FSHB_BUBBU
ID FSHB_BUBBU Reviewed; 129 AA.
AC Q6SV86; Q0Q0G4;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 61.
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 Bubalus bubalis (Domestic water buffalo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bubalus.
OX NCBI_TaxID=89462;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Wang A., Shi D., Li N.;
RT "Sequence analysis of the water buffalo follicle stimulating hormone-beta
RT subunit gene.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Yadav S.P., Goswami S.L., De S., Datta T.K., Yadav P., Raghvan S.,
RA Singh R.;
RL Submitted (MAY-2006) 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; AY449463; AAR13163.1; -; Genomic_DNA.
DR EMBL; DQ666186; ABG57183.1; -; mRNA.
DR RefSeq; NP_001277871.1; NM_001290942.1.
DR AlphaFoldDB; Q6SV86; -.
DR SMR; Q6SV86; -.
DR GeneID; 102406062; -.
DR KEGG; bbub:102406062; -.
DR CTD; 2488; -.
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: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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hormone; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000250"
FT CHAIN 21..129
FT /note="Follitropin subunit beta"
FT /id="PRO_0000042050"
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; 14593 MW; 3547D4109CFF2343 CRC64;
MKSVQFCFLF CCWRAICCRS CELTNITITV EKEECGFCIS INTTWCAGYC YTRDLVYRDP
ARPNIQKTCT YKELVYETVK VPGCAHHADS LYTYPVATEC QCGKCDGDST DCTVRGLGPS
YCSFSESRE
