ID   LSHB_STRCA              Reviewed;         128 AA.
AC   P80664;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 77.
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;
GN   Name=LHB;
OS   Struthio camelus (Common ostrich).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC   Struthio.
OX   NCBI_TaxID=8801;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=8925835; DOI=10.1111/j.1432-1033.1996.0262h.x;
RA   Koide Y., Papkoff H., Kawauchi H.;
RT   "Complete amino acid sequences of follitropin and lutropin in the ostrich,
RT   Struthio camelus.";
RL   Eur. J. Biochem. 240:262-267(1996).
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   PIR; S74085; S74085.
DR   AlphaFoldDB; P80664; -.
DR   SMR; P80664; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0035938; P:estradiol secretion; IMP:AgBase.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Hormone; Secreted.
FT   CHAIN           1..128
FT                   /note="Lutropin subunit beta"
FT                   /id="PRO_0000149042"
FT   CARBOHYD        22
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        18..66
FT                   /evidence="ECO:0000250"
FT   DISULFID        32..81
FT                   /evidence="ECO:0000250"
FT   DISULFID        35..119
FT                   /evidence="ECO:0000250"
FT   DISULFID        43..97
FT                   /evidence="ECO:0000250"
FT   DISULFID        47..99
FT                   /evidence="ECO:0000250"
FT   DISULFID        102..109
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   128 AA;  12856 MW;  5EA6B1DB9FF908F6 CRC64;
     VPLGVPVALG VPPSRPPCRP VNVTVAAEKD ECPQCLAVTT TACGGYCRTR EPVYRSPLGG
     PAQQACGYGA LRYERLALPG CAPGADPTVA VPVALSCRCA RCPMATADCT VAGLGPAFCG
     APAGFGPQ