ID   FSHB_MOUSE              Reviewed;         130 AA.
AC   Q60687;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 159.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8543187; DOI=10.1016/0378-1119(95)00611-7;
RA   Kumar T.R., Kelly M., Mortrud M., Low M.J., Matzuk M.M.;
RT   "Cloning of the mouse gonadotropin beta-subunit-encoding genes, I.
RT   Structure of the follicle-stimulating hormone beta-subunit-encoding gene.";
RL   Gene 166:333-334(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pituitary;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=9020850; DOI=10.1038/ng0297-201;
RA   Kumar T.R., Wang Y., Lu N., Matzuk M.M.;
RT   "Follicle stimulating hormone is required for ovarian follicle maturation
RT   but not male fertility.";
RL   Nat. Genet. 15:201-204(1997).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=11416011; DOI=10.1210/endo.142.7.8230;
RA   Wreford N.G., Rajendra Kumar T., Matzuk M.M., de Kretser D.M.;
RT   "Analysis of the testicular phenotype of the follicle-stimulating hormone
RT   beta-subunit knockout and the activin type II receptor knockout mice by
RT   stereological analysis.";
RL   Endocrinology 142:2916-2920(2001).
RN   [6]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=23371388; DOI=10.1210/me.2012-1289;
RA   Xie H., Cherrington B.D., Meadows J.D., Witham E.A., Mellon P.L.;
RT   "Msx1 homeodomain protein represses the alphaGSU and GnRH receptor genes
RT   during gonadotrope development.";
RL   Mol. Endocrinol. 27:422-436(2013).
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 (By
CC       similarity). Follitropin is involved in follicle development and
CC       spermatogenesis in reproductive organs (PubMed:9020850,
CC       PubMed:11416011). {ECO:0000250|UniProtKB:P01225,
CC       ECO:0000269|PubMed:11416011, ECO:0000269|PubMed:9020850}.
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   -!- DEVELOPMENTAL STAGE: Expressed in the developing pituitary gland at
CC       18.5 dpc. {ECO:0000269|PubMed:23371388}.
CC   -!- DISRUPTION PHENOTYPE: Mice lacking Fshb are viable (PubMed:9020850).
CC       Females are infertile displaying abnormal uterus and ovaries that
CC       lacked corpora lutea. The infertility is due to impaired follicle
CC       maturation which appears before antral follicle formation
CC       (PubMed:9020850). Males are fertile and spermatogenesis proceeds
CC       normally. However, these mice display a reduced testes size and
CC       epididymal sperm count (PubMed:9020850, PubMed:11416011). The number of
CC       Sertoli cells is significantly reduced and their ability to support
CC       germ cell development is also affected (PubMed:11416011).
CC       {ECO:0000269|PubMed:11416011, ECO:0000269|PubMed:9020850}.
CC   -!- SIMILARITY: Belongs to the glycoprotein hormones subunit beta family.
CC       {ECO:0000305}.
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DR   EMBL; U12932; AAA92804.1; -; Genomic_DNA.
DR   EMBL; AK017593; BAB30827.1; -; mRNA.
DR   EMBL; BC061159; AAH61159.1; -; mRNA.
DR   CCDS; CCDS16504.1; -.
DR   PIR; JC4526; JC4526.
DR   RefSeq; NP_032071.1; NM_008045.3.
DR   AlphaFoldDB; Q60687; -.
DR   SMR; Q60687; -.
DR   STRING; 10090.ENSMUSP00000028533; -.
DR   GlyCosmos; Q60687; 2 sites, No reported glycans.
DR   GlyGen; Q60687; 2 sites.
DR   PhosphoSitePlus; Q60687; -.
DR   PaxDb; 10090-ENSMUSP00000028533; -.
DR   Antibodypedia; 12775; 1102 antibodies from 38 providers.
DR   DNASU; 14308; -.
DR   Ensembl; ENSMUST00000028533.7; ENSMUSP00000028533.7; ENSMUSG00000027120.7.
