LSHB_PANTA
ID LSHB_PANTA Reviewed; 142 AA.
AC Q9BDI9;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 62.
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 Panthera tigris altaica (Siberian tiger).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Pantherinae;
OC Panthera.
OX NCBI_TaxID=74533;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pituitary;
RX PubMed=12493701; DOI=10.1095/biolreprod.101.002204;
RA Crichton E.G., Bedows E., Miller-Lindholm A.K., Baldwin D.M.,
RA Armstrong D.L., Graham L.H., Ford J.J., Gjorret J.O., Hyttel P., Pope C.E.,
RA Vajta G., Loskutoff N.M.;
RT "Efficacy of porcine gonadotropins for repeated stimulation of ovarian
RT activity for oocyte retrieval and in vitro embryo production and
RT cryopreservation in Siberian tigers (Panthera tigris altaica).";
RL Biol. Reprod. 68:105-113(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pituitary;
RA Liao M., Zhu M., Zhang A.;
RT "Cloning of follicle-stimulating hormone (FSH) and luteinizing hormone (LH)
RT genes in Panthera tigris altaica.";
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Promotes spermatogenesis and ovulation by stimulating the
CC testes and ovaries to synthesize steroids. {ECO:0000250}.
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the glycoprotein hormones subunit beta family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF354938; AAK30589.1; -; mRNA.
DR EMBL; AF540935; AAN28376.1; -; mRNA.
DR AlphaFoldDB; Q9BDI9; -.
DR SMR; Q9BDI9; -.
DR Proteomes; UP000675900; Unplaced.
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; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..142
FT /note="Lutropin subunit beta"
FT /id="PRO_0000042867"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 30..78
FT /evidence="ECO:0000250"
FT DISULFID 44..93
FT /evidence="ECO:0000250"
FT DISULFID 47..131
FT /evidence="ECO:0000250"
FT DISULFID 55..109
FT /evidence="ECO:0000250"
FT DISULFID 59..111
FT /evidence="ECO:0000250"
FT DISULFID 114..121
FT /evidence="ECO:0000250"
SQ SEQUENCE 142 AA; 15117 MW; 234986A0271943DB CRC64;
MEMLQGLLLL WLLLNVGGVW TSRGPLRPLC RPINATLAAE NEACPVCVTF TTTICAGYCP
SMMRVLPAAL PPVPQPVCTY RELRFASVRL PGCPPGVDPV VSFPVALSCR CGPCRLSSSD
CGGPRAQPLA CDRPPLPGLP FL
