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UniProtKB/Swiss-Prot entry P01229


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name LSHB_HUMAN
Primary accession number P01229
Secondary accession numbers None
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on November 1, 1995 (Sequence version 3)
Annotations were last modified on    June 16, 2009 (Entry version 103)
Name and origin of the protein
Protein name Lutropin subunit beta [Precursor]
Synonyms Lutropin beta chain
Luteinizing hormone subunit beta
LSH-beta
LSH-B
LH-B
Gene name
Name: LHB
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1038/307037a0; PubMed=6690982 [NCBI, ExPASy, EBI, Israel, Japan]
Talmadge K., Vamvakopoulos N.C., Fiddes J.C.;
"Evolution of the genes for the beta subunits of human chorionic gonadotropin and luteinizing hormone.";
Nature 307:37-40(1984).
[2]
PROTEIN SEQUENCE OF 21-141.
PubMed=1191677 [NCBI, ExPASy, EBI, Israel, Japan]
Sairam M.R., Li C.H.;
"Human pituitary lutropin. Isolation, properties, and the complete amino acid sequence of the beta-subunit.";
Biochim. Biophys. Acta 412:70-81(1975).
[3]
PRELIMINARY PROTEIN SEQUENCE OF 21-141.
PubMed=4685398 [NCBI, ExPASy, EBI, Israel, Japan]
Shome B., Parlow A.F.;
"The primary structure of the hormone-specific, beta subunit of human pituitary luteinizing hormone (hLH).";
J. Clin. Endocrinol. Metab. 36:618-621(1973).
[4]
PRELIMINARY PARTIAL PROTEIN SEQUENCE.
DOI=10.1016/0014-5793(73)80534-4; PubMed=4719207 [NCBI, ExPASy, EBI, Israel, Japan]
Closset J., Hennen G., Lequin R.M.;
"Human luteinizing hormone. The amino acid sequence of the subunit.";
FEBS Lett. 29:97-100(1973).
[5]
STRUCTURE OF CARBOHYDRATE.
DOI=10.1111/j.1432-1033.1991.tb15702.x; PubMed=1991473 [NCBI, ExPASy, EBI, Israel, Japan]
Weisshaar G., Hiyama J., Renwick A.G.C., Nimtz M.;
"NMR investigations of the N-linked oligosaccharides at individual glycosylation sites of human lutropin.";
Eur. J. Biochem. 195:257-268(1991).
[6]
STRUCTURE BY NMR OF 58-77.
DOI=10.1210/me.6.6.904; PubMed=1495492 [NCBI, ExPASy, EBI, Israel, Japan]
Keutmann H.T., Hua Q.-X., Weiss M.A.;
"Structure of a receptor-binding fragment from human luteinizing hormone beta-subunit determined by [1H]- and [15N]nuclear magnetic resonance spectroscopy.";
Mol. Endocrinol. 6:904-913(1992).
[7]
VARIANT HYPOGONADISM ARG-74.
PubMed=1727547 [NCBI, ExPASy, EBI, Israel, Japan]
Weiss J., Axelrod L., Whitcomb R.W., Harris P.E., Crowley W.F. Jr., Jameson J.L.;
"Hypogonadism caused by a single amino acid substitution in the beta subunit of luteinizing hormone.";
N. Engl. J. Med. 326:179-183(1992).
[8]
VARIANT SER-122.
DOI=10.1016/S0015-0282(97)00445-7; PubMed=9457942 [NCBI, ExPASy, EBI, Israel, Japan]
Liao W.X., Roy A.C., Chan C., Arulkumaran S., Ratnam S.S.;
"A new molecular variant of luteinizing hormone associated with female infertility.";
Fertil. Steril. 69:102-106(1998).
[9]
VARIANTS ARG-28 AND THR-35.
DOI=10.1093/humrep/13.12.3338; PubMed=9886510 [NCBI, ExPASy, EBI, Israel, Japan]
Takahashi K., Kurioka H., Ozaki T., Kanasaki H., Kohsaka M., Miyazaki K., Karino K.;
"Increased prevalence of luteinizing hormone beta-subunit variant in Japanese infertility patients.";
Hum. Reprod. 13:3338-3344(1998).
[10]
VARIANT THR-18.
DOI=10.1093/molehr/8.3.201; PubMed=11870227 [NCBI, ExPASy, EBI, Israel, Japan]
Jiang M., Lamminen T., Pakarinen P., Hellman J., Manna P., Herrera R.J., Huhtaniemi I.;
"A novel Ala(-3)Thr mutation in the signal peptide of human luteinizing hormone beta-subunit: potentiation of the inositol phosphate signalling pathway and attenuation of the adenylate cyclase pathway by recombinant variant hormone.";
Mol. Hum. Reprod. 8:201-212(2002).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X00264; CAA25067.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S71273; AAD14960.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00000854; -.
PIR I37994; UTHUB.
RefSeq NP_000885.1; -.
UniGene Hs.154704
3D structure databases
PDB
1M92; Model; -; A=1-141.[ExPASy / RCSB / EBI]
PDBsum 1M92; -.
SMR P01229; 22-131.
ModBase P01229.
PTM databases
GlycoSuiteDB P01229; -.
Organism-specific databases
GeneCards GC19M054211; -.
H-InvDB HIX0040153; -.
HGNC HGNC:6584; LHB.
GenAtlas LHB.
MIM 152780; gene+phenotype. [NCBI / EBI]
Orphanet 755; Leydig cell hypoplasia.
PharmGKB PA30356; -.
Gene expression databases
ArrayExpress P01229; -.
Bgee P01229; -.
CleanEx HS_LHB; -.
GermOnline ENSG00000104826; Homo sapiens.
Ontologies
GO
GO:0005576; Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005625; Cellular component: soluble fraction (traceable author statement from ProtInc).
GO:0005179; Molecular function: hormone activity (inferred from electronic annotation from UniProtKB-KW).
GO:0007267; Biological process: cell-cell signaling (traceable author statement from ProtInc).
GO:0008584; Biological process: male gonad development (traceable author statement from ProtInc).
GO:0006701; Biological process: progesterone biosynthetic process (traceable author statement from UniProtKB).
GO:0007530; Biological process: sex determination (inferred from electronic annotation from UniProtKB-KW).
GO:0007165; Biological process: signal transduction (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR006208; Cys_knot.
IPR001545; Gonadotropin_bsu.
IPR018245; Gonadotropin_bsu_CS.
Graphical view of domain structure.
PANTHER PTHR11515; Gly_hormoneB; 1.
Pfam PF00007; Cys_knot; 1.
Pfam graphical view of domain structure.
SMART SM00068; GHB; 1.
SMART graphical view of domain structure.
PROSITE PS00261; GLYCO_HORMONE_BETA_1; 1.
PS00689; GLYCO_HORMONE_BETA_2; 1.
Proteomic databases
PRIDE P01229; -.
Genome annotation databases
Ensembl ENSG00000104826; Homo sapiens. [Contig view]
GeneID 3972; -.
KEGG hsa:3972; -.
Phylogenomic databases
HOGENOM P01229; -.
HOVERGEN P01229; -.
OMA P01229; LSCRCGP.
Other
DrugBank DB00044; Lutropin alfa.
DB00032; Menotropins.
NextBio 15570; -.
SOURCE LHB; Homo sapiens.
ProtoNet P01229.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Direct protein sequencing; Disease mutation; Disulfide bond; Glycoprotein; Hormone; Polymorphism; Pseudohermaphroditism; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    20  20      
CHAIN   21   141  121     Lutropin subunit beta. PRO_0000011726
CARBOHYD   50    50        N-linked (GlcNAc...) [GlycoSuiteDB]. CAR_000045
DISULFID   29    77        By similarity. 
DISULFID   43    92        By similarity. 
DISULFID   46   130        By similarity. 
DISULFID   54   108        By similarity. 
DISULFID   58   110        By similarity. 
DISULFID   113   120        By similarity. 
VARIANT   15    15  1     M -> I (in dbSNP:rs34247911 [NCBI]). VAR_034098 
VARIANT   18    18  1     A -> T (more effective in stimulating IP3 but not cAMP production; dbSNP:rs5030775 [NCBI]). VAR_015672 
VARIANT   28    28  1     W -> R (in dbSNP:rs1800447 [NCBI]). VAR_014589 
VARIANT   35    35  1     I -> T (in dbSNP:rs34349826 [NCBI]). VAR_014590 
VARIANT   74    74  1     Q -> R (in hypogonadism; lack of receptor-binding; dbSNP:rs5030773 [NCBI]). VAR_003189 
VARIANT   122   122  1     G -> S (may be implicated in female infertility; dbSNP:rs5030774 [NCBI]). VAR_015673 
CONFLICT   39    39        E -> Q (in Ref. 2; AA sequence). 
CONFLICT   76    76        Missing (in Ref. 2; AA sequence). 
CONFLICT   132   135        HPQL -> PQH (in Ref. 2; AA sequence). 
STRAND   21    23  3      
STRAND   28    38  11      
STRAND   47    55  9      
STRAND   75    88  14      
STRAND   99   112  14      
TURN   115   117  3      
Sequence information
Length: 141 AA [This is the length of the unprocessed precursor] Molecular weight: 15345 Da [This is the MW of the unprocessed precursor] CRC64: E411766253113F7C [This is a checksum on the sequence]
        10         20         30         40         50         60 
MEMLQGLLLL LLLSMGGAWA SREPLRPWCH PINAILAVEK EGCPVCITVN TTICAGYCPT 

        70         80         90        100        110        120 
MMRVLQAVLP PLPQVVCTYR DVRFESIRLP GCPRGVDPVV SFPVALSCRC GPCRRSTSDC 

       130        140 
GGPKDHPLTC DHPQLSGLLF L 

P01229 in FASTA format

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