ID   LSHB_OSPRU              Reviewed;         138 AA.
AC   O46483;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 74.
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; Fragment;
GN   Name=LHB;
OS   Osphranter rufus (Red kangaroo) (Macropus rufus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Diprotodontia; Macropodidae; Osphranter.
OX   NCBI_TaxID=9321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pituitary;
RX   PubMed=9680384; DOI=10.1007/s003359900836;
RA   Harrison G.A., Deane E.M., Cooper D.W.;
RT   "cDNA cloning of luteinizing hormone subunits from brushtail possum and red
RT   kangaroo.";
RL   Mamm. Genome 9:638-642(1998).
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; AF017450; AAC96021.1; -; mRNA.
DR   AlphaFoldDB; O46483; -.
DR   SMR; O46483; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
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; Secreted; Signal.
FT   SIGNAL          <1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..138
FT                   /note="Lutropin subunit beta"
FT                   /id="PRO_0000011728"
FT   CARBOHYD        31
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        27..75
FT                   /evidence="ECO:0000250"
FT   DISULFID        41..90
FT                   /evidence="ECO:0000250"
FT   DISULFID        44..128
FT                   /evidence="ECO:0000250"
FT   DISULFID        52..106
FT                   /evidence="ECO:0000250"
FT   DISULFID        56..108
FT                   /evidence="ECO:0000250"
FT   DISULFID        111..118
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   138 AA;  14698 MW;  2460213836DBFA7B CRC64;
     RYQELTVLLL LLLEGGSWGA SPLRPLCRPT NATLAAESDA CPVCVTFTTT ICAGYCPSMV
     RVLPAALPPS PQLVCTYREL SFSSIRLPGC PPGVDPIFSF PVALSCSCGS CRLSHSDCGG
     PRAQPHLCTR PHLSLRLL