FSHB_RABIT
ID FSHB_RABIT Reviewed; 129 AA.
AC Q6IY73;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 84.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Japanese white; TISSUE=Pituitary;
RA Suzuki O.;
RL Submitted (JUN-2004) 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; AY614704; AAT37166.1; -; mRNA.
DR RefSeq; NP_001075640.1; NM_001082171.2.
DR AlphaFoldDB; Q6IY73; -.
DR SMR; Q6IY73; -.
DR STRING; 9986.ENSOCUP00000016404; -.
DR Ensembl; ENSOCUT00000023790; ENSOCUP00000016404; ENSOCUG00000021932.
DR GeneID; 100008946; -.
DR KEGG; ocu:100008946; -.
DR CTD; 2488; -.
DR eggNOG; ENOG502S39C; Eukaryota.
DR GeneTree; ENSGT00940000160051; -.
DR HOGENOM; CLU_126319_3_0_1; -.
DR InParanoid; Q6IY73; -.
DR OMA; LCWKAIC; -.
DR OrthoDB; 1362225at2759; -.
DR Proteomes; UP000001811; Chromosome 1.
DR Bgee; ENSOCUG00000021932; Expressed in uterus.
DR ExpressionAtlas; Q6IY73; baseline.
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:0042699; P:follicle-stimulating hormone signaling pathway; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0045780; P:positive regulation of bone resorption; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0010893; P:positive regulation of steroid biosynthetic process; IEA:Ensembl.
DR GO; GO:0045670; P:regulation of osteoclast differentiation; IEA:Ensembl.
DR GO; GO:0010469; P:regulation of signaling receptor activity; ISS:UniProtKB.
DR GO; GO:0060011; P:Sertoli cell proliferation; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
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_0000042863"
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; 14588 MW; 4BEE732CD92A992B CRC64;
MKSVQFCFLF CCWKAICCSS CELTNITIAV EKEECRFCIS INTTWCSGYC YTRDLVYKDP
ARPNIQKICT FKELVYETVR VPGCAHHADS LYTYPVATEC HCGNCDSDST DCTVRGLGPS
YCSFGEMKE
