ID   LSHB_PHOSU              Reviewed;         128 AA.
AC   Q9QYA9;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 72.
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   Phodopus sungorus (Striped hairy-footed hamster) (Djungarian hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Phodopus.
OX   NCBI_TaxID=10044;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10611080; DOI=10.1095/biolreprod62.1.155;
RA   Bernard D.J., Merzlyak I.Y., Horton T.H., Turek F.W.;
RT   "Differential regulation of pituitary gonadotropin subunit messenger
RT   ribonucleic acid levels in photostimulated Siberian hamsters.";
RL   Biol. Reprod. 62:155-161(2000).
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; AF106915; AAF15966.1; -; mRNA.
DR   AlphaFoldDB; Q9QYA9; -.
DR   SMR; Q9QYA9; -.
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.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hormone; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000250"
FT   CHAIN           21..>128
FT                   /note="Lutropin subunit beta"
FT                   /id="PRO_0000011731"
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   NON_TER         128
SQ   SEQUENCE   128 AA;  13660 MW;  BBF9F655E8E08625 CRC64;
     MERLQGLLLW LLLSPSVVWA SRGPLRPLCR PVNATLAAEN EACPVCITFS TSICAGYCPS
     MVRVLPAALP PVPQPVCTYH ELHFASVRLP GCPPGVDPMV SFPVALSCRC GPCRLSTSDC
     GGPRTQPM