ID   FSHB_MACFA              Reviewed;         129 AA.
AC   Q6EV79;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 76.
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   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC   TISSUE=Pituitary;
RX   PubMed=10612425; DOI=10.1016/s0303-7207(99)00140-9;
RA   Schmidt A., Gromoll J., Weinbauer G.F., Galla H.J., Chappel S., Simoni M.;
RT   "Cloning and expression of cynomolgus monkey (Macaca fascicularis)
RT   gonadotropins luteinizing hormone and follicle-stimulating hormone and
RT   identification of two polymorphic sites in the luteinizing hormone beta
RT   subunit.";
RL   Mol. Cell. Endocrinol. 156:73-83(1999).
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       (PubMed:10612425). Follitropin is involved in follicle development and
CC       spermatogenesis in reproductive organs (By similarity).
CC       {ECO:0000250|UniProtKB:P01225, ECO:0000269|PubMed:10612425}.
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:0000269|PubMed:10612425}.
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; AJ781395; CAH03729.1; -; mRNA.
DR   RefSeq; XP_005578391.1; XM_005578334.2.
DR   AlphaFoldDB; Q6EV79; -.
DR   SMR; Q6EV79; -.
DR   STRING; 9541.XP_005578391.1; -.
DR   GeneID; 101864888; -.
DR   KEGG; mcf:101864888; -.
DR   CTD; 2488; -.
DR   VEuPathDB; HostDB:ENSMFAG00000039808; -.
DR   eggNOG; ENOG502S39C; Eukaryota.
DR   OrthoDB; 1362225at2759; -.
DR   Proteomes; UP000233100; Chromosome 14.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0016914; C:follicle-stimulating hormone complex; IDA:UniProtKB.
DR   GO; GO:0016913; F:follicle-stimulating hormone activity; IDA:UniProtKB.
DR   GO; GO:0042699; P:follicle-stimulating hormone signaling pathway; IDA:UniProtKB.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:0010469; P:regulation of signaling receptor activity; IDA: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; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000250"
FT   CHAIN           19..129
FT                   /note="Follitropin subunit beta"
FT                   /id="PRO_0000011712"
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;  14644 MW;  305D9F0228D31E20 CRC64;
     MKTVQFCFLF CCWKAICCNS CELTNITIAI EKEECRFCIS INTTWCAGYC YTRDLVYKDP
     ARPNIQKTCT FKEVVYETVR VPGCAHHADS LYTYPVATQC HCGKCDSDST DCTVRGLGPS
     YCSFSEMKE