621 Interleukin-1 receptor
IPR015631 Signalling lymphocyte activation molecule
IPR015651 CD86 T cell co-stimulatory antigen
IPR015707 Beta-2-Microglobulin
IPR015725 Myosin light chain kinase
IPR015726 Serine/threonine protein kinase, striated muscle-specific
IPR015775 Tyrosine-protein kinase, receptor Axl-related
IPR015776 Tyrosine-protein kinase, platelet-derived growth factor receptor alpha
IPR015781 Tyrosine-protein kinase, angiopoietin receptor
IPR015924 CD84 immune receptor
IPR016243 Tyrosine-protein kinase, CSF-1/PDGF receptor
IPR016247 Tyrosine-protein kinase, receptor ROR, subgroup
IPR016248 Tyrosine-protein kinase, fibroblast growth factor receptor
IPR016332 Alpha-1B-glycoprotein/leukocyte immunoglobulin-like receptor
IPR016663 Myelin-oligodendrocyte glycoprotein
IPR020426 Tyrosine-protein kinase, neurotrophic receptor, N-terminal region
IPR020446 Tyrosine-protein kinase, neurotrophic receptor, type 3, N-terminal region
IPR020455 Tyrosine-protein kinase, neurotrophic receptor, type 2, N-terminal region
IPR020675 Myosin light chain kinase-related
IPR020678 Nexilin
IPR020682 Obscurin/Myosin light chain kinase
IPR020704 Tyrosine-protein kinase, receptor TYRO3, Zebrafish
IPR020705 Tyrosine-protein kinase, receptor MER
IPR020716 Tyrosine-protein kinase, muscle/skeletal receptor
IPR020718 Tyrosine-protein kinase, PDGF/VEGF receptor, fly
IPR020721 Tyrosine-protein kinase, vascular endothelial growth factor receptor 3 (VEGFR3)
IPR020722 Tyrosine-protein kinase, vascular endothelial growth factor receptor 1 (VEGFR1)
IPR020725 Tyrosine-protein kinase, myoblast growth factor receptor Egl-15
IPR020727 Tyrosine-protein kinase, platelet-derived growth factor receptor beta
IPR020729 Tyrosine-protein kinase, macrophage colony-stimulating factor 1 receptor
IPR020730 Tyrosine-protein kinase, mast/stem cell growth factor receptor
IPR020732 Tyrosine-protein kinase, fibroblast growth factor receptor-related
IPR020741 Tyrosine-protein kinase, receptor TYRO3
IPR020763 Tyrosine-protein kinase, receptor ROR
IPR020774 Tyrosine-protein kinase, receptor PTK7
IPR020777 Tyrosine-protein kinase, neurotrophic receptor
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Contains
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IPR003006 Immunoglobulin/major histocompatibility complex, conserved site
IPR003596 Immunoglobulin V-set, subgroup
IPR003597 Immunoglobulin C1-set
IPR003598 Immunoglobulin subtype 2
IPR003599 Immunoglobulin subtype
IPR013098 Immunoglobulin I-set
IPR013106 Immunoglobulin V-set
IPR013151 Immunoglobulin
IPR013162 CD80-like, immunoglobulin C2-set
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InterPro annotation
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Entry Details in BioMart
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Abstract
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The basic structure of immunoglobulin (Ig) molecules is a tetramer of two light chains and two heavy chains linked by disulphide bonds. There are two types of light chains: kappa and lambda, each composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains: alpha, delta, epsilon, gamma and mu, all consisting of a variable domain (VH) and three (in alpha, delta and gamma) or four (in epsilon and mu) constant domains (CH1 to CH4). Ig molecules are highly modular proteins, in which the variable and constant domains have clear, conserved sequence patterns. The domains in Ig and Ig-like molecules are grouped into four types: V-set (variable; IPR013106), C1-set (constant-1; IPR003597), C2-set (constant-2; IPR008424) and I-set (intermediate; IPR013098) [1]. Structural studies have shown that these domains share a common core Greek-key beta-sandwich structure, with the types differing in the number of strands in the beta-sheets as well as in their sequence patterns [2, 3].
Immunoglobulin-like domains that are related in both sequence and structure can be found in several diverse protein families. Ig-like domains are involved in a variety of functions, including cell-cell recognition, cell-surface receptors, muscle structure and the immune system [4].
This entry is for immunoglobulin-like domains. Studies indicate that the interactions essential for defining the structure of these beta sandwich proteins are also important in nucleation of folding, and that proteins containing this fold may share similar folding pathways even though the proteins may have low sequence homology. The fold consists of a beta-sandwich formed of 7 strands in 2 sheets with a Greek-key topology. Some members of the fold have additional strands. The Pfam alignments do not include the first and last strand of the immunoglobulin-like domain.
