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LSHB_HORSE
ID   LSHB_HORSE              Reviewed;         169 AA.
AC   P08751; P01234;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 2.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Lutropin/choriogonadotropin subunit beta;
DE   AltName: Full=LSH-B/CG-B;
DE   AltName: Full=Luteinizing hormone subunit beta;
DE   AltName: Full=Lutropin/choriogonadotropin beta chain;
DE   Flags: Precursor;
GN   Name=LHB;
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1379674; DOI=10.1210/mend.6.6.1379674;
RA   Sherman G.B., Wolfe M.W., Farmerie T.A., Clay C.M., Threadgill D.S.,
RA   Sharp D.C., Nilson J.H.;
RT   "A single gene encodes the beta-subunits of equine luteinizing hormone and
RT   chorionic gonadotropin.";
RL   Mol. Endocrinol. 6:951-959(1992).
RN   [2]
RP   PROTEIN SEQUENCE OF 21-169.
RX   PubMed=3298239; DOI=10.1016/s0021-9258(18)47457-1;
RA   Bousfield G.R., Liu W.-K., Sugino H., Ward D.N.;
RT   "Structural studies on equine glycoprotein hormones. Amino acid sequence of
RT   equine lutropin beta-subunit.";
RL   J. Biol. Chem. 262:8610-8620(1987).
RN   [3]
RP   PROTEIN SEQUENCE OF 21-169.
RX   PubMed=3298238; DOI=10.1016/s0021-9258(18)47456-x;
RA   Sugino H., Bousfield G.R., Moore W.T. Jr., Ward D.N.;
RT   "Structural studies on equine glycoprotein hormones. Amino acid sequence of
RT   equine chorionic gonadotropin beta-subunit.";
RL   J. Biol. Chem. 262:8603-8609(1987).
RN   [4]
RP   PARTIAL PROTEIN SEQUENCE.
RA   Ward D.N., Moore W.T. Jr., Burleigh B.D.;
RT   "Structural studies on equine chorionic gonadotropin.";
RL   J. Protein Chem. 1:263-280(1982).
RN   [5]
RP   STRUCTURE OF CARBOHYDRATES.
RX   PubMed=2331995; DOI=10.1111/j.1432-1033.1990.tb15474.x;
RA   Damm J.B.L., Haard K., Kamerling J.P., van Dedem G.W.K.,
RA   Vliegenthart J.F.G.;
RT   "Structure determination of the major N- and O-linked carbohydrate chains
RT   of the beta subunit from equine chorionic gonadotropin.";
RL   Eur. J. Biochem. 189:175-183(1990).
RN   [6]
RP   GLYCOSYLATION AT SER-138; SER-143; THR-147; SER-148; THR-149; SER-150;
RP   THR-151; THR-153; SER-157; SER-160; SER-161 AND SER-169.
RX   PubMed=11133668; DOI=10.1095/biolreprod64.1.136;
RA   Bousfield G.R., Butnev V.Y., Butnev V.Y.;
RT   "Identification of twelve O-glycosylation sites in equine chorionic
RT   gonadotropin beta and equine luteinizing hormone beta by solid-phase Edman
RT   degradation.";
RL   Biol. Reprod. 64:136-147(2001).
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   -!- PTM: Microheterogeneity at Asn-33. O-glycosylation appears to be
CC       responsible for the beta subunit contribution to the difference in LH-
CC       receptor binding activity between LSH-B and CG-B.
CC       {ECO:0000269|PubMed:11133668}.
CC   -!- SIMILARITY: Belongs to the glycoprotein hormones subunit beta family.
CC       {ECO:0000305}.
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DR   EMBL; S41704; AAB22775.1; -; Genomic_DNA.
DR   PIR; A41917; KTHOB.
DR   RefSeq; NP_001184022.1; NM_001197093.1.
DR   AlphaFoldDB; P08751; -.
DR   SMR; P08751; -.
DR   STRING; 9796.ENSECAP00000005559; -.
DR   GlyConnect; 90; 5 N-Linked glycans, 9 O-Linked glycans.
DR   iPTMnet; P08751; -.
DR   PaxDb; P08751; -.
DR   Ensembl; ENSECAT00000007582; ENSECAP00000005559; ENSECAG00000007548.
DR   GeneID; 100054774; -.
DR   KEGG; ecb:100054774; -.
DR   CTD; 3972; -.
DR   GeneTree; ENSGT00940000161285; -.
DR   InParanoid; P08751; -.
DR   OrthoDB; 1362225at2759; -.
DR   Proteomes; UP000002281; Chromosome 10.
DR   Bgee; ENSECAG00000007548; Expressed in trophoblast and 21 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   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Hormone;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000269|PubMed:3298238,
FT                   ECO:0000269|PubMed:3298239"
FT   CHAIN           21..169
FT                   /note="Lutropin/choriogonadotropin subunit beta"
FT                   /id="PRO_0000011725"
FT   REGION          131..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        33
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:3298238"
FT   CARBOHYD        138
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000269|PubMed:11133668"
FT   CARBOHYD        143
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000269|PubMed:11133668"
FT   CARBOHYD        147
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000269|PubMed:11133668"
FT   CARBOHYD        148
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000269|PubMed:11133668"
FT   CARBOHYD        149
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000269|PubMed:11133668"
FT   CARBOHYD        150
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000269|PubMed:11133668"
FT   CARBOHYD        151
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000269|PubMed:11133668"
FT   CARBOHYD        153
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000269|PubMed:11133668"
FT   CARBOHYD        157
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000269|PubMed:11133668"
FT   CARBOHYD        160
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000269|PubMed:11133668"
FT   CARBOHYD        161
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000269|PubMed:11133668"
FT   CARBOHYD        169
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000269|PubMed:11133668"
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   169 AA;  17865 MW;  1244ADBEB843EF1A CRC64;
     METLQGLLLW MLLSVGGVWA SRGPLRPLCR PINATLAAEK EACPICITFT TSICAGYCPS
     MVRVMPAALP AIPQPVCTYR ELRFASIRLP GCPPGVDPMV SFPVALSCHC GPCQIKTTDC
     GVFRDQPLAC APQASSSSKD PPSQPLTSTS TPTPGASRRS SHPLPIKTS
 
 
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