[1]	NUCLEOTIDE SEQUENCE. DOI=10.1016/0303-7207(93)90119-5; PubMed=8349025 [NCBI, ExPASy, EBI, Israel, Japan] Brown P., McNeilly J.R., Wallace R.M., McNeilly A.S., Clark A.J.; "Characterization of the ovine LH beta-subunit gene: the promoter directs gonadotrope-specific expression in transgenic mice."; Mol. Cell. Endocrinol. 93:157-165(1993).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Pituitary; DOI=10.1093/nar/18.8.2175; PubMed=2336396 [NCBI, ExPASy, EBI, Israel, Japan] D'Angelo-Bernard G., Moumni M., Jutisz M., Counis R.; "Cloning and sequence analysis of the cDNA for the precursor of the beta subunit of ovine luteinizing hormone."; Nucleic Acids Res. 18:2175-2175(1990).
[3]	PROTEIN SEQUENCE OF 21-139. PubMed=4556309 [NCBI, ExPASy, EBI, Israel, Japan] Liu W.-K., Nahm H.S., Sweeney C.M., Holcomb G.N., Ward D.N.; "The primary structure of ovine luteinizing hormone. II. The amino acid sequence of the reduced, S-carboxymethylated A-subunit (LH-beta)."; J. Biol. Chem. 247:4365-4381(1972).
[4]	PROTEIN SEQUENCE OF 21-139. DOI=10.1016/0003-9861(72)90375-X; PubMed=4575435 [NCBI, ExPASy, EBI, Israel, Japan] Sairam M.R., Samy T.S.A., Papkoff H., Li C.H.; "The primary structure of ovine interstitial cell-stimulating hormone. II. The beta-subunit."; Arch. Biochem. Biophys. 153:572-586(1972).
[5]	PROTEIN SEQUENCE OF 21-49; 64-82; 84-106 AND 115-138, FUNCTION, AND SUBUNIT. PubMed=2456202 [NCBI, ExPASy, EBI, Israel, Japan] Nomura K., Tsunasawa S., Ohmura K., Sakiyama F., Shizume K.; "Renotropic activity in ovine luteinizing hormone isoform(s)."; Endocrinology 123:700-712(1988).
[6]	PRELIMINARY ASSIGNMENT OF DISULFIDE BONDS. PubMed=1201911 [NCBI, ExPASy, EBI, Israel, Japan] Chung D., Sairam M.R., Li C.H.; "The primary structure of ovine interstitial cell stimulating hormone. IV: disulfide bridges of the beta subunit."; Int. J. Pept. Protein Res. 7:487-493(1975).
[7]	STRUCTURE OF CARBOHYDRATE. PubMed=2209620 [NCBI, ExPASy, EBI, Israel, Japan] Weisshaar G., Hiyama J., Renwick A.G.C.; "Site-specific N-glycosylation of ovine lutropin. Structural analysis by one- and two-dimensional 1H-NMR spectroscopy."; Eur. J. Biochem. 192:741-751(1990).

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: 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.
SIMILARITY: Belongs to the glycoprotein hormones subunit beta family.

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

S64695; AAB27819.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X52488; CAA36729.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

I46949; UTSHB.

NP_001009380.1; -.

3D structure databases

HSSP

P01233; 1HCN. [HSSP ENTRY / PDB]

ModBase

P01231.

PTM databases

GlycoSuiteDB

P01231; -.

Family and domain databases

InterPro

IPR006208; Cys_knot.
IPR002400; GF_cysknot.
IPR001545; Gly_hormoneB.
Graphical view of domain structure.

PANTHER

PTHR11515; Gly_hormoneB; 1.

Pfam

PF00007; Cys_knot; 1.
Pfam graphical view of domain structure.

PRINTS

PR00438; GFCYSKNOT.

SMART

SM00068; GHB; 1.
SMART graphical view of domain structure.

PROSITE

PS00261; GLYCO_HORMONE_BETA_1; 1.
PS00689; GLYCO_HORMONE_BETA_2; 1.

Genome annotation databases

GeneID

443395; -.

Phylogenomic databases

HOVERGEN

P01231; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Direct protein sequencing; Glycoprotein; Hormone; Secreted; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 20`	`20`
`CHAIN`	`21 141`	`121`	`Lutropin subunit beta.`	`PRO_0000011734`
`CHAIN`	`21 139`	`119`	`LH beta-3.`	`PRO_0000011735`
`CHAIN`	`21 138`	`118`	`LH beta-2.`	`PRO_0000011736`
`CHAIN`	`21 137`	`117`	`LH beta-1.`	`PRO_0000011737`
`MOD_RES`	`21 21`		`Blocked amino end (Ser).`
`CARBOHYD`	`33 33`		`N-linked (GlcNAc...) [GlycoSuiteDB].`	`CAR_000046`
`DISULFID`	`29 77`		`By similarity.`
`DISULFID`	`43 92`
`DISULFID`	`46 130`
`DISULFID`	`54 108`		`By similarity.`
`DISULFID`	`58 110`		`By similarity.`
`DISULFID`	`113 120`
`VARIANT`	`138 141`	`4`	`Missing (in some molecules).`
`CONFLICT`	`30 30`		`Q -> E (in Ref. 4; AA sequence).`
`CONFLICT`	`40 40`		`K -> N (in Ref. 5; AA sequence).`
`CONFLICT`	`59 59`		`L -> P (in Ref. 1; AAB27819).`
`CONFLICT`	`63 63`		`R -> Q (in Ref. 2; CAA36729).`
`CONFLICT`	`71 71`		`P -> PP (in Ref. 4; AA sequence).`
`CONFLICT`	`79 79`		`Y -> V (in Ref. 5; AA sequence).`
`CONFLICT`	`81 81`		`E -> Q (in Ref. 4; AA sequence).`
`CONFLICT`	`122 123`		`GP -> PG (in Ref. 3, 4 and 5).`
`CONFLICT`	`126 126`		`Q -> E (in Ref. 3 and 4).`

Sequence information

Length: 141 AA [This is the length of the unprocessed precursor]

Molecular weight: 15184 Da [This is the MW of the unprocessed precursor]

CRC64: C59EC7C0AA55A9DC [This is a checksum on the sequence]

        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

P01231 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools