The Fibronectin type III ___domain is an evolutionarily conserved protein ___domain that is widely found in animal proteins. The fibronectin protein in which this ___domain was first identified contains 16 copies of this ___domain. The ___domain is about 100 amino acids long and possesses a beta sandwich structure. Of the three fibronectin-type domains, type III is the only one without disulfide bonding present. Fibronectin domains are found in a wide variety of extracellular proteins. They are widely distributed in animal species, but also found sporadically in yeast, plant and bacterial proteins.
Fibronectin type III ___domain | |||||||||
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![]() The tenth type III ___domain of fibronectin | |||||||||
Identifiers | |||||||||
Symbol | fn3 | ||||||||
Pfam | PF00041 | ||||||||
Pfam clan | CL0159 | ||||||||
InterPro | IPR003961 | ||||||||
SMART | FN3 | ||||||||
PROSITE | PDOC00214 | ||||||||
SCOP2 | 1ttf / SCOPe / SUPFAM | ||||||||
CDD | cd00063 | ||||||||
Membranome | 66 | ||||||||
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Human proteins containing this ___domain
editABI3BP; ANKFN1; ASTN2; AXL; BOC; BZRAP1; C20orf75; CDON; CHL1; CMYA5; CNTFR; CNTN1; CNTN2; CNTN3; CNTN4; CNTN5; CNTN6; COL12A1; COL14A1; COL20A1; COL7A1; CRLF1; CRLF3; CSF2RB; CSF3R; DCC; DSCAM; DSCAML1; EBI3; EGFLAM; EPHA1; EPHA10; EPHA2; EPHA3; EPHA4; EPHA5; EPHA6; EPHA7; EPHA8; EPHB1; EPHB2; EPHB3; EPHB4; EPHB6; EPOR; FANK1; FLRT1; FLRT2; FLRT3; FN1; FNDC1; FNDC3A; FNDC3B; FNDC4; FNDC5; FNDC7; FNDC8; FSD1; FSD1L; FSD2; GHR; HCFC1; HCFC2; HUGO; IFNGR2; IGF1R; IGSF22; IGSF9; IGSF9B; IL4R; IL11RA; IL12B; IL12RB1; IL12RB2; IL20RB; IL23R; IL27RA; IL31RA; IL6R; IL6ST; IL7R; INSR; INSRR; ITGB4; KAL1; KALRN; L1CAM; LEPR; LIFR; LRFN2; LRFN3; LRFN4; LRFN5; LRIT1; LRRN1; LRRN3; MERTK; MID1; MID2; MPL; MYBPC1; MYBPC2; MYBPC3; MYBPH; MYBPHL; MYLK; MYOM1; MYOM2; MYOM3; NCAM1; NCAM2; NEO1; NFASC; NOPE; NPHS1; NRCAM; OBSCN; OBSL1; OSMR; PHYHIP; PHYHIPL; PRLR; PRODH2; PTPRB; PTPRC; PTPRD; PTPRF; PTPRG; PTPRH; PTPRJ; PTPRK; PTPRM; PTPRO; PTPRS; PTPRT; PTPRU; PTPRZ1; PTPsigma; PUNC; RIMBP2; ROBO1; ROBO2; ROBO3; ROBO4; ROS1; SDK1; SDK2; SNED1; SORL1; SPEG; TEK; TIE1; TNC; TNN; TNR; TNXB; TRIM36; TRIM42; TRIM46; TRIM67; TRIM9; TTN; TYRO3; UMODL1; USH2A; VASN; VWA1; dJ34F7.1; fmi;
See also
edit- Monobodies are engineered (synthetic) antibody mimetics based on a fibronectin type III ___domain (specifically, the 10th FN3 ___domain of human fibronectin). Monobodies feature either diversified loops or diversified strands of a flat beta-sheet surface, which serve as interaction epitopes. Monobody binders have been selected a wide variety of target molecules, and have expanded beyond the potential range of binding interfaces observed in both natural and synthetic antibodies.
References
edit- Bazan JF (September 1990). "Structural design and molecular evolution of a cytokine receptor superfamily". Proceedings of the National Academy of Sciences of the United States of America. 87 (18): 6934–8. Bibcode:1990PNAS...87.6934B. doi:10.1073/pnas.87.18.6934. PMC 54656. PMID 2169613.
- Little E, Bork P, Doolittle RF (December 1994). "Tracing the spread of fibronectin type III domains in bacterial glycohydrolases". Journal of Molecular Evolution. 39 (6): 631–43. Bibcode:1994JMolE..39..631L. doi:10.1007/bf00160409. PMID 7528812. S2CID 11909704.
- Kornblihtt AR, Umezawa K, Vibe-Pedersen K, Baralle FE (July 1985). "Primary structure of human fibronectin: differential splicing may generate at least 10 polypeptides from a single gene". The EMBO Journal. 4 (7): 1755–9. doi:10.1002/j.1460-2075.1985.tb03847.x. PMC 554414. PMID 2992939.