FSHB_MOUSE
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 03-AUG-2022, entry version 151.
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).
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 -!- 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 normaly. 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 GlyGen; Q60687; 2 sites.
DR PhosphoSitePlus; Q60687; -.
DR PaxDb; Q60687; -.
DR PRIDE; Q60687; -.
DR Antibodypedia; 12775; 995 antibodies from 38 providers.
DR DNASU; 14308; -.
DR Ensembl; ENSMUST00000028533; ENSMUSP00000028533; ENSMUSG00000027120.
DR GeneID; 14308; -.
DR KEGG; mmu:14308; -.
DR UCSC; uc008llt.1; mouse.
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; 1362225at2759; -.
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 72 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 tissues.
DR ExpressionAtlas; Q60687; baseline and differential.
DR Genevisible; Q60687; MM.
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; -; 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..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