A number of sequences identified by this domain are related to oprin, a snake venom metalloproteinase inhibitor from Didelphis marsupialis (Southern opossum) [5] and belong, along with oprin, to MEROPS inhibitor family I43, clan I- [6].
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Structural links
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Database links
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Interactions
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This domain has been experimentally proven to be involved in Protein:Protein interactions. Representative
data is shown with the following
example proteins:
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Example proteins
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A2CG49 Kalirin
O00241 Signal-regulatory protein beta-1
O01761 Muscle M-line assembly protein unc-89
P14090 Endoglucanase C
P20241 Neuroglian
More proteins
Example Proteins Key
| InterPro entry accession number/name and structure databases |
Colour code |
| IPR003305 |
Carbohydrate-binding, CenC-like |
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| IPR013783 |
Immunoglobulin-like fold |
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| IPR001251 |
Cellular retinaldehyde-binding/triple function, C-terminal |
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| IPR017441 |
Protein kinase, ATP binding site |
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| IPR017442 |
Serine/threonine-protein kinase-like domain |
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| IPR014756 |
Immunoglobulin E-set |
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| IPR013098 |
Immunoglobulin I-set |
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| IPR007850 |
RCSD |
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| IPR011009 |
Protein kinase-like domain |
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| IPR008957 |
Fibronectin, type III-like fold |
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| IPR018159 |
Spectrin/alpha-actinin |
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| IPR013106 |
Immunoglobulin V-set |
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| IPR008979 |
Galactose-binding domain-like |
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| IPR000719 |
Protein kinase, catalytic domain |
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| IPR002290 |
Serine/threonine-protein kinase domain |
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| IPR011511 |
Variant SH3 |
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| IPR003961 |
Fibronectin, type III |
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| IPR002017 |
Spectrin repeat |
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| IPR011993 |
Pleckstrin homology-type |
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| IPR007110 |
Immunoglobulin-like |
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| IPR003598 |
Immunoglobulin subtype 2 |
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| IPR003599 |
Immunoglobulin subtype |
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| IPR001701 |
Glycoside hydrolase, family 9 |
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| IPR003597 |
Immunoglobulin C1-set |
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| IPR001849 |
Pleckstrin homology |
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| IPR000219 |
Dbl homology (DH) domain |
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| IPR004197 |
Glycoside hydrolase, family 9, N-terminal, Ig-like |
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| IPR001452 |
Src homology-3 domain |
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| IPR013151 |
Immunoglobulin |
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| IPR012341 |
Six-hairpin glycosidase |
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| IPR008928 |
Six-hairpin glycosidase-like |
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| IPR008271 |
Serine/threonine-protein kinase, active site |
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| IPR018221 |
Glycoside hydrolase, family 9, active site |
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| IPR009134 |
Tyrosine-protein kinase, vascular endothelial growth factor receptor (VEGFR), N-terminal |
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ModBase |
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SWISS-MODEL |
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PDB Chain |
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CATH Domain |
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SCOP Domain |
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Publications
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1.
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Smith DK, Xue H.
Sequence profiles of immunoglobulin and immunoglobulin-like domains.
J. Mol. Biol. 274 530-45 1997
[PubMed: 9417933]
http://dx.doi.org/10.1006/jmbi.1997.1432
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2.
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Potapov V, Sobolev V, Edelman M, Kister A, Gelfand I.
Protein--protein recognition: juxtaposition of domain and interface cores in immunoglobulins and other sandwich-like proteins.
J. Mol. Biol. 342 665-79 2004
[PubMed: 15327963]
http://dx.doi.org/10.1016/j.jmb.2004.06.072
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3.
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Fowler SB, Clarke J.
Mapping the folding pathway of an immunoglobulin domain: structural detail from Phi value analysis and movement of the transition state.
Structure 9 355-66 2001
[PubMed: 11377196]
http://dx.doi.org/10.1016/S0969-2126(01)00596-2
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4.
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Teichmann SA, Chothia C.
Immunoglobulin superfamily proteins in Caenorhabditis elegans.
J. Mol. Biol. 296 1367-83 2000
[PubMed: 10698639]
http://dx.doi.org/10.1006/jmbi.1999.3497
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5.
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Neves-Ferreira AG, Cardinale N, Rocha SL, Perales J, Domont GB.
Isolation and characterization of DM40 and DM43, two snake venom metalloproteinase inhibitors from Didelphis marsupialis serum.
Biochim. Biophys. Acta 1474 309-20 2000
[PubMed: 10779682]
http://dx.doi.org/10.1016/S0304-4165(00)00022-2
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6.
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Rawlings ND, Tolle DP, Barrett AJ.
Evolutionary families of peptidase inhibitors.
Biochem. J. 378 705-16 2004
[PubMed: 14705960]
http://dx.doi.org/10.1042/BJ20031825
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Additional Reading
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Grotenbreg GM, Roan NR, Guillen E, Meijers R, Wang JH, Bell GW, Starnbach MN, Ploegh HL.
Discovery of CD8+ T cell epitopes in Chlamydia trachomatis infection through use of caged class I MHC tetramers.
Proc. Natl. Acad. Sci. U.S.A. 105 2008 3831-6
[PubMed: 18245382]
http://dx.doi.org/10.1073/pnas.0711504105
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Covaceuszach S, Cassetta A, Konarev PV, Gonfloni S, Rudolph R, Svergun DI, Lamba D, Cattaneo A.
Dissecting NGF interactions with TrkA and p75 receptors by structural and functional studies of an anti-NGF neutralizing antibody.
J. Mol. Biol. 381 2008 881-96
[PubMed: 18635195]
http://dx.doi.org/10.1016/j.jmb.2008.06.008
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Armani A, Galli S, Giacomello E, Bagnato P, Barone V, Rossi D, Sorrentino V.
Molecular interactions with obscurin are involved in the localization of muscle-specific small ankyrin1 isoforms to subcompartments of the sarcoplasmic reticulum.
Exp. Cell Res. 312 2006 3546-58
[PubMed: 16962094]
http://dx.doi.org/10.1016/j.yexcr.2006.07.027
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Rudolph MJ, Gergen JP.
DNA-binding by Ig-fold proteins.
Nat. Struct. Biol. 8 2001 384-6
[PubMed: 11323707]
http://dx.doi.org/10.1038/87531
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Halaby DM, Mornon JP.
The immunoglobulin superfamily: an insight on its tissular, species, and functional diversity.
J. Mol. Evol. 46 1998 389-400
[PubMed: 9541533]
http://dx.doi.org/10.1007/PL00006318
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Halaby DM, Poupon A, Mornon J.
The immunoglobulin fold family: sequence analysis and 3D structure comparisons.
Protein Eng. 12 1999 563-71
[PubMed: 10436082]
http://dx.doi.org/10.1093/protein/12.7.563
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Morstadt L, Bohm A, Yuksel D, Kumar K, Stollar BD, Baleja JD.
Engineering and characterization of a single chain surrogate light chain variable domain.
Protein Sci. 17 2008 458-65
[PubMed: 18287279]
http://dx.doi.org/10.1110/ps.073269808
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Bork P, Holm L, Sander C.
The immunoglobulin fold. Structural classification, sequence patterns and common core.
J. Mol. Biol. 242 1994 309-20
[PubMed: 7932691]
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Volbeda A, Hol WG.
Crystal structure of hexameric haemocyanin from Panulirus interruptus refined at 3.2 A resolution.
J. Mol. Biol. 209 1989 249-79
[PubMed: 2585484]
http://dx.doi.org/10.1016/0022-2836(89)90276-3
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Olsen SK, Ibrahimi OA, Raucci A, Zhang F, Eliseenkova AV, Yayon A, Basilico C, Linhardt RJ, Schlessinger J, Mohammadi M.
Insights into the molecular basis for fibroblast growth factor receptor autoinhibition and ligand-binding promiscuity.
Proc. Natl. Acad. Sci. U.S.A. 101 2004 935-40
[PubMed: 14732692]
http://dx.doi.org/10.1073/pnas.0307287101
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van der Ven PF, Wiesner S, Salmikangas P, Auerbach D, Himmel M, Kempa S, Hayess K, Pacholsky D, Taivainen A, Schroder R, Carpen O, Furst DO.
Indications for a novel muscular dystrophy pathway. gamma-filamin, the muscle-specific filamin isoform, interacts with myotilin.
J. Cell Biol. 151 2000 235-48
[PubMed: 11038172]
http://dx.doi.org/10.1083/jcb.151.2.235
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Mohammed F, Cobbold M, Zarling AL, Salim M, Barrett-Wilt GA, Shabanowitz J, Hunt DF, Engelhard VH, Willcox BE.
Phosphorylation-dependent interaction between antigenic peptides and MHC class I: a molecular basis for the presentation of transformed self.
Nat. Immunol. 9 2008 1236-43
[PubMed: 18836451]
http://dx.doi.org/10.1038/ni.1660
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Lin DY, Tanaka Y, Iwasaki M, Gittis AG, Su HP, Mikami B, Okazaki T, Honjo T, Minato N, Garboczi DN.
The PD-1/PD-L1 complex resembles the antigen-binding Fv domains of antibodies and T cell receptors.
Proc. Natl. Acad. Sci. U.S.A. 105 2008 3011-6
[PubMed: 18287011]
http://dx.doi.org/10.1073/pnas.0712278105
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