FSHB_HORSE
ID FSHB_HORSE Reviewed; 129 AA.
AC P01226; Q9TTJ9;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 125.
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 Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pituitary;
RX PubMed=11717129; DOI=10.1095/biolreprod65.6.1686;
RA Saneyoshi T., Min K.S., Jing Ma X., Nambo Y., Hiyama T., Tanaka S.,
RA Shiota K.;
RT "Equine follicle-stimulating hormone: molecular cloning of beta subunit and
RT biological role of the asparagine-linked oligosaccharide at asparagine(56)
RT of alpha subunit.";
RL Biol. Reprod. 65:1686-1690(2001).
RN [2]
RP PROTEIN SEQUENCE OF 19-129.
RX PubMed=670202; DOI=10.1016/s0021-9258(17)30379-4;
RA Fujiki Y., Rathnam P., Saxena B.B.;
RT "Amino acid sequence of the beta-subunit of the follicle-stimulating
RT hormone from equine pituitary glands.";
RL J. Biol. Chem. 253:5363-5368(1978).
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; AB029157; BAA88560.1; -; mRNA.
DR PIR; A01494; FTHOB.
DR RefSeq; NP_001075284.1; NM_001081815.2.
DR RefSeq; XP_014596961.1; XM_014741475.1.
DR RefSeq; XP_014596962.1; XM_014741476.1.
DR RefSeq; XP_014596963.1; XM_014741477.1.
DR AlphaFoldDB; P01226; -.
DR SMR; P01226; -.
DR STRING; 9796.ENSECAP00000016667; -.
DR PaxDb; P01226; -.
DR Ensembl; ENSECAT00000020310; ENSECAP00000016667; ENSECAG00000019116.
DR GeneID; 100033829; -.
DR KEGG; ecb:100033829; -.
DR CTD; 2488; -.
DR GeneTree; ENSGT00940000160051; -.
DR HOGENOM; CLU_126319_3_0_1; -.
DR InParanoid; P01226; -.
DR OMA; LCWKAIC; -.
DR OrthoDB; 1362225at2759; -.
DR TreeFam; TF332940; -.
DR Proteomes; UP000002281; Chromosome 7.
DR Bgee; ENSECAG00000019116; Expressed in inner cell mass and 1 other tissue.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
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..18
FT /evidence="ECO:0000269|PubMed:670202"
FT CHAIN 19..129
FT /note="Follitropin subunit beta"
FT /id="PRO_0000011710"
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 34..36
FT /note="ECG -> GCR (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="S -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="N -> K (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="A -> Z (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="E -> ZYPVALSY (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 129 AA; 14387 MW; 3916FA71490947CE CRC64;
MKSVQFCFLF CCWKAVCCNS CELTNITIAV EKEECGFCIS INTTWCAGYC YTRDLVYKDP
ARPNIQKTCT FKELVYETVK VPGCAHHADS LYTYPVATAC HCGKCNSDST DCTVRGLGPS
YCSFGDMKE
