ID   FSHB_GORGO              Reviewed;         129 AA.
AC   A1BN60;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 59.
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   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=17227474; DOI=10.1111/j.1469-1809.2006.00299.x;
RA   Grigorova M., Rull K., Laan M.;
RT   "Haplotype structure of FSHB, the beta-subunit gene for fertility-
RT   associated follicle-stimulating hormone: possible influence of balancing
RT   selection.";
RL   Ann. Hum. Genet. 71:18-28(2007).
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; DQ304480; ABC72311.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1BN60; -.
DR   SMR; A1BN60; -.
DR   STRING; 9593.ENSGGOP00000009287; -.
DR   eggNOG; ENOG502S39C; Eukaryota.
DR   HOGENOM; CLU_126319_3_0_1; -.
DR   InParanoid; A1BN60; -.
DR   Proteomes; UP000001519; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0042699; P:follicle-stimulating hormone signaling pathway; IBA:GO_Central.
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   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Hormone; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000250"
FT   CHAIN           21..129
FT                   /note="Follitropin subunit beta"
FT                   /id="PRO_0000285558"
FT   CARBOHYD        25
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:P01225"
FT   CARBOHYD        42
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:P01225"
FT   DISULFID        21..69
FT                   /evidence="ECO:0000250|UniProtKB:P01225"
FT   DISULFID        35..84
FT                   /evidence="ECO:0000250|UniProtKB:P01225"
FT   DISULFID        38..122
FT                   /evidence="ECO:0000250|UniProtKB:P01225"
FT   DISULFID        46..100
FT                   /evidence="ECO:0000250|UniProtKB:P01225"
FT   DISULFID        50..102
FT                   /evidence="ECO:0000250|UniProtKB:P01225"
FT   DISULFID        105..112
FT                   /evidence="ECO:0000250|UniProtKB:P01225"
SQ   SEQUENCE   129 AA;  14686 MW;  9D2D877DD01CFE2B CRC64;
     MKTLQFFFLF CCWKAICCNS CELTNITIAI EKEECRFCIS INTTWCAGYC YTRDLVYKDP
     ARPNIQKTCT FKELVYETVR VPGCAHHADS LYTYPVATQC HCGKCDSDST DCTVRGLGPS
     YCSFGEMKE