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Database: UniProt
Entry: FSHB_CAPHI
LinkDB: FSHB_CAPHI
Original site: FSHB_CAPHI 
ID   FSHB_CAPHI              Reviewed;         129 AA.
AC   Q8HY83; Q8MJ51;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, 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   Capra hircus (Goat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Capra.
OX   NCBI_TaxID=9925;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Guan H.-B., Li Q.-Z., Zhang L.;
RT   "Nucleotide sequence of cloned cDNA for beta subunit of Cervus nippon
RT   follicle stimulating hormone.";
RL   Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Ding J.T., Zhang J.Q., Sun H.C., Jiang X.P.;
RT   "Cloning and DNA sequence analysis of the cDNA for goat follicle
RT   stimulating hormone.";
RL   Submitted (JUN-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; AY156689; AAN84783.1; -; mRNA.
DR   EMBL; AF522070; AAM81325.1; -; mRNA.
DR   RefSeq; XP_013825236.2; XM_013969782.2.
DR   AlphaFoldDB; Q8HY83; -.
DR   SMR; Q8HY83; -.
DR   STRING; 9925.ENSCHIP00000026623; -.
DR   GlyCosmos; Q8HY83; 2 sites, No reported glycans.
DR   GeneID; 100861299; -.
DR   CTD; 2488; -.
DR   OrthoDB; 5353873at2759; -.
DR   Proteomes; UP000291000; Unassembled WGS sequence.
DR   Proteomes; UP000694566; Unplaced.
DR   Proteomes; UP000694900; Genome assembly.
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; Cystine-knot cytokines; 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:SF17; FOLLITROPIN SUBUNIT BETA; 1.
DR   PANTHER; PTHR11515; GLYCOPROTEIN HORMONE BETA CHAIN; 1.
DR   Pfam; PF00007; Cys_knot; 1.
DR   SMART; SM00068; GHB; 1.
DR   SUPFAM; SSF57501; Cystine-knot cytokines; 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_0000011707"
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"
FT   CONFLICT        4
FT                   /note="V -> I (in Ref. 2; AAM81325)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        126
FT                   /note="D -> E (in Ref. 2; AAM81325)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   129 AA;  14688 MW;  83D76DD0F5823D40 CRC64;
     MKSVQFCFLF CCWRAICCRS CELTNITITV EKEECSFCIS INTTWCAGYC YTRDLVYKDP
     ARPNIQKACT FKELVYETVK VPGCARHADS LYTYPVATEC HCGKCDRDST DCTVRGLGPS
     YCSFSDIRE
//
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