ID   FSHB_PANTA              Reviewed;         129 AA.
AC   Q9BDJ0;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 68.
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   Panthera tigris altaica (Siberian tiger).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Pantherinae;
OC   Panthera.
OX   NCBI_TaxID=74533;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pituitary;
RX   PubMed=12493701; DOI=10.1095/biolreprod.101.002204;
RA   Crichton E.G., Bedows E., Miller-Lindholm A.K., Baldwin D.M.,
RA   Armstrong D.L., Graham L.H., Ford J.J., Gjorret J.O., Hyttel P., Pope C.E.,
RA   Vajta G., Loskutoff N.M.;
RT   "Efficacy of porcine gonadotropins for repeated stimulation of ovarian
RT   activity for oocyte retrieval and in vitro embryo production and
RT   cryopreservation in Siberian tigers (Panthera tigris altaica).";
RL   Biol. Reprod. 68:105-113(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pituitary;
RA   Liao M., Zhu M., Zhang A.;
RT   "Cloning of follicle-stimulating hormone (FSH) and luteinizing hormone (LH)
RT   genes in Panthera tigris altaica.";
RL   Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
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; AF354937; AAK30588.1; -; mRNA.
DR   EMBL; AF540937; AAN28381.1; -; mRNA.
DR   RefSeq; XP_007082072.1; XM_007082010.1.
DR   AlphaFoldDB; Q9BDJ0; -.
DR   SMR; Q9BDJ0; -.
DR   Ensembl; ENSPTIT00000029662; ENSPTIP00000025150; ENSPTIG00000021036.
DR   GeneID; 102970900; -.
DR   KEGG; ptg:102970900; -.
DR   GeneTree; ENSGT00940000160051; -.
DR   Proteomes; UP000675900; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
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:0010893; P:positive regulation of steroid biosynthetic process; IEA:Ensembl.
DR   GO; GO:0010469; P:regulation of signaling receptor activity; ISS:UniProtKB.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
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_0000042862"
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;  14655 MW;  835E6DC2558DEE41 CRC64;
     MKSVQFCFLF CCWRVICCKS CELTNITITV EKEECRFCMS INATWCAGYC YTRDLVYKDP
     ARPNNQKTCT FKELVYETVK VPGCAHQADS LYTYPVATEC HCGKCDSDST DCTVQGLGPS
     YCSFSEMKE