LSHB_BOVIN
ID LSHB_BOVIN Reviewed; 141 AA.
AC P04651;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Lutropin subunit beta;
DE AltName: Full=Luteinizing hormone subunit beta;
DE Short=LH-B;
DE Short=LSH-B;
DE Short=LSH-beta;
DE AltName: Full=Lutropin beta chain;
DE Flags: Precursor;
GN Name=LHB;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2987241; DOI=10.1016/s0021-9258(18)88889-5;
RA Virgin J.B., Silver B.J., Thomason A.R., Nilson J.H.;
RT "The gene for the beta subunit of bovine luteinizing hormone encodes a
RT gonadotropin mRNA with an unusually short 5'-untranslated region.";
RL J. Biol. Chem. 260:7072-7077(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3838746; DOI=10.1016/s0021-9258(18)89124-4;
RA Maurer R.A.;
RT "Analysis of several bovine lutropin beta subunit cDNAs reveals
RT heterogeneity in nucleotide sequence.";
RL J. Biol. Chem. 260:4684-4687(1985).
RN [3]
RP PROTEIN SEQUENCE OF 21-139.
RX PubMed=4770795; DOI=10.1111/j.1432-1033.1973.tb03121.x;
RA Maghuin-Rogister G., Hennen G.;
RT "Luteinizing hormone. The primary structures of the beta-subunit from
RT bovine and porcine species.";
RL Eur. J. Biochem. 39:235-253(1973).
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; M10077; AAA30623.1; -; mRNA.
DR EMBL; M11506; AAB59267.1; -; Genomic_DNA.
DR PIR; A92534; UTBOB.
DR RefSeq; NP_776355.1; NM_173930.1.
DR PDB; 6P57; X-ray; 3.16 A; A/B=1-141.
DR PDBsum; 6P57; -.
DR AlphaFoldDB; P04651; -.
DR SMR; P04651; -.
DR STRING; 9913.ENSBTAP00000048635; -.
DR GlyConnect; 349; 6 N-Linked glycans.
DR GlyConnect; 353; 2 N-Linked glycans (1 site).
DR PaxDb; P04651; -.
DR Ensembl; ENSBTAT00000057054; ENSBTAP00000048635; ENSBTAG00000038735.
DR GeneID; 280839; -.
DR KEGG; bta:280839; -.
DR CTD; 3972; -.
DR VEuPathDB; HostDB:ENSBTAG00000038735; -.
DR eggNOG; ENOG502S49V; Eukaryota.
DR GeneTree; ENSGT00940000161285; -.
DR HOGENOM; CLU_126319_0_0_1; -.
DR InParanoid; P04651; -.
DR OMA; GPCRLSN; -.
DR OrthoDB; 1362225at2759; -.
DR TreeFam; TF332940; -.
DR Reactome; R-BTA-193993; Mineralocorticoid biosynthesis.
DR Reactome; R-BTA-209822; Glycoprotein hormones.
DR Reactome; R-BTA-375281; Hormone ligand-binding receptors.
DR Reactome; R-BTA-8866910; TFAP2 (AP-2) family regulates transcription of growth factors and their receptors.
DR Reactome; R-BTA-975578; Reactions specific to the complex N-glycan synthesis pathway.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000038735; Expressed in adenohypophysis and 78 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
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 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hormone; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:4770795"
FT CHAIN 21..141
FT /note="Lutropin subunit beta"
FT /evidence="ECO:0000269|PubMed:4770795"
FT /id="PRO_0000011719"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /id="CAR_000044"
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"
FT CONFLICT 1..2
FT /note="Missing (in Ref. 2; AAA30623)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="Q -> E (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="P -> S (in Ref. 2; AAA30623)"
FT /evidence="ECO:0000305"
FT CONFLICT 122..123
FT /note="GP -> PG (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="Q -> E (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 29..38
FT /evidence="ECO:0007829|PDB:6P57"
FT STRAND 47..55
FT /evidence="ECO:0007829|PDB:6P57"
FT STRAND 77..88
FT /evidence="ECO:0007829|PDB:6P57"
FT STRAND 99..110
FT /evidence="ECO:0007829|PDB:6P57"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:6P57"
SQ SEQUENCE 141 AA; 15202 MW; 44FB1CBD4901BC95 CRC64;
MEMFQGLLLW LLLGVAGVWA SRGPLRPLCQ PINATLAAEK EACPVCITFT TSICAGYCPS
MKRVLPVILP PMPQRVCTYH ELRFASVRLP GCPPGVDPMV SFPVALSCHC GPCRLSSTDC
GGPRTQPLAC DHPPLPDILF L
