Reviewed, UniProtKB/Swiss-Prot P22888 (LSHR_HUMAN)

Names and origin

Protein names

Recommended name:
    Lutropin-choriogonadotropic hormone receptor
Alternative name(s):
    LH/CG-R
    LSH-R
    Luteinizing hormone receptor
      Short name=LHR

Gene names

Name:	LHCGR
Synonyms:	LCGR, LGR2, LHRHR

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	699 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	Receptor for lutropin-choriogonadotropic hormone. The activity of this receptor is mediated by G proteins which activate adenylate cyclase.
Subcellular location	Cell membrane; Multi-pass membrane protein.
Tissue specificity	Gonadal and thyroid cells.
Involvement in disease	Defects in LHCGR are a cause of familial male precocious puberty (FMPP) [MIM:176410]; also known as testotoxicosis. In FMPP the receptor is constitutively activated. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15 Ref.19 Ref.21 Defects in LHCGR are a cause of Leydig cell hypoplasia (LCH) [MIM:152790]. LCH is an autosomal recessive disease characterized by male pseudohermaphroditism. In LCH the testes are small with marked immaturity of the Leydig cells which correlates with undetectable plasma testosterone levels and elevated gonadotropins. Ref.13 Ref.16 Ref.17 Ref.20 Ref.23 Ref.24
Sequence similarities	Belongs to the G-protein coupled receptor 1 family. FSH/LSH/TSH subfamily. Contains 7 LRR (leucine-rich) repeats.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Domain	Leucine-rich repeat Repeat Signal Transmembrane
Molecular function	G-protein coupled receptor Receptor Transducer
PTM	Disulfide bond Glycoprotein Lipoprotein Palmitate Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	G-protein signaling, coupled to cyclic nucleotide second messenger Ref.13 Traceable author statement. Source: ProtInc male genitalia development Ref.24 Traceable author statement. Source: ProtInc male gonad development Ref.13 Traceable author statement. Source: ProtInc
Cellular component	endosome Traceable author statement. Source: ProtInc integral to plasma membrane Ref.13 Traceable author statement. Source: ProtInc
Molecular function	lutropin-choriogonadotropic hormone receptor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.

Isoform Long (identifier: P22888-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform Short (identifier: P22888-2)

The sequence of this isoform differs from the canonical sequence as follows:
     227-289: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 26

26

Potential

Chain

27 – 699

673

Lutropin-choriogonadotropic hormone receptor

PRO_0000012780

Regions

Topological domain

27 – 363

337

Extracellular Potential

Transmembrane

364 – 385

22

1 Potential

Topological domain

386 – 395

10

Cytoplasmic Potential

Transmembrane

396 – 416

21

2 Potential

Topological domain

417 – 439

23

Extracellular Potential

Transmembrane

440 – 462

23

3 Potential

Topological domain

463 – 482

20

Cytoplasmic Potential

Transmembrane

483 – 505

23

4 Potential

Topological domain

506 – 525

20

Extracellular Potential

Transmembrane

526 – 549

24

5 Potential

Topological domain

550 – 570

21

Cytoplasmic Potential

Transmembrane

571 – 594

24

6 Potential

Topological domain

595 – 605

11

Extracellular Potential

Transmembrane

606 – 627

22

7 Potential

Topological domain

628 – 699

72

Cytoplasmic Potential

Repeat

48 – 71

24

LRR 1

Repeat

97 – 121

25

LRR 2

Repeat

122 – 147

26

LRR 3

Repeat

149 – 171

23

LRR 4

Repeat

172 – 196

25

LRR 5

Repeat

197 – 220

24

LRR 6

Repeat

221 – 244

24

LRR 7

Amino acid modifications

Lipidation

643

1

S-palmitoyl cysteine Ref.7

Lipidation

644

1

S-palmitoyl cysteine Ref.7

Glycosylation

99

1

N-linked (GlcNAc...) Potential

Glycosylation

174

1

N-linked (GlcNAc...) Potential

Glycosylation

195

1

N-linked (GlcNAc...) Potential

Glycosylation

291

1

N-linked (GlcNAc...) Potential

Glycosylation

299

1

N-linked (GlcNAc...) Potential

Glycosylation

313

1

N-linked (GlcNAc...) Potential

Disulfide bond

439 ↔ 514

By similarity

Natural variations

Alternative sequence

227 – 289

63

Missing in isoform Short.

VSP_001962

Natural variant

18

1

Q → QLQ

VAR_003549

Natural variant

131

1

C → R in LCH. Ref.17

VAR_010154

Natural variant

284

1

N → S

VAR_003550

Natural variant

291

1

N → S: dbSNP rs12470652.

