LSHB_PHYMC
ID LSHB_PHYMC Reviewed; 118 AA.
AC P25330;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 23-FEB-2022, entry version 78.
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 Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=3771098; DOI=10.1111/j.1399-3011.1986.tb03238.x;
RA Pankov Y.A., Karasyov V.S.;
RT "Primary structure of sperm whale luteinizing hormone.";
RL Int. J. Pept. Protein Res. 28:124-129(1986).
RN [2]
RP PROTEIN SEQUENCE.
RX PubMed=6466737;
RA Pankov Y.A., Karasev V.S.;
RT "Luteinizing hormone of the sperm whale. Amino acid sequences of reduced
RT and carboxymethylated beta-subunits.";
RL Biokhimiia 49:1004-1018(1984).
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; PN0141; PN0141.
DR STRING; 9755.ENSPCTP00005012694; -.
DR iPTMnet; P25330; -.
DR Proteomes; UP000248484; Genome assembly.
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 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hormone;
KW Reference proteome; Secreted.
FT CHAIN 1..118
FT /note="Lutropin subunit beta"
FT /id="PRO_0000149041"
FT CARBOHYD 13
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:6466737"
FT DISULFID 9..57
FT /evidence="ECO:0000250"
FT DISULFID 23..72
FT /evidence="ECO:0000250"
FT DISULFID 26..110
FT /evidence="ECO:0000250"
FT DISULFID 34..88
FT /evidence="ECO:0000250"
FT DISULFID 38..90
FT /evidence="ECO:0000250"
FT DISULFID 93..100
FT /evidence="ECO:0000250"
SQ SEQUENCE 118 AA; 12412 MW; 81177A56382F15E7 CRC64;
PRGPLRPLCR PINATLAAQN ZACPVCITFT TSICAGYCPS MVRVLPAALP PVPZPVCTYR
QLRFASIRLP GCPPGVNPMV SFPVALSCHC GPCRLSSSDC GPGRAQPLAC NRSPRPGL
