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LSHB_LITCT
ID   LSHB_LITCT              Reviewed;         112 AA.
AC   P80071;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   25-MAY-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;
GN   Name=lhb;
OS   Lithobates catesbeianus (American bullfrog) (Rana catesbeiana).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX   NCBI_TaxID=8400;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=1555571; DOI=10.1111/j.1432-1033.1992.tb16756.x;
RA   Hiroaki H., Tomoko H., Yoichi H.;
RT   "Amphibian lutropin from the bullfrog Rana catesbeiana. Complete amino acid
RT   sequence of the beta subunit.";
RL   Eur. J. Biochem. 205:105-110(1992).
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   PIR; S21196; S21196.
DR   AlphaFoldDB; P80071; -.
DR   SMR; P80071; -.
DR   GlyConnect; 351; 1 N-Linked glycan (1 site).
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; Secreted.
FT   CHAIN           1..112
FT                   /note="Lutropin subunit beta"
FT                   /id="PRO_0000149043"
FT   CARBOHYD        8
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /id="CAR_000047"
FT   DISULFID        4..52
FT                   /evidence="ECO:0000250"
FT   DISULFID        18..67
FT                   /evidence="ECO:0000250"
FT   DISULFID        21..105
FT                   /evidence="ECO:0000250"
FT   DISULFID        29..83
FT                   /evidence="ECO:0000250"
FT   DISULFID        33..85
FT                   /evidence="ECO:0000250"
FT   DISULFID        88..95
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   112 AA;  12676 MW;  3DF55E5CD91D1071 CRC64;
     RHVCHLANAT ISAEKDHCPV CITFTTSICT GYCQTMDPVY KTALSSFKQN ICTYKEIRYD
     TIKLPDCLPG TDPFFTYPVA LSCYCDLCKM DYSDCTVESS EPDVCMKRRI SI
 
 
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