ID   LSHB_COTJA              Reviewed;         166 AA.
AC   P45657;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 82.
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   Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Perdicinae; Coturnix.
OX   NCBI_TaxID=93934;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7515015; DOI=10.1006/gcen.1994.1040;
RA   Ando H., Ishii S.;
RT   "Molecular cloning of complementary deoxyribonucleic acids for the
RT   pituitary glycoprotein hormone alpha-subunit and luteinizing hormone beta-
RT   subunit precursor molecules of Japanese quail (Coturnix coturnix
RT   japonica).";
RL   Gen. Comp. Endocrinol. 93:357-368(1994).
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; S70834; AAB30867.1; -; mRNA.
DR   AlphaFoldDB; P45657; -.
DR   SMR; P45657; -.
DR   Proteomes; UP000694412; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0033574; P:response to testosterone; TAS: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   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hormone; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..166
FT                   /note="Lutropin subunit beta"
FT                   /id="PRO_0000011739"
FT   CARBOHYD        60
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        56..104
FT                   /evidence="ECO:0000250"
FT   DISULFID        70..119
FT                   /evidence="ECO:0000250"
FT   DISULFID        73..157
FT                   /evidence="ECO:0000250"
FT   DISULFID        81..135
FT                   /evidence="ECO:0000250"
FT   DISULFID        85..137
FT                   /evidence="ECO:0000250"
FT   DISULFID        140..147
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   166 AA;  17030 MW;  6BF293BEC3C5FAC7 CRC64;
     MGGAQVLLLL TLLGTPLVTH GTPPLVVDPS IGSQLGLGSV LGLDLGSMGG SGRPPCRPIN
     VTVAVEKEEC PQCMAVTTTA CGGYCRTREP VYRSPLGPPP QSSCTYGALR YERWDLWGCP
     IGSDPKVILP VALSCRCARC PIATSDCTVQ GLGPAFCGAP GGFGGQ