FSHB_SHEEP
ID FSHB_SHEEP Reviewed; 129 AA.
AC P01227;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 2.
DT 03-AUG-2022, entry version 113.
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 Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2505233; DOI=10.1093/nar/17.15.6391;
RA Mountford P.S., Bello P.A., Brandon M.R., Adams T.E.;
RT "Cloning and DNA sequence analysis of the cDNA for the precursor of ovine
RT follicle stimulating hormone beta-subunit.";
RL Nucleic Acids Res. 17:6391-6391(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1930694; DOI=10.1089/dna.1991.10.593;
RA Guzman K., Miller C.D., Phillips C.L., Miller W.L.;
RT "The gene encoding ovine follicle-stimulating hormone beta: isolation,
RT characterization, and comparison to a related ovine genomic sequence.";
RL DNA Cell Biol. 10:593-601(1991).
RN [3]
RP PROTEIN SEQUENCE OF 20-129.
RX PubMed=6798969; DOI=10.1042/bj1970541;
RA Sairam M.R., Seidah N.G., Chretien M.;
RT "Primary structure of the ovine pituitary follitropin beta-subunit.";
RL Biochem. J. 197:541-552(1981).
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; X15493; CAA33516.1; -; mRNA.
DR EMBL; S64745; AAB20317.1; -; Genomic_DNA.
DR PIR; A40410; FTSHB.
DR RefSeq; NP_001009798.1; NM_001009798.1.
DR AlphaFoldDB; P01227; -.
DR SMR; P01227; -.
DR STRING; 9940.ENSOARP00000016546; -.
DR Ensembl; ENSOART00000016782; ENSOARP00000016546; ENSOARG00000015425.
DR Ensembl; ENSOART00020017224; ENSOARP00020014220; ENSOARG00020011317.
DR GeneID; 443387; -.
DR KEGG; oas:443387; -.
DR CTD; 2488; -.
DR eggNOG; ENOG502S39C; Eukaryota.
DR HOGENOM; CLU_126319_3_0_1; -.
DR OMA; LCWKAIC; -.
DR OrthoDB; 1362225at2759; -.
DR Proteomes; UP000002356; Chromosome 15.
DR Bgee; ENSOARG00000015425; Expressed in pituitary gland and 1 other tissue.
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:0035938; P:estradiol secretion; IMP:AgBase.
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; -; 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 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hormone;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:6798969"
FT CHAIN 20..129
FT /note="Follitropin subunit beta"
FT /id="PRO_0000011717"
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 68
FT /note="A -> T (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="R -> T (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 128..129
FT /note="RE -> ERZ (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 129 AA; 14669 MW; 83D76DCDC971EF40 CRC64;
MKSVQFCFLF CCWRAICCRS CELTNITITV EKEECSFCIS INTTWCAGYC YTRDLVYKDP
ARPNIQKACT FKELVYETVK VPGCAHHADS LYTYPVATEC HCGKCDRDST DCTVRGLGPS
YCSFSDIRE
