LSHB_RABIT
ID LSHB_RABIT Reviewed; 141 AA.
AC Q6IY74; Q7M3C7;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=Japanese white, and New Zealand white; TISSUE=Pituitary;
RA Suzuki O.;
RT "Rabbit luteinizing hormone gene.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 19-137.
RA Glenn S.D., Nahm H.S., Ward D.N.;
RT "The amino acid sequence of the rabbit lutropin beta subunit.";
RL J. Protein Chem. 3:259-273(1984).
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}.
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DR EMBL; AB234232; BAE44302.1; -; Genomic_DNA.
DR EMBL; AB235913; BAE45120.1; -; mRNA.
DR EMBL; AY614703; AAT37165.1; -; mRNA.
DR PIR; A61465; A61465.
DR RefSeq; NP_001076164.1; NM_001082695.1.
DR AlphaFoldDB; Q6IY74; -.
DR SMR; Q6IY74; -.
DR STRING; 9986.ENSOCUP00000025405; -.
DR Ensembl; ENSOCUT00000022613; ENSOCUP00000025405; ENSOCUG00000026635.
DR GeneID; 100009427; -.
DR KEGG; ocu:100009427; -.
DR CTD; 3972; -.
DR eggNOG; ENOG502S49V; Eukaryota.
DR GeneTree; ENSGT00940000161285; -.
DR HOGENOM; CLU_126319_0_0_1; -.
DR InParanoid; Q6IY74; -.
DR OMA; GPCRLSN; -.
DR OrthoDB; 1362225at2759; -.
DR TreeFam; TF332940; -.
DR Proteomes; UP000001811; Unplaced.
DR Bgee; ENSOCUG00000026635; Expressed in skin of back and 6 other tissues.
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; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 19..141
FT /note="Lutropin subunit beta"
FT /id="PRO_0000042868"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 20..21
FT /note="AP -> PA (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="Q -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 141 AA; 14752 MW; BA531BD25AC81A2C CRC64;
MGTLQGLLLW LLLGTGGAQA PRGPLRPLCR PVNATLAAEN EACPVCITFT TSICAGYCPS
MVRVLPAALP PVPQPVCTYR ELRFASIRLP GCPPGVDPEV SFPVALSCRC GPCRLSSSDC
GGPRAQPLAC DLPHLPGLLF L
