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Reviewed, UniProtKB/Swiss-Prot P01231 (LSHB_SHEEP)

Last modified June 16, 2009. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Lutropin subunit beta
      Short name=Lutropin beta chain
Alternative name(s):
    Luteinizing hormone subunit beta
    LSH-beta
      Short name=LSH-B
      Short name=LH-B
    Interstitial cell-stimulating hormone
Cleaved into the following 3 chains:
    1- Recommended name:
            LH beta-1
    2- Recommended name:
            LH beta-2
    3- Recommended name:
            LH beta-3
Gene names
Name: LHB
OrganismOvis aries (Sheep)
Taxonomic identifier9940 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeOvis

Protein attributes

Sequence length141 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Promotes spermatogenesis and ovulation by stimulating the testes and ovaries to synthesize steroids. The LH alpha 3/LH beta 3 heterodimer was shown to have potent renotropic and weak gonadotropic activity.

Subunit structure

Heterodimer of a common alpha chain and a unique beta chain which confers biological specificity to thyrotropin, lutropin, follitropin and gonadotropin. The beta chain can also be formed by LH beta 1, LH beta 2 and LH beta 3.

Subcellular location

Secreted.

Sequence similarities

Belongs to the glycoprotein hormones subunit beta family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionHormone
   PTMDisulfide bond
Glycoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionhormone activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020
Chain21 – 141121Lutropin subunit beta Ref.3
PRO_0000011734
Chain21 – 139119LH beta-3
PRO_0000011735
Chain21 – 138118LH beta-2
PRO_0000011736
Chain21 – 137117LH beta-1
PRO_0000011737

Amino acid modifications

Modified residue211Blocked amino end (Ser) Ref.3
Glycosylation331N-linked (GlcNAc...) Ref.3
CAR_000046
Disulfide bond29 ↔ 77 By similarity
Disulfide bond43 ↔ 92
Disulfide bond46 ↔ 130
Disulfide bond54 ↔ 108 By similarity
Disulfide bond58 ↔ 110 By similarity
Disulfide bond113 ↔ 120

Natural variations

Natural variant138 – 1414Missing in some molecules.

Experimental info

Sequence conflict301Q → E AA sequence Ref.4
Sequence conflict401K → N AA sequence Ref.5
Sequence conflict591L → P in AAB27819. Ref.1
Sequence conflict631R → Q in CAA36729. Ref.2
Sequence conflict711P → PP AA sequence Ref.4
Sequence conflict791Y → V AA sequence Ref.5
Sequence conflict811E → Q AA sequence Ref.4
Sequence conflict122 – 1232GP → PG AA sequence Ref.3
Sequence conflict122 – 1232GP → PG AA sequence Ref.4
Sequence conflict122 – 1232GP → PG AA sequence Ref.5
Sequence conflict1261Q → E AA sequence Ref.3
Sequence conflict1261Q → E AA sequence Ref.4

Sequences

Sequence LengthMass (Da)Tools
P01231-1 [UniParc].

Last modified November 1, 1995. Version 3.
Checksum: C59EC7C0AA55A9DC

FASTA14115,184
        10         20         30         40         50         60 
MEMLQGLLLW LLLGVAGVWA SRGPLRPLCQ PINATLAAEK EACPVCITFT TSICAGYCLS 

        70         80         90        100        110        120 
MKRVLPVILP PMPQRVCTYH ELRFASVRLP GCPPGVDPMV SFPVALSCHC GPCRLSSTDC 

       130        140 
GGPRTQPLAC DHPPLPDILF L 

« Hide

References

[1]"Characterization of the ovine LH beta-subunit gene: the promoter directs gonadotrope-specific expression in transgenic mice."
Brown P., McNeilly J.R., Wallace R.M., McNeilly A.S., Clark A.J.
Mol. Cell. Endocrinol. 93:157-165(1993) [PubMed: 8349025] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[2]"Cloning and sequence analysis of the cDNA for the precursor of the beta subunit of ovine luteinizing hormone."
D'Angelo-Bernard G., Moumni M., Jutisz M., Counis R.
Nucleic Acids Res. 18:2175-2175(1990) [PubMed: 2336396] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Pituitary.
[3]"The primary structure of ovine luteinizing hormone. II. The amino acid sequence of the reduced, S-carboxymethylated A-subunit (LH-beta)."
Liu W.-K., Nahm H.S., Sweeney C.M., Holcomb G.N., Ward D.N.
J. Biol. Chem. 247:4365-4381(1972) [PubMed: 4556309] [Abstract]
Cited for: PROTEIN SEQUENCE OF 21-139.
[4]"The primary structure of ovine interstitial cell-stimulating hormone. II. The beta-subunit."
Sairam M.R., Samy T.S.A., Papkoff H., Li C.H.
Arch. Biochem. Biophys. 153:572-586(1972) [PubMed: 4575435] [Abstract]
Cited for: PROTEIN SEQUENCE OF 21-139.
[5]"Renotropic activity in ovine luteinizing hormone isoform(s)."
Nomura K., Tsunasawa S., Ohmura K., Sakiyama F., Shizume K.
Endocrinology 123:700-712(1988) [PubMed: 2456202] [Abstract]
Cited for: PROTEIN SEQUENCE OF 21-49; 64-82; 84-106 AND 115-138, FUNCTION, SUBUNIT.
[6]"The primary structure of ovine interstitial cell stimulating hormone. IV: disulfide bridges of the beta subunit."
Chung D., Sairam M.R., Li C.H.
Int. J. Pept. Protein Res. 7:487-493(1975) [PubMed: 1201911] [Abstract]
Cited for: PRELIMINARY ASSIGNMENT OF DISULFIDE BONDS.
[7]"Site-specific N-glycosylation of ovine lutropin. Structural analysis by one- and two-dimensional 1H-NMR spectroscopy."
Weisshaar G., Hiyama J., Renwick A.G.C.
Eur. J. Biochem. 192:741-751(1990) [PubMed: 2209620] [Abstract]
Cited for: STRUCTURE OF CARBOHYDRATE.

Cross-references

Sequence databases

S64695 Genomic DNA. Translation: AAB27819.1.
X52488 mRNA. Translation: CAA36729.1.
PIRUTSHB. I46949.
RefSeqNP_001009380.1.
UniGeneOar.442

3D structure databases

HSSPHSSP built from PDB template 1HCN based on UniProtKB P01233.
ModBaseSearch...

PTM databases

GlycoSuiteDBP01231.

Genome annotation databases

GeneID443395.

Phylogenomic databases

HOVERGENP01231.

Family and domain databases

InterProIPR006208. Cys_knot.
IPR001545. Gonadotropin_bsu.
IPR018245. Gonadotropin_bsu_CS.
[Graphical view]
PANTHERPTHR11515. Gly_hormoneB. 1 hit.
PfamPF00007. Cys_knot. 1 hit.
[Graphical view]
SMARTSM00068. GHB. 1 hit.
[Graphical view]
PROSITEPS00261. GLYCO_HORMONE_BETA_1. 1 hit.
PS00689. GLYCO_HORMONE_BETA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLSHB_SHEEP
AccessionPrimary (citable) accession number: P01231
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1995
Last modified: June 16, 2009
This is version 80 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents