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LSHB_CERSI
ID   LSHB_CERSI              Reviewed;         141 AA.
AC   O77835; O19102;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 71.
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=LHB1;
GN   and
GN   Name=LHB2;
OS   Ceratotherium simum (White rhinoceros) (Square-lipped rhinoceros).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Rhinocerotidae; Ceratotherium.
OX   NCBI_TaxID=9807;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9723860; DOI=10.1677/jme.0.0210019;
RA   Lund L.A., Sherman G.B.;
RT   "Duplication of the southern white rhinoceros (Ceratotherium simum simum)
RT   luteinizing hormone beta subunit gene.";
RL   J. Mol. Endocrinol. 21:19-30(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 7-141.
RC   TISSUE=Pituitary;
RX   PubMed=9305757; DOI=10.1016/s0378-1119(97)00080-2;
RA   Sherman G.B., Lund L.A., Bunick D., Winn R.J.;
RT   "Characterization and phylogenetic significance of rhinoceros luteinizing
RT   hormone beta (LHbeta) subunit messenger RNA structure, complementary DNA
RT   sequence and gene copy number.";
RL   Gene 195:131-139(1997).
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; AF024521; AAC36049.1; -; Genomic_DNA.
DR   EMBL; AF024520; AAC36048.1; -; Genomic_DNA.
DR   EMBL; U72659; AAB71983.1; -; mRNA.
DR   AlphaFoldDB; O77835; -.
DR   SMR; O77835; -.
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   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hormone; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000250"
FT   CHAIN           21..141
FT                   /note="Lutropin subunit beta"
FT                   /id="PRO_0000011721"
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        22
FT                   /note="R -> K (in Ref. 2; AAB71983)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   141 AA;  14930 MW;  FFEDB157C51976C9 CRC64;
     MEMLQGLLLW LLLSVGGVWA SRGPLRPLCR PINATLAAEN EACPVCITFT TSICAGYCPS
     MVRVLPAALP PAPQPVCTYH ELRFASIRLP GCPPGVDPMV SFPVALSCRC GPCRLSSSDC
     GGPRAQPLAC DRPPLPGLLF L
 
 
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