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FSHB_BOVIN
ID   FSHB_BOVIN              Reviewed;         129 AA.
AC   P04837;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   03-AUG-2022, entry version 135.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3092216; DOI=10.1073/pnas.83.17.6618;
RA   Esch F.S., Mason A.J., Cooksey K., Mercado M., Shimasaki S.;
RT   "Cloning and DNA sequence analysis of the cDNA for the precursor of the
RT   beta chain of bovine follicle stimulating hormone.";
RL   Proc. Natl. Acad. Sci. U.S.A. 83:6618-6621(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3096676; DOI=10.1089/dna.1986.5.363;
RA   Maurer R.A., Beck A.;
RT   "Isolation and nucleotide sequence analysis of a cloned cDNA encoding the
RT   beta-subunit of bovine follicle-stimulating hormone.";
RL   DNA 5:363-369(1986).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2840246; DOI=10.1089/dna.1988.7.227;
RA   Kim K.E., Gordon D.F., Maurer R.A.;
RT   "Nucleotide sequence of the bovine gene for follicle-stimulating hormone
RT   beta-subunit.";
RL   DNA 7:227-233(1988).
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; M13383; AAA30526.1; -; mRNA.
DR   EMBL; M14853; AAA30527.1; -; mRNA.
DR   EMBL; M83753; AAA30528.1; -; Genomic_DNA.
DR   PIR; A29816; A23550.
DR   RefSeq; NP_776485.1; NM_174060.1.
DR   AlphaFoldDB; P04837; -.
DR   SMR; P04837; -.
DR   STRING; 9913.ENSBTAP00000014462; -.
DR   GlyConnect; 164; 2 N-Linked glycans.
DR   PaxDb; P04837; -.
DR   Ensembl; ENSBTAT00000014462; ENSBTAP00000014462; ENSBTAG00000010889.
DR   GeneID; 281171; -.
DR   KEGG; bta:281171; -.
DR   CTD; 2488; -.
DR   VEuPathDB; HostDB:ENSBTAG00000010889; -.
DR   eggNOG; ENOG502S39C; Eukaryota.
DR   GeneTree; ENSGT00940000160051; -.
DR   HOGENOM; CLU_126319_3_0_1; -.
DR   InParanoid; P04837; -.
DR   OMA; LCWKAIC; -.
DR   OrthoDB; 1362225at2759; -.
DR   TreeFam; TF332940; -.
DR   Reactome; R-BTA-209822; Glycoprotein hormones.
DR   Proteomes; UP000009136; Chromosome 15.
DR   Bgee; ENSBTAG00000010889; Expressed in adenohypophysis and 22 other tissues.
DR   ExpressionAtlas; P04837; baseline and differential.
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   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hormone; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000250"
FT   CHAIN           21..129
FT                   /note="Follitropin subunit beta"
FT                   /id="PRO_0000011706"
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;  14713 MW;  8150FBAED1C1AF99 CRC64;
     MKSVQFCFLF CCWRAICCRS CELTNITITV EKEECGFCIS INTTWCAGYC YTRDLVYRDP
     ARPNIQKTCT FKELVYETVK VPGCAHHADS LYTYPVATEC HCSKCDSDST DCTVRGLGPS
     YCSFREIKE
 
 
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