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LSHB_PANTR
ID   LSHB_PANTR              Reviewed;         141 AA.
AC   Q2Q1P2;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 80.
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   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Hallast P., Rull K., Laan M.;
RT   "What is the evidence for the functionality of CGB1 and CGB2?";
RL   Submitted (OCT-2005) 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}.
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DR   EMBL; DQ238551; ABB83544.1; -; Genomic_DNA.
DR   RefSeq; NP_001065271.1; NM_001071803.1.
DR   AlphaFoldDB; Q2Q1P2; -.
DR   SMR; Q2Q1P2; -.
DR   STRING; 9598.ENSPTRP00000019333; -.
DR   PaxDb; Q2Q1P2; -.
DR   Ensembl; ENSPTRT00000020941; ENSPTRP00000019333; ENSPTRG00000011271.
DR   GeneID; 468950; -.
DR   KEGG; ptr:468950; -.
DR   CTD; 3972; -.
DR   VGNC; VGNC:2324; LHB.
DR   eggNOG; ENOG502S49V; Eukaryota.
DR   GeneTree; ENSGT00940000163162; -.
DR   InParanoid; Q2Q1P2; -.
DR   OMA; NSICAGY; -.
DR   Proteomes; UP000002277; Chromosome 19.
DR   Bgee; ENSPTRG00000011271; Expressed in pituitary gland and 13 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Hormone; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000250"
FT   CHAIN           21..141
FT                   /note="Lutropin subunit beta"
FT                   /id="PRO_0000226051"
FT   CARBOHYD        33
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        50
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"
SQ   SEQUENCE   141 AA;  15333 MW;  26585DF3F19B17DE CRC64;
     MEMLQGLLLL LLLSMGGAWA SREPLRPWCH PINATLAVEK EGCPVCITVN TTICAGYCPT
     MMRVLQAVLP PLPQVVCTYR DVRFESIRLP GCPRGVDPVV SFPVALSCRC GPCRRSTSDC
     GGPKDHPLTC DHPQLSGLLF L
 
 
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