VAR_055922

Natural variant

306

1

S → N

VAR_003551

Natural variant

343

1

C → S in LCH.

VAR_010155

Natural variant

354

1

E → K in LCH. Ref.20

VAR_003552

Natural variant

373

1

A → V in FMPP. Ref.19

VAR_003553

Natural variant

398

1

M → T in FMPP. Ref.15

VAR_003554

Natural variant

457

1

L → R in FMPP. Ref.21

VAR_010156

Natural variant

542

1

I → L in FMPP.

VAR_010157

Natural variant

543

1

C → R in FMPP.

VAR_010158

Natural variant

564

1

D → G in FMPP.

VAR_010159

Natural variant

564

1

D → N in a breast cancer sample; somatic mutation. Ref.26

VAR_035764

Natural variant

568

1

A → V in FMPP. Ref.12

VAR_003555

Natural variant

571

1

M → I in FMPP. Ref.9

VAR_003556

Natural variant

572

1

A → V in FMPP. Ref.11

VAR_003557

Natural variant

575

1

I → L in FMPP.

VAR_010160

Natural variant

577

1

T → I in FMPP. Ref.10 Ref.14

VAR_003558

Natural variant

578

1

D → E in FMPP.

VAR_010161

Natural variant

578

1

D → G in FMPP. Ref.8 Ref.9

VAR_003559

Natural variant

578

1

D → H in Leydig cell tumor; somatic mutation; causes receptor activation and precocious puberty. Ref.25

VAR_010162

Natural variant

578

1

D → Y in FMPP.

VAR_010163

Natural variant

581

1

C → R in FMPP.

VAR_010164

Natural variant

593

1

A → P in LCH; abolishes signal transduction. Ref.13

VAR_003560

Natural variant

608 – 609

2

Missing in LCH.

VAR_003561

Natural variant

616

1

S → Y in LCH; micropenis. Ref.16

VAR_003562

Natural variant

625

1

I → K in LCH. Ref.24

VAR_003563

Experimental info

Mutagenesis

643

1

C → G: Loss of palmitoylation. Ref.7

Mutagenesis

644

1

C → G: Loss of palmitoylation. Ref.7

Sequence conflict

7

1

A → P in AAA70231. Ref.3

Sequence conflict

19

1

P → A in AAA70231. Ref.3

Sequence conflict

27 – 28

2

EA → R in AAA70231. Ref.3

Sequence conflict

44 – 51

8

CPGPTAGL → APAPRPS in AAA70231. Ref.3

Sequence conflict

68

1

A → S in AAA70231. Ref.3

Sequence conflict

124

1

R → G Ref.1

Sequence conflict

124

1

R → G Ref.4

Sequence conflict

262 – 263

2

RE → KQ in AAA70231. Ref.3

Sequence conflict

270

1

E → R in AAA70231. Ref.3

Sequence conflict

274

1

T → H in AAA70231. Ref.3

Sequence conflict

290

1

Q → L in AAA70231. Ref.3

Sequence conflict

311 – 323

13

Missing in AAA70231. Ref.3

Sequence conflict

312

1

S → N in AAB19917. Ref.2

Sequence conflict

448

1

F → L in AAA70231. Ref.3

Sequence conflict

540

1

F → L in AAA70231. Ref.3

Sequence conflict

546

1

Y → T Ref.2

Sequence conflict

649

1

E → DP in AAA70231. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

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.

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.

.

.

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.

.

.

.

.

.

699

Helix Strand Turn

Details...

