FSHB_PIG
ID FSHB_PIG Reviewed; 129 AA.
AC P01228; Q3LRP6;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 3.
DT 03-AUG-2022, entry version 134.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Landrace X Yorkshire; TISSUE=Pituitary anterior lobe;
RX PubMed=2174241; DOI=10.1677/jme.0.0050147;
RA Hirai T., Takikawa H., Kato Y.;
RT "The gene for the beta subunit of porcine FSH: absence of consensus
RT oestrogen-responsive element and presence of retroposons.";
RL J. Mol. Endocrinol. 5:147-158(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Meishan;
RX PubMed=10690358; DOI=10.1046/j.1365-2052.2000.00581.x;
RA Li M.D., Rohrer G.A., Wise T.H., Ford J.J.;
RT "Identification and characterization of a new allele for the beta subunit
RT of follicle-stimulating hormone in Chinese pig breeds.";
RL Anim. Genet. 31:28-30(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Blood;
RA Wang J.F., Ran X.Q., Liu J.J.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 15-129.
RC TISSUE=Pituitary anterior lobe;
RX PubMed=3129323; DOI=10.1016/0303-7207(88)90097-4;
RA Kato Y.;
RT "Cloning and DNA sequence analysis of the cDNA for the precursor of porcine
RT follicle stimulating hormone (FSH) beta subunit.";
RL Mol. Cell. Endocrinol. 55:107-112(1988).
RN [5]
RP PROTEIN SEQUENCE OF 21-126.
RX PubMed=658036; DOI=10.1111/j.1432-1033.1978.tb12290.x;
RA Closset J., Maghuin-Rogister G., Hennen G., Strosberg A.D.;
RT "Porcine follitropin. The amino-acid sequence of the beta subunit.";
RL Eur. J. Biochem. 86:115-120(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; D00621; BAA00499.1; -; Genomic_DNA.
DR EMBL; AF134151; AAD34785.1; -; mRNA.
DR EMBL; DQ189097; ABA29775.1; -; Genomic_DNA.
DR EMBL; EF066511; ABL09972.1; -; Genomic_DNA.
DR EMBL; M35676; AAA31039.1; -; mRNA.
DR PIR; A48169; FTPGB.
DR RefSeq; NP_999040.1; NM_213875.1.
DR AlphaFoldDB; P01228; -.
DR SMR; P01228; -.
DR STRING; 9823.ENSSSCP00000014160; -.
DR PaxDb; P01228; -.
DR PRIDE; P01228; -.
DR Ensembl; ENSSSCT00000014555; ENSSSCP00000014160; ENSSSCG00000013328.
DR Ensembl; ENSSSCT00005017472; ENSSSCP00005010449; ENSSSCG00005011332.
DR Ensembl; ENSSSCT00015003072; ENSSSCP00015001000; ENSSSCG00015002484.
DR Ensembl; ENSSSCT00045064077; ENSSSCP00045045238; ENSSSCG00045037160.
DR Ensembl; ENSSSCT00055033933; ENSSSCP00055026967; ENSSSCG00055017256.
DR Ensembl; ENSSSCT00060072875; ENSSSCP00060031425; ENSSSCG00060053521.
DR Ensembl; ENSSSCT00065056533; ENSSSCP00065024589; ENSSSCG00065041317.
DR Ensembl; ENSSSCT00070008873; ENSSSCP00070007285; ENSSSCG00070004693.
DR GeneID; 396895; -.
DR KEGG; ssc:396895; -.
DR CTD; 2488; -.
DR VGNC; VGNC:99654; FSHB.
DR eggNOG; ENOG502S39C; Eukaryota.
DR GeneTree; ENSGT00940000160051; -.
DR HOGENOM; CLU_126319_3_0_1; -.
DR InParanoid; P01228; -.
DR OMA; LCWKAIC; -.
DR OrthoDB; 1362225at2759; -.
DR TreeFam; TF332940; -.
DR Reactome; R-SSC-209822; Glycoprotein hormones.
DR Reactome; R-SSC-375281; Hormone ligand-binding receptors.
DR Reactome; R-SSC-418555; G alpha (s) signalling events.
DR Proteomes; UP000008227; Chromosome 2.
DR Proteomes; UP000314985; Chromosome 2.
DR Bgee; ENSSSCG00000013328; Expressed in pituitary gland and 4 other tissues.
DR Genevisible; P01228; SS.
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:0045780; P:positive regulation of bone resorption; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0010893; P:positive regulation of steroid biosynthetic process; IEA:Ensembl.
DR GO; GO:0045670; P:regulation of osteoclast differentiation; IEA:Ensembl.
DR GO; GO:0010469; P:regulation of signaling receptor activity; ISS:UniProtKB.
DR GO; GO:0060011; P:Sertoli cell proliferation; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
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..20
FT /evidence="ECO:0000269|PubMed:658036"
FT CHAIN 21..129
FT /note="Follitropin subunit beta"
FT /id="PRO_0000011715"
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 32..36
FT /note="KEECN -> VKCLT (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 51..52
FT /note="YT -> TTG (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 71..72
FT /note="FK -> YR (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="S -> G (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 129 AA; 14605 MW; 20BBCBEDF209E1EA CRC64;
MKSLQFCFLF CCWKAICCNS CELTNITITV EKEECNFCIS INTTWCAGYC YTRDLVYKDP
ARPNIQKTCT FKELVYETVK VPGCAHHADS LYTYPVATEC HCGKCDSDST DCTVRGLGPS
YCSFSEMKE
