Is a component of

FSH

Peptide Sequence

SCELTNITISVEKEECRFCISINTTWCEGYCYTRDLVYKDPARPNTQKVCTFKELVYETIRLPGCARHSDSLYTYPVATE CHCGKCDSDSTDCTVRGLGPSYCSFGEMKE

Ser-Cys-Glu-Leu-Thr-Asn-Ile-Thr-Ile-Ser-Val-Glu-Lys-Glu-Glu-Cys-Arg-Phe-Cys-Ile-Ser-Ile-Asn-Thr-Thr-Trp-Cys-Glu-Gly-Tyr-Cys-Tyr-Thr-Arg-Asp-Leu-Val-Tyr-Lys-Asp-Pro-Ala-Arg-Pro-Asn-Thr-Gln-Lys-Val-Cys-Thr-Phe-Lys-Glu-Leu-Val-Tyr-Glu-Thr-Ile-Arg-Leu-Pro-Gly-Cys-Ala-Arg-His-Ser-Asp-Ser-Leu-Tyr-Thr-Tyr-Pro-Val-Ala-Thr-Glu-Cys-His-Cys-Gly-Lys-Cys-Asp-Ser-Asp-Ser-Thr-Asp-Cys-Thr-Val-Arg-Gly-Leu-Gly-Pro-Ser-Tyr-Cys-Ser-Phe-Gly-Glu-Met-Lys-Glu

Post-translational Modification

The production of biologically active FSH requires appropriately folded and glycosylated FSHβ and common α subunits that assemble to form the heterodimeric hormone. FSHβ is glysolyated at asparagine residues at positions 6 and 23, and disulfide bond formation occurs between cysteine residues at postions 2 and 50; 16 and 65; 19 and 103; 27 and 81; 31 and 83 and 86 and 93. The FSHβ and common alpha subunits then assemble to form the biologically active FSH heterodimer.