ID   LSHB_EQUQB              Reviewed;         169 AA.
AC   O46641;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Lutropin/choriogonadotropin subunit beta;
DE   AltName: Full=LSH-B/CG-B;
DE   AltName: Full=Luteinizing hormone subunit beta;
DE   AltName: Full=Lutropin/choriogonadotropin beta chain;
DE   Flags: Precursor;
GN   Name=LHB;
OS   Equus quagga burchellii (Plains zebra) (Equus burchelli).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus; Equus quagga.
OX   NCBI_TaxID=89252;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pituitary;
RX   PubMed=10341734; DOI=10.1530/jrf.0.1150159;
RA   Chopineau M., Martinat N., Pourchet C., Stewart F., Combarnous Y.,
RA   Guillou F.;
RT   "Cloning, sequencing and functional expression of zebra (Equus burchelli)
RT   LH.";
RL   J. Reprod. Fertil. 115:159-166(1999).
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; Y16265; CAA76146.1; -; mRNA.
DR   AlphaFoldDB; O46641; -.
DR   SMR; O46641; -.
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..20
FT                   /evidence="ECO:0000250"
FT   CHAIN           21..169
FT                   /note="Lutropin/choriogonadotropin subunit beta"
FT                   /id="PRO_0000011723"
FT   REGION          131..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        33
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        158
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        46..130
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"
SQ   SEQUENCE   169 AA;  17824 MW;  322DF724AEAA93E9 CRC64;
     MEMLQGLLLW MLLSVGGVWA SRGPLRPLCR PINATLAAEK EACPICITFT TSICAGYCPS
     MVRVMPAALP PIPQPVCTYR ELRFASIRLP GCPPGVDPMV SFPVALSCHC GPCRLKTTDC
     GGPRDHPLAC APQASSSSKD PPSQPLTSTS TPTPGASNRS SHPLPIKTS