P01231 (LSHB_SHEEP) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lutropin subunit beta
Short name=Lutropin beta chain

Alternative name(s):
Interstitial cell-stimulating hormone
Luteinizing hormone subunit beta
Short name=LH-B
Short name=LSH-B
Short name=LSH-beta

Cleaved into the following 3 chains:

1. LH beta-1
2. LH beta-2
3. LH beta-3

Gene names

Name:

LHB

Organism

Ovis aries (Sheep)

Taxonomic identifier

9940 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Caprinae › Ovis

Protein attributes

Sequence length	141 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Ref.5
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. Ref.5
Subcellular location	Secreted.
Sequence similarities	Belongs to the glycoprotein hormones subunit beta family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Hormone
PTM	Disulfide bond Glycoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	hormone activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	Ref.3 Ref.4 Ref.5
	Chain	21 – 141	121	Lutropin subunit beta Ref.3		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
Amino acid modifications
	Modified residue	21	1	Blocked amino end (Ser) Ref.3
	Glycosylation	33	1	N-linked (GlcNAc...) Ref.3		CAR_000046
	Disulfide bond	29 ↔ 77		By similarity
	Disulfide bond	43 ↔ 92		Ref.6
	Disulfide bond	46 ↔ 130		Ref.6
	Disulfide bond	54 ↔ 108		By similarity
	Disulfide bond	58 ↔ 110		By similarity
	Disulfide bond	113 ↔ 120		Ref.6
Natural variations
	Natural variant	138 – 141	4	Missing in some molecules.
Experimental info
	Sequence conflict	30	1	Q → E AA sequence Ref.4
	Sequence conflict	40	1	K → N AA sequence Ref.5
	Sequence conflict	59	1	L → P in AAB27819. Ref.1
	Sequence conflict	63	1	R → Q in CAA36729. Ref.2
	Sequence conflict	71	1	P → PP AA sequence Ref.4
	Sequence conflict	79	1	Y → V AA sequence Ref.5
	Sequence conflict	81	1	E → Q AA sequence Ref.4
	Sequence conflict	122 – 123	2	GP → PG AA sequence Ref.3
	Sequence conflict	122 – 123	2	GP → PG AA sequence Ref.4
	Sequence conflict	122 – 123	2	GP → PG AA sequence Ref.5
	Sequence conflict	126	1	Q → E AA sequence Ref.3
	Sequence conflict	126	1	Q → E AA sequence Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P01231 [UniParc]. Last modified November 1, 1995. Version 3. Checksum: C59EC7C0AA55A9DC	FASTA	141	15,184
	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

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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	S64695 Genomic DNA. Translation: AAB27819.1. X52488 mRNA. Translation: CAA36729.1.
PIR	UTSHB. I46949.
RefSeq	NP_001009380.1. NM_001009380.1.
UniGene	Oar.442.
3D structure databases
ProteinModelPortal	P01231.
SMR	P01231. Positions 24-131.
ModBase	Search...
PTM databases
GlycoSuiteDB	P01231.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	443395.
Organism-specific databases
CTD	3972.
Phylogenomic databases
HOVERGEN	HBG006698.
Family and domain databases
InterPro	IPR006208. Cys_knot. IPR001545. Gonadotropin_bsu. IPR018245. Gonadotropin_bsu_CS. [Graphical view]
PANTHER	PTHR11515. Gly_hormoneB. 1 hit.
Pfam	PF00007. Cys_knot. 1 hit. [Graphical view]
SMART	SM00068. GHB. 1 hit. [Graphical view]
PROSITE	PS00261. GLYCO_HORMONE_BETA_1. 1 hit. PS00689. GLYCO_HORMONE_BETA_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LSHB_SHEEP

Accession

Primary (citable) accession number: P01231

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	November 1, 1995
Last modified:	June 28, 2011
This is version 89 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program