I-set domains are found in several cell adhesion molecules, including vascular (VCAM), intercellular (ICAM), neural (NCAM) and mucosal addressin (MADCAM) cell adhesion molecules, as well as junction adhesion molecules (JAM). I-set domains are also present in several other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1,[2] and the signalling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.[3]
| Immunoglobulin I-set domain | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
 Structures of fibroblast growth factor 1.[1] | |||||||||||
| Identifiers | |||||||||||
| Symbol | I-set | ||||||||||
| Pfam | PF07679 | ||||||||||
| InterPro | IPR013098 | ||||||||||
| |||||||||||
Human proteins containing this domain
edit- ADAMTSL1, ADAMTSL3, ALPK3, AXL,
- BOC,
- C9orf94, CADM2, CADM4, CCDC141, CDON, CEACAM7, CHL1, CILP2, CNTN1, CNTN2, CNTN3, CNTN4, CNTN5, CNTN6, CXADR,
- DCC, DSCAM, DSCAML1,
- ESAM,
- FGFR1, FGFR3, FGFR4, FGFRL1, FLT1, FLT4, FSTL4, FSTL5,
- HMCN1, HNT, HSPG2,
- ICAM5, IGFBP7, IGFBPL1, IGSF10, IGSF22, IGSF9, ISLR,
- KALRN, KAZALD1, KDR, KIAA0626, KIRREL, KIRREL2, KIRREL3,
- L1CAM, LINGO1, LINGO2, LRFN2, LRFN3, LRFN4, LRFN5, LRIG1, LRIG2, LRIG3, LRIT2, LRIT3, LRRC24, LRRC4B, LRRC4C, LRRN1, LRRN3, LRRN5, LSAMP,
- MAG, MDGA2, MFAP3L, MUSK, MXRA5, MYBPC1, MYBPC2, MYBPC3, MYBPH, MYBPHL, MYLK, MYOM1, MYOM2, MYOM3, MYOT, MYPN,
- NCAM1, NCAM2, NEGR1, NEO1, NEXN, NFASC, NGL1, NOPE, NPHS1, NPTN, NRCAM, NRG2, NT, NTRK2, NTRK3,
- OBSCN, OBSL1, OPCML,
- PALLD, PAPLN, PDGFRA, PRODH2, PTK7, PTPRD, PTPRF, PTPRS, PTPsigma, PUNC,
- ROBO1, ROBO2, ROBO3, ROBO4, ROR1, ROR2,
- SDK1, SDK2, SIGLEC1, SIGLEC6, SPEG,
- TRIO, TTN,
- UNC5A, UNC5B, UNC5C,
- VCAM1, WFIKKN1, WFIKKN2,
References
edit- ^ Plotnikov AN, Hubbard SR, Schlessinger J, Mohammadi M (May 2000). "Crystal structures of two FGF-FGFR complexes reveal the determinants of ligand-receptor specificity". Cell. 101 (4): 413–24. doi:10.1016/S0092-8674(00)80851-X. PMID 10830168. S2CID 16374022.413-24&rft.date=2000-05&rft_id=https://api.semanticscholar.org/CorpusID:16374022#id-name=S2CID&rft_id=info:pmid/10830168&rft_id=info:doi/10.1016/S0092-8674(00)80851-X&rft.aulast=Plotnikov&rft.aufirst=AN&rft.au=Hubbard, SR&rft.au=Schlessinger, J&rft.au=Mohammadi, M&rft_id=https://doi.org/10.1016%2FS0092-8674%2800%2980851-X&rfr_id=info:sid/en.wikipedia.org:Immunoglobulin I-set domain" class="Z3988">
- ^ Sonderegger P, Welte W, Diederichs K, Freigang J, Proba K, Leder L (2000). "The crystal structure of the ligand binding module of axonin-1/TAG-1 suggests a zipper mechanism for neural cell adhesion" (PDF). Cell. 101 (4): 425–33. doi:10.1016/S0092-8674(00)80852-1. PMID 10830169. S2CID 15440572. Archived from the original (PDF) on 2018-07-19. Retrieved 2020-09-03.425-33&rft.date=2000&rft_id=https://api.semanticscholar.org/CorpusID:15440572#id-name=S2CID&rft_id=info:pmid/10830169&rft_id=info:doi/10.1016/S0092-8674(00)80852-1&rft.aulast=Sonderegger&rft.aufirst=P&rft.au=Welte, W&rft.au=Diederichs, K&rft.au=Freigang, J&rft.au=Proba, K&rft.au=Leder, L&rft_id=https://www.zora.uzh.ch/id/eprint/1084/1/Freigang_2000%2C_Cell.pdf&rfr_id=info:sid/en.wikipedia.org:Immunoglobulin I-set domain" class="Z3988">
- ^ Stuart DI, Jones EY, Harlos K, Esnouf RM, Love CA (2006). "Structure determination of human semaphorin 4D as an example of the use of MAD in non-optimal cases". Acta Crystallogr. D. 62 (Pt 1): 108–15. doi:10.1107/S0907444905034992. PMID 16369100.108-15&rft.date=2006&rft_id=info:doi/10.1107/S0907444905034992&rft_id=info:pmid/16369100&rft.aulast=Stuart&rft.aufirst=DI&rft.au=Jones, EY&rft.au=Harlos, K&rft.au=Esnouf, RM&rft.au=Love, CA&rft_id=https://doi.org/10.1107%2FS0907444905034992&rfr_id=info:sid/en.wikipedia.org:Immunoglobulin I-set domain" class="Z3988">
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