ID   FSHB_MASCO              Reviewed;         130 AA.
AC   Q6SI68;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=Follitropin subunit beta;
DE   AltName: Full=Follicle-stimulating hormone beta subunit;
DE            Short=FSH-B;
DE            Short=FSH-beta;
DE   AltName: Full=Follitropin beta chain;
DE   Flags: Precursor;
GN   Name=FSHB;
OS   Mastomys coucha (Southern multimammate mouse) (Praomys coucha).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mastomys.
OX   NCBI_TaxID=35658;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=MCC; TISSUE=Pituitary;
RX   PubMed=15364211; DOI=10.1016/j.ygcen.2004.06.009;
RA   Takano K., Koura M., Noguchi Y., Yamamoto Y., Uchio-Yamada K., Matsuda J.,
RA   Suzuki O.;
RT   "Sequence analysis of cDNA encoding follicle-stimulating hormone and
RT   luteinizing hormone beta-subunits in the Mastomys (Praomys coucha).";
RL   Gen. Comp. Endocrinol. 138:281-286(2004).
CC   -!- FUNCTION: Together with the alpha chain CGA constitutes follitropin,
CC       the follicle-stimulating hormone, and provides its biological
CC       specificity to the hormone heterodimer. Binds FSHR, a G protein-coupled
CC       receptor, on target cells to activate downstream signaling pathways.
CC       Follitropin is involved in follicle development and spermatogenesis in
CC       reproductive organs. {ECO:0000250|UniProtKB:P01225}.
CC   -!- SUBUNIT: Heterodimer. The active follitropin is a heterodimer composed
CC       of an alpha chain/CGA shared with other hormones and a unique beta
CC       chain/FSHB shown here. {ECO:0000250|UniProtKB:P01225}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01225}.
CC       Note=Efficient secretion requires dimerization with CGA.
CC       {ECO:0000250|UniProtKB:P01225}.
CC   -!- SIMILARITY: Belongs to the glycoprotein hormones subunit beta family.
CC       {ECO:0000305}.
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DR   EMBL; AY458603; AAR21602.1; -; mRNA.
DR   AlphaFoldDB; Q6SI68; -.
DR   SMR; Q6SI68; -.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0016914; C:follicle-stimulating hormone complex; ISS:UniProtKB.
DR   GO; GO:0016913; F:follicle-stimulating hormone activity; ISS:UniProtKB.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0010469; P:regulation of signaling receptor activity; ISS:UniProtKB.
DR   CDD; cd00069; GHB_like; 1.
DR   Gene3D; 2.10.90.10; -; 1.
DR   InterPro; IPR029034; Cystine-knot_cytokine.
DR   InterPro; IPR006208; Glyco_hormone_CN.
DR   InterPro; IPR001545; Gonadotropin_bsu.
DR   InterPro; IPR018245; Gonadotropin_bsu_CS.
DR   PANTHER; PTHR11515; PTHR11515; 1.
DR   Pfam; PF00007; Cys_knot; 1.
DR   SMART; SM00068; GHB; 1.
DR   SUPFAM; SSF57501; SSF57501; 1.
DR   PROSITE; PS00261; GLYCO_HORMONE_BETA_1; 1.
DR   PROSITE; PS00689; GLYCO_HORMONE_BETA_2; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hormone; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..130
FT                   /note="Follitropin subunit beta"
FT                   /id="PRO_0000042881"
FT   CARBOHYD        26
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:P01225"
FT   CARBOHYD        43
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:P01225"
FT   DISULFID        22..70
FT                   /evidence="ECO:0000250|UniProtKB:P01225"
FT   DISULFID        36..85
FT                   /evidence="ECO:0000250|UniProtKB:P01225"
FT   DISULFID        39..123
FT                   /evidence="ECO:0000250|UniProtKB:P01225"
FT   DISULFID        47..101
FT                   /evidence="ECO:0000250|UniProtKB:P01225"
FT   DISULFID        51..103
FT                   /evidence="ECO:0000250|UniProtKB:P01225"
FT   DISULFID        106..113
FT                   /evidence="ECO:0000250|UniProtKB:P01225"
SQ   SEQUENCE   130 AA;  14887 MW;  4737ACDA37F2A4CD CRC64;
     MMKSIQLCIL LWCWRAICCH SCELTNITIS IEKEECRFCI SINTTWCAGY CYTRDLVYKD
     PARPNTQKVC TFKELVYETI RLPGCARHSD SLYTYPVATE CHCGKCDSDS TDCTVRGLGP
     SYCSFSEMKE