LSHB_SHEEP
ID LSHB_SHEEP Reviewed; 141 AA.
AC P01231;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 3.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=Lutropin subunit beta;
DE Short=Lutropin beta chain;
DE AltName: Full=Interstitial cell-stimulating hormone;
DE AltName: Full=Luteinizing hormone subunit beta;
DE Short=LH-B;
DE Short=LSH-B;
DE Short=LSH-beta;
DE Contains:
DE RecName: Full=LH beta-1;
DE Contains:
DE RecName: Full=LH beta-2;
DE Contains:
DE RecName: Full=LH beta-3;
DE Flags: Precursor;
GN Name=LHB;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=8349025; DOI=10.1016/0303-7207(93)90119-5;
RA Brown P., McNeilly J.R., Wallace R.M., McNeilly A.S., Clark A.J.;
RT "Characterization of the ovine LH beta-subunit gene: the promoter directs
RT gonadotrope-specific expression in transgenic mice.";
RL Mol. Cell. Endocrinol. 93:157-165(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pituitary;
RX PubMed=2336396; DOI=10.1093/nar/18.8.2175;
RA D'Angelo-Bernard G., Moumni M., Jutisz M., Counis R.;
RT "Cloning and sequence analysis of the cDNA for the precursor of the beta
RT subunit of ovine luteinizing hormone.";
RL Nucleic Acids Res. 18:2175-2175(1990).
RN [3]
RP PROTEIN SEQUENCE OF 21-139.
RX PubMed=4556309; DOI=10.1016/s0021-9258(19)45083-7;
RA Liu W.-K., Nahm H.S., Sweeney C.M., Holcomb G.N., Ward D.N.;
RT "The primary structure of ovine luteinizing hormone. II. The amino acid
RT sequence of the reduced, S-carboxymethylated A-subunit (LH-beta).";
RL J. Biol. Chem. 247:4365-4381(1972).
RN [4]
RP PROTEIN SEQUENCE OF 21-139.
RX PubMed=4575435; DOI=10.1016/0003-9861(72)90375-x;
RA Sairam M.R., Samy T.S.A., Papkoff H., Li C.H.;
RT "The primary structure of ovine interstitial cell-stimulating hormone. II.
RT The beta-subunit.";
RL Arch. Biochem. Biophys. 153:572-586(1972).
RN [5]
RP PROTEIN SEQUENCE OF 21-49; 64-82; 84-106 AND 115-138, FUNCTION, AND
RP SUBUNIT.
RX PubMed=2456202; DOI=10.1210/endo-123-2-700;
RA Nomura K., Tsunasawa S., Ohmura K., Sakiyama F., Shizume K.;
RT "Renotropic activity in ovine luteinizing hormone isoform(s).";
RL Endocrinology 123:700-712(1988).
RN [6]
RP PRELIMINARY ASSIGNMENT OF DISULFIDE BONDS.
RX PubMed=1201911; DOI=10.1111/j.1399-3011.1975.tb02470.x;
RA Chung D., Sairam M.R., Li C.H.;
RT "The primary structure of ovine interstitial cell stimulating hormone. IV:
RT disulfide bridges of the beta subunit.";
RL Int. J. Pept. Protein Res. 7:487-493(1975).
RN [7]
RP STRUCTURE OF CARBOHYDRATE.
RX PubMed=2209620; DOI=10.1111/j.1432-1033.1990.tb19285.x;
RA Weisshaar G., Hiyama J., Renwick A.G.C.;
RT "Site-specific N-glycosylation of ovine lutropin. Structural analysis by
RT one- and two-dimensional 1H-NMR spectroscopy.";
RL Eur. J. Biochem. 192:741-751(1990).
CC -!- FUNCTION: Promotes spermatogenesis and ovulation by stimulating the
CC testes and ovaries to synthesize steroids. The LH alpha 3/LH beta 3
CC heterodimer was shown to have potent renotropic and weak gonadotropic
CC activity. {ECO:0000269|PubMed:2456202}.
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. The beta chain can also be formed by LH
CC beta 1, LH beta 2 and LH beta 3. {ECO:0000269|PubMed:2456202}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the glycoprotein hormones subunit beta family.
CC {ECO:0000305}.
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DR EMBL; S64695; AAB27819.1; -; Genomic_DNA.
DR EMBL; X52488; CAA36729.1; -; mRNA.
DR PIR; I46949; UTSHB.
DR RefSeq; NP_001009380.1; NM_001009380.1.
DR AlphaFoldDB; P01231; -.
DR SMR; P01231; -.
DR STRING; 9940.ENSOARP00000013484; -.
DR GlyConnect; 348; 3 N-Linked glycans.
DR GlyConnect; 352; 5 N-Linked glycans (1 site).
DR PRIDE; P01231; -.
DR GeneID; 443395; -.
DR KEGG; oas:443395; -.
DR CTD; 3972; -.
DR eggNOG; ENOG502S49V; Eukaryota.
DR OrthoDB; 1362225at2759; -.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0035938; P:estradiol secretion; IMP: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 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hormone;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:2456202,
FT ECO:0000269|PubMed:4556309, ECO:0000269|PubMed:4575435"
FT CHAIN 21..141
FT /note="Lutropin subunit beta"
FT /evidence="ECO:0000269|PubMed:4556309"
FT /id="PRO_0000011734"
FT CHAIN 21..139
FT /note="LH beta-3"
FT /id="PRO_0000011735"
FT CHAIN 21..138
FT /note="LH beta-2"
FT /id="PRO_0000011736"
FT CHAIN 21..137
FT /note="LH beta-1"
FT /id="PRO_0000011737"
FT MOD_RES 21
FT /note="Blocked amino end (Ser)"
FT /evidence="ECO:0000269|PubMed:4556309"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:4556309"
FT /id="CAR_000046"
FT DISULFID 29..77
FT /evidence="ECO:0000250"
FT DISULFID 43..92
FT DISULFID 46..130
FT DISULFID 54..108
FT /evidence="ECO:0000250"
FT DISULFID 58..110
FT /evidence="ECO:0000250"
FT DISULFID 113..120
FT VARIANT 138..141
FT /note="Missing (in some molecules)"
FT CONFLICT 30
FT /note="Q -> E (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="K -> N (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="L -> P (in Ref. 1; AAB27819)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="R -> Q (in Ref. 2; CAA36729)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="P -> PP (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="Y -> V (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="E -> Q (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 122..123
FT /note="GP -> PG (in Ref. 3; AA sequence, 4; AA sequence and
FT 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="Q -> E (in Ref. 3; AA sequence and 4; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 141 AA; 15184 MW; C59EC7C0AA55A9DC CRC64;
MEMLQGLLLW LLLGVAGVWA SRGPLRPLCQ PINATLAAEK EACPVCITFT TSICAGYCLS
MKRVLPVILP PMPQRVCTYH ELRFASVRLP GCPPGVDPMV SFPVALSCHC GPCRLSSTDC
GGPRTQPLAC DHPPLPDILF L
