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LSHB_MELGA
ID   LSHB_MELGA              Reviewed;         159 AA.
AC   P45646;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 87.
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   Meleagris gallopavo (Wild turkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Meleagridinae; Meleagris.
OX   NCBI_TaxID=9103;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pituitary;
RX   PubMed=7772235; DOI=10.1677/jme.0.0140117;
RA   You S., Foster L.K., Silsby J.L., el Halawani M.E., Foster D.N.;
RT   "Sequence analysis of the turkey LH beta subunit and its regulation by
RT   gonadotrophin-releasing hormone and prolactin in cultured pituitary
RT   cells.";
RL   J. Mol. Endocrinol. 14:117-129(1995).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA74125.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; L35519; AAA74125.1; ALT_INIT; mRNA.
DR   PIR; I51373; I51373.
DR   RefSeq; NP_001290081.1; NM_001303152.1.
DR   AlphaFoldDB; P45646; -.
DR   SMR; P45646; -.
DR   GeneID; 723987; -.
DR   CTD; 3972; -.
DR   InParanoid; P45646; -.
DR   OrthoDB; 1362225at2759; -.
DR   Proteomes; UP000001645; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0035938; P:estradiol secretion; IMP:AgBase.
DR   GO; GO:0009416; P:response to light stimulus; TAS: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   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hormone; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..39
FT                   /evidence="ECO:0000255"
FT   CHAIN           40..159
FT                   /note="Lutropin subunit beta"
FT                   /id="PRO_0000011729"
FT   CARBOHYD        52
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        48..96
FT                   /evidence="ECO:0000250"
FT   DISULFID        62..111
FT                   /evidence="ECO:0000250"
FT   DISULFID        65..149
FT                   /evidence="ECO:0000250"
FT   DISULFID        73..127
FT                   /evidence="ECO:0000250"
FT   DISULFID        77..129
FT                   /evidence="ECO:0000250"
FT   DISULFID        132..139
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   159 AA;  16285 MW;  52B50C8C879653C6 CRC64;
     MGGAQVLVLM TLLGTPPVTT GTPPVVVDPS VAVVGPPLGL GGGGRPPCRP INVTVAVEKD
     ECPQCMAVTT TACGGYCRTR EPVYRSPLGR PPQSSCTYGA LRYERWALWG CPIGSDPRVL
     LPVALSCRCA RCPIATSDCT VQGLGPAFCG APGGFGIGE
 
 
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