20210801 20180803 20180328 20210801 IID50202 Follistatin Activin-binding protein Rattus norvegicus 344 P21674 Q80XW7 Binds directly to activin and functions as an activin antagonist. Specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (FSH). Cell projection, Lamellipodium membrane. SL-0292 unkown Cell membrane. SL-0039 unkown Cytoplasm. SL-0086 unkown 0 0 0 0 Fst FST_RAT MVCARHQPGGLCLLLLLLCQFMEDRSAQAGNCWLRQAKNGRCQVLYKTELSKEECCSTGRLSTSWTEEDVNDNTLFKWMIFNGGAPNCIPCKETCENVDCGPGKKCRMNKKNKPRCVCAPDCSNITWKGPVCGLDGKTYRNECALLKARCKEQPELEVQYQGKCKKTCRDVFCPGSSTCVVDQTNNAYCVTCNRICPEPSSSEQSLCGNDGVTYSSACHLRKATCLLGRSIGLAYEGKCIKAKSCEDIQCGGGKKCLWDFKVGRGRCSLCDELCPDSKSDEPVCASDNATYASECAMKEAACSSGVLLEVKHSGSCNSISEETEEEEEEEDQDYSFPISSTLEW 1 1lr8A 93 165 order 1 2 2arpF 93 93 disorder 3 3 2arpF 94 241 order 3 4 1lr7A 93 165 order 2 5 1lr9A 93 165 order 4 1 1lr8 X-RAY 289K 6.5 12867435 C.A.INNIS,M.HYVONEN CRYSTAL STRUCTURES OF THE HEPARAN SULFATE-BINDING DOMAIN OF FOLLISTATIN: INSIGHTS INTO LIGAND BINDING. 2003 J.BIOL.CHEM. 278 39969 x-ray 1lr8 A 93 165 100 0 1 1lr8_1 786 Monomer monomer 1lr8A P21674 IID50202 2 1lr7 X-RAY 289K 8.5 12867435 C.A.INNIS,M.HYVONEN CRYSTAL STRUCTURES OF THE HEPARAN SULFATE-BINDING DOMAIN OF FOLLISTATIN: INSIGHTS INTO LIGAND BINDING. 2003 J.BIOL.CHEM. 278 39969 x-ray 1lr7 A 93 165 100 0 1 1lr7_1 786 Monomer monomer 1lr7A P21674 IID50202 3 2arp X-RAY 293K 8 16482217 A.E.HARRINGTON,S.A.MORRIS-TRIGGS,B.T.RUOTOLO,C.V.ROBINSON,S.OHNUMA,M.HYVONEN STRUCTURAL BASIS FOR THE INHIBITION OF ACTIVIN SIGNALLING BY FOLLISTATIN 2006 EMBO J. 25 1035 x-ray 2arp F 93 241 100 1 93 93 1 2arp_1 1800 Hetero tetramer 2arpF P21674 IID50202 2arpA P08476 IID00338 2arpA-2arpA 2arpF-2arpA 4 1lr9 X-RAY 289K 8.5 12867435 C.A.INNIS,M.HYVONEN CRYSTAL STRUCTURES OF THE HEPARAN SULFATE-BINDING DOMAIN OF FOLLISTATIN: INSIGHTS INTO LIGAND BINDING. 2003 J.BIOL.CHEM. 278 39969 x-ray 1lr9 A 93 165 100 0 1 1lr9_1 786 Monomer monomer 1lr9A P21674 IID50202 29-276,280-318 1-28,277-279,319-344 17-318 1-16,319-344 1-16,319-344 11-19,321-330