FSHB_RAT
ID FSHB_RAT Reviewed; 130 AA.
AC P18427;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 2.
DT 03-AUG-2022, entry version 149.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Holtzman;
RX PubMed=3155259; DOI=10.1210/mend-1-10-717;
RA Maurer R.A.;
RT "Molecular cloning and nucleotide sequence analysis of complementary
RT deoxyribonucleic acid for the beta-subunit of rat follicle stimulating
RT hormone.";
RL Mol. Endocrinol. 1:717-723(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2504572; DOI=10.1089/dna.1.1989.8.339;
RA Gharib S.D., Roy A., Wierman M.E., Chin W.W.;
RT "Isolation and characterization of the gene encoding the beta-subunit of
RT rat follicle-stimulating hormone.";
RL DNA 8:339-349(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE OF 55-130.
RC STRAIN=Sprague-Dawley;
RA Kato Y., Ezashi T., Hirai T., Kato T.;
RT "Strain difference in nucleotide sequences of rat glycoprotein hormone
RT subunit cDNAs and gene fragment.";
RL Zool. Sci. 7:877-885(1990).
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; M36804; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; M27048; AAB60705.1; -; Genomic_DNA.
DR EMBL; M27044; AAB60705.1; JOINED; Genomic_DNA.
DR EMBL; D00577; BAA00455.1; -; Genomic_DNA.
DR PIR; A32893; A32893.
DR PIR; I83048; I83048.
DR RefSeq; NP_001007598.1; NM_001007597.2.
DR AlphaFoldDB; P18427; -.
DR SMR; P18427; -.
DR STRING; 10116.ENSRNOP00000006512; -.
DR GlyGen; P18427; 2 sites.
DR PaxDb; P18427; -.
DR Ensembl; ENSRNOT00000006512; ENSRNOP00000006512; ENSRNOG00000004898.
DR GeneID; 25447; -.
DR KEGG; rno:25447; -.
DR UCSC; RGD:2630; rat.
DR CTD; 2488; -.
DR RGD; 2630; Fshb.
DR eggNOG; ENOG502S39C; Eukaryota.
DR GeneTree; ENSGT00940000160051; -.
DR HOGENOM; CLU_126319_3_0_1; -.
DR InParanoid; P18427; -.
DR OMA; LCWKAIC; -.
DR OrthoDB; 1362225at2759; -.
DR PhylomeDB; P18427; -.
DR TreeFam; TF332940; -.
DR Reactome; R-RNO-209822; Glycoprotein hormones.
DR Reactome; R-RNO-375281; Hormone ligand-binding receptors.
DR PRO; PR:P18427; -.
DR Proteomes; UP000002494; Chromosome 3.
DR ExpressionAtlas; P18427; baseline and differential.
DR Genevisible; P18427; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0001541; P:ovarian follicle development; ISO:RGD.
DR GO; GO:0045780; P:positive regulation of bone resorption; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0010893; P:positive regulation of steroid biosynthetic process; ISO:RGD.
DR GO; GO:0045670; P:regulation of osteoclast differentiation; ISO:RGD.
DR GO; GO:0010469; P:regulation of signaling receptor activity; ISS:UniProtKB.
DR GO; GO:0060011; P:Sertoli cell proliferation; ISO:RGD.
DR GO; GO:0007283; P:spermatogenesis; ISO:RGD.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISO:RGD.
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; 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..20
FT CHAIN 21..130
FT /note="Follitropin subunit beta"
FT /id="PRO_0000011716"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P01225"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P01225"
FT DISULFID 22..70
FT /evidence="ECO:0000250|UniProtKB:P01225"
FT DISULFID 36..85
FT /evidence="ECO:0000250|UniProtKB:P01225"
FT DISULFID 39..123
FT /evidence="ECO:0000250|UniProtKB:P01225"
FT DISULFID 47..101
FT /evidence="ECO:0000250|UniProtKB:P01225"
FT DISULFID 51..103
FT /evidence="ECO:0000250|UniProtKB:P01225"
FT DISULFID 106..113
FT /evidence="ECO:0000250|UniProtKB:P01225"
FT VARIANT 73
FT /note="K -> R (in strain: Sprague-Dawley)"
SQ SEQUENCE 130 AA; 14814 MW; 690E3FC5FC1BD097 CRC64;
MMKSIQLCIL LWCLRAVCCH SCELTNITIS VEKEECRFCI SINTTWCEGY CYTRDLVYKD
PARPNTQKVC TFKELVYETI RLPGCARHSD SLYTYPVATE CHCGKCDSDS TDCTVRGLGP
SYCSFGEMKE