DR   GeneID; 14308; -.
DR   KEGG; mmu:14308; -.
DR   UCSC; uc008llt.1; mouse.
DR   AGR; MGI:95582; -.
DR   CTD; 2488; -.
DR   MGI; MGI:95582; Fshb.
DR   VEuPathDB; HostDB:ENSMUSG00000027120; -.
DR   eggNOG; ENOG502S39C; Eukaryota.
DR   GeneTree; ENSGT00940000160051; -.
DR   HOGENOM; CLU_126319_3_0_1; -.
DR   InParanoid; Q60687; -.
DR   OMA; LCWKAIC; -.
DR   OrthoDB; 5353873at2759; -.
DR   PhylomeDB; Q60687; -.
DR   TreeFam; TF332940; -.
DR   Reactome; R-MMU-209822; Glycoprotein hormones.
DR   Reactome; R-MMU-375281; Hormone ligand-binding receptors.
DR   Reactome; R-MMU-418555; G alpha (s) signalling events.
DR   BioGRID-ORCS; 14308; 1 hit in 77 CRISPR screens.
DR   PRO; PR:Q60687; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q60687; Protein.
DR   Bgee; ENSMUSG00000027120; Expressed in pituitary gland and 10 other cell types or tissues.
DR   ExpressionAtlas; Q60687; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
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; IMP:MGI.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0001541; P:ovarian follicle development; IMP:MGI.
DR   GO; GO:0045780; P:positive regulation of bone resorption; IMP:MGI.
DR   GO; GO:0010628; P:positive regulation of gene expression; IDA:MGI.
DR   GO; GO:0010893; P:positive regulation of steroid biosynthetic process; ISO:MGI.
DR   GO; GO:0045670; P:regulation of osteoclast differentiation; IMP:MGI.
DR   GO; GO:0010469; P:regulation of signaling receptor activity; ISS:UniProtKB.
DR   GO; GO:0060011; P:Sertoli cell proliferation; IMP:MGI.
DR   GO; GO:0007283; P:spermatogenesis; IGI:MGI.
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; Cystine-knot cytokines; 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:SF17; FOLLITROPIN SUBUNIT BETA; 1.
DR   PANTHER; PTHR11515; GLYCOPROTEIN HORMONE BETA CHAIN; 1.
DR   Pfam; PF00007; Cys_knot; 1.
DR   SMART; SM00068; GHB; 1.
DR   SUPFAM; SSF57501; Cystine-knot cytokines; 1.
DR   PROSITE; PS00261; GLYCO_HORMONE_BETA_1; 1.
DR   PROSITE; PS00689; GLYCO_HORMONE_BETA_2; 1.
DR   Genevisible; Q60687; MM.
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..130
FT                   /note="Follitropin subunit beta"
FT                   /id="PRO_0000011713"
FT   CARBOHYD        26
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:P01225"
FT   CARBOHYD        43
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:P01225"
FT   DISULFID        22..70
FT                   /evidence="ECO:0000250|UniProtKB:P01225"
FT   DISULFID        36..85
FT                   /evidence="ECO:0000250|UniProtKB:P01225"
FT   DISULFID        39..123
FT                   /evidence="ECO:0000250|UniProtKB:P01225"
FT   DISULFID        47..101
FT                   /evidence="ECO:0000250|UniProtKB:P01225"
FT   DISULFID        51..103
FT                   /evidence="ECO:0000250|UniProtKB:P01225"
FT   DISULFID        106..113
FT                   /evidence="ECO:0000250|UniProtKB:P01225"
SQ   SEQUENCE   130 AA;  14919 MW;  7F9C28C2E34AC161 CRC64;
     MMKLIQLCIL FWCWRAICCH SCELTNITIS VEKEECRFCI SINTTWCAGY CYTRDLVYKD
     PARPNTQKVC TFKELVYETV RLPGCARHSD SLYTYPVATE CHCGKCDSDS TDCTVRGLGP
     SYCSFSEMKE
//