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LSHB_MOUSE
ID   LSHB_MOUSE              Reviewed;         141 AA.
AC   O09108; Q60844;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   25-MAY-2022, entry version 124.
DE   RecName: Full=Lutropin subunit beta;
DE            Short=Lutropin beta chain;
DE   AltName: Full=Luteinizing hormone subunit beta;
DE            Short=LH-B;
DE            Short=LSH-B;
DE            Short=LSH-beta;
DE   Flags: Precursor;
GN   Name=Lhb;
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].
RC   STRAIN=129/Sv;
RX   PubMed=8543188; DOI=10.1016/0378-1119(96)81753-7;
RA   Kumar T.R., Matzuk M.M.;
RT   "Cloning of the mouse gonadotropin beta-subunit-encoding genes, II.
RT   Structure of the luteinizing hormone beta-subunit-encoding genes.";
RL   Gene 166:335-336(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 18-122.
RC   STRAIN=C57BL/6 X CBA; TISSUE=Pituitary anterior lobe;
RA   Brown P., Brooks J., McNeilly J.R., McNeilly A.S.;
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Promotes spermatogenesis and ovulation by stimulating the
CC       testes and ovaries to synthesize steroids.
CC   -!- SUBUNIT: Heterodimer of a common alpha chain and a unique beta chain
CC       which confers biological specificity to thyrotropin, lutropin,
CC       follitropin and gonadotropin.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the glycoprotein hormones subunit beta family.
CC       {ECO:0000305}.
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DR   EMBL; U25145; AAA92841.1; -; Genomic_DNA.
DR   EMBL; Y10418; CAA71445.1; -; mRNA.
DR   CCDS; CCDS21242.1; -.
DR   PIR; JC4527; JC4527.
DR   AlphaFoldDB; O09108; -.
DR   SMR; O09108; -.
DR   STRING; 10090.ENSMUSP00000072276; -.
DR   GlyGen; O09108; 1 site.
DR   PaxDb; O09108; -.
DR   PRIDE; O09108; -.
DR   ProteomicsDB; 293403; -.
DR   MGI; MGI:96782; Lhb.
DR   eggNOG; ENOG502S49V; Eukaryota.
DR   InParanoid; O09108; -.
DR   PhylomeDB; O09108; -.
DR   Reactome; R-MMU-193048; Androgen biosynthesis.
DR   Reactome; R-MMU-193993; Mineralocorticoid biosynthesis.
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   Reactome; R-MMU-8866910; TFAP2 (AP-2) family regulates transcription of growth factors and their receptors.
DR   Reactome; R-MMU-975578; Reactions specific to the complex N-glycan synthesis pathway.
DR   ChiTaRS; Lhb; mouse.
DR   PRO; PR:O09108; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; O09108; protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005179; F:hormone activity; ISO:MGI.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0035471; P:luteinizing hormone signaling pathway involved in ovarian follicle development; IDA:MGI.
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..141
FT                   /note="Lutropin subunit beta"
FT                   /id="PRO_0000011730"
FT   CARBOHYD        33
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        29..77
FT                   /evidence="ECO:0000250"
FT   DISULFID        43..92
FT                   /evidence="ECO:0000250"
FT   DISULFID        54..108
FT                   /evidence="ECO:0000250"
FT   DISULFID        58..110
FT                   /evidence="ECO:0000250"
FT   DISULFID        113..120
FT                   /evidence="ECO:0000250"
FT   CONFLICT        83
FT                   /note="A -> R (in Ref. 2; CAA71445)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   141 AA;  15028 MW;  5E997CABF33D90BF CRC64;
     MERLQGLLLW LLLSPSVVWA SRGPLRPLCR PVNATLAAEN EFCPVCITFT TSICAGYCPS
     MVRVLPAALP PVPQPVCTYR ELAFASVRLP GCPPGVDPIV SFPVALSCRC GPCRLSSSDC
     GGPRTQPMAC DLPHLPGLLL L
 
 
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