FSHB_LITCT
ID FSHB_LITCT Reviewed; 107 AA.
AC Q9PS36;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 74.
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;
GN Name=fshb;
OS Lithobates catesbeianus (American bullfrog) (Rana catesbeiana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX NCBI_TaxID=8400;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=1426958; DOI=10.1016/0016-6480(92)90203-v;
RA Hayashi T., Hanaoka Y., Hayashi H.;
RT "The complete amino acid sequence of the follitropin beta-subunit of the
RT bullfrog, Rana catesbeiana.";
RL Gen. Comp. Endocrinol. 88:144-150(1992).
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 AlphaFoldDB; Q9PS36; -.
DR SMR; Q9PS36; -.
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; Secreted.
FT CHAIN 1..107
FT /note="Follitropin subunit beta"
FT /id="PRO_0000149039"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P01225"
FT CARBOHYD 22
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P01225"
FT DISULFID 1..49
FT /evidence="ECO:0000250|UniProtKB:P01225"
FT DISULFID 15..64
FT /evidence="ECO:0000250|UniProtKB:P01225"
FT DISULFID 18..102
FT /evidence="ECO:0000250|UniProtKB:P01225"
FT DISULFID 26..80
FT /evidence="ECO:0000250|UniProtKB:P01225"
FT DISULFID 30..82
FT /evidence="ECO:0000250|UniProtKB:P01225"
FT DISULFID 85..92
FT /evidence="ECO:0000250|UniProtKB:P01225"
SQ SEQUENCE 107 AA; 11794 MW; 64736A6BE1B077EC CRC64;
CELSNITIVL EKEECGACVS VNATWCSGYC YTKDANLMYP QKSEKQGVCT YTEVIYETVK
IPGCAENVNP FYTYPVAVDC HCGRCDSETT DCTVRALGPT YCSLSQD