Beta strand

53 – 55

3

Turn

64 – 66

3

Helix

67 – 69

3

Beta strand

77 – 79

3

Beta strand

87 – 89

3

Turn

94 – 96

3

Beta strand

102 – 104

3

Turn

111 – 113

3

Helix

117 – 119

3

Beta strand

127 – 129

3

Helix

138 – 141

4

Helix

142 – 145

4

Beta strand

146 – 149

4

Beta strand

152 – 154

3

Turn

159 – 163

5

Turn

167 – 170

4

Beta strand

178 – 180

3

Turn

189 – 195

7

Beta strand

200 – 203

4

Turn

208 – 212

5

Helix

216 – 218

3

Beta strand

226 – 228

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long [UniParc]. Last modified February 12, 2003. Version 3. Checksum: 16F9980BB0ED7146	FASTA	699	78,616
	10 20 30 40 50 60 MKQRFSALQL LKLLLLLQPP LPRALREALC PEPCNCVPDG ALRCPGPTAG LTRLSLAYLP 70 80 90 100 110 120 VKVIPSQAFR GLNEVIKIEI SQIDSLERIE ANAFDNLLNL SEILIQNTKN LRYIEPGAFI 130 140 150 160 170 180 NLPRLKYLSI CNTGIRKFPD VTKVFSSESN FILEICDNLH ITTIPGNAFQ GMNNESVTLK 190 200 210 220 230 240 LYGNGFEEVQ SHAFNGTTLT SLELKENVHL EKMHNGAFRG ATGPKTLDIS STKLQALPSY 250 260 270 280 290 300 GLESIQRLIA TSSYSLKKLP SRETFVNLLE ATLTYPSHCC AFRNLPTKEQ NFSHSISENF 310 320 330 340 350 360 SKQCESTVRK VSNKTLYSSM LAESELSGWD YEYGFCLPKT PRCAPEPDAF NPCEDIMGYD 370 380 390 400 410 420 FLRVLIWLIN ILAIMGNMTV LFVLLTSRYK LTVPRFLMCN LSFADFCMGL YLLLIASVDS 430 440 450 460 470 480 QTKGQYYNHA IDWQTGSGCS TAGFFTVFAS ELSVYTLTVI TLERWHTITY AIHLDQKLRL 490 500 510 520 530 540 RHAILIMLGG WLFSSLIAML PLVGVSNYMK VSICFPMDVE TTLSQVYILT ILILNVVAFF 550 560 570 580 590 600 IICACYIKIY FAVRNPELMA TNKDTKIAKK MAILIFTDFT CMAPISFFAI SAAFKVPLIT 610 620 630 640 650 660 VTNSKVLLVL FYPINSCANP FLYAIFTKTF QRDFFLLLSK FGCCKRRAEL YRRKDFSAYT 670 680 690 SNCKNGFTGS NKPSQSTLKL STLHCQGTAL LDKTRYTEC
	Isoform Short. Checksum: AE5D1307EC86D581	FASTA	636	71,588
	10 20 30 40 50 60 MKQRFSALQL LKLLLLLQPP LPRALREALC PEPCNCVPDG ALRCPGPTAG LTRLSLAYLP 70 80 90 100 110 120 VKVIPSQAFR GLNEVIKIEI SQIDSLERIE ANAFDNLLNL SEILIQNTKN LRYIEPGAFI 130 140 150 160 170 180 NLPRLKYLSI CNTGIRKFPD VTKVFSSESN FILEICDNLH ITTIPGNAFQ GMNNESVTLK 190 200 210 220 230 240 LYGNGFEEVQ SHAFNGTTLT SLELKENVHL EKMHNGAFRG ATGPKTQNFS HSISENFSKQ 250 260 270 280 290 300 CESTVRKVSN KTLYSSMLAE SELSGWDYEY GFCLPKTPRC APEPDAFNPC EDIMGYDFLR 310 320 330 340 350 360 VLIWLINILA IMGNMTVLFV LLTSRYKLTV PRFLMCNLSF ADFCMGLYLL LIASVDSQTK 370 380 390 400 410 420 GQYYNHAIDW QTGSGCSTAG FFTVFASELS VYTLTVITLE RWHTITYAIH LDQKLRLRHA 430 440 450 460 470 480 ILIMLGGWLF SSLIAMLPLV GVSNYMKVSI CFPMDVETTL SQVYILTILI LNVVAFFIIC 490 500 510 520 530 540 ACYIKIYFAV RNPELMATNK DTKIAKKMAI LIFTDFTCMA PISFFAISAA FKVPLITVTN 550 560 570 580 590 600 SKVLLVLFYP INSCANPFLY AIFTKTFQRD FFLLLSKFGC CKRRAELYRR KDFSAYTSNC 610 620 630 KNGFTGSNKP SQSTLKLSTL HCQGTALLDK TRYTEC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequencing of human LH/hCG receptor cDNA." Minegish T., Nakamura K., Takakura Y., Miyamoto K., Hasegawa Y., Ibuki Y., Igarashi M. Biochem. Biophys. Res. Commun. 172:1049-1054(1990) [PubMed: 2244890] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Ovary.
[2]	"Expression of human luteinizing hormone (LH) receptor: interaction with LH and chorionic gonadotropin from human but not equine, rat, and ovine species." Jia X.-C., Oikawa M., Bo M., Tanaka T., Ny T., Boime I., Hsueh A.J.W. Mol. Endocrinol. 5:759-768(1991) [PubMed: 1922095] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Ovary.
[3]	"Isolation of TSH and LH/CG receptor cDNAs from human thyroid: regulation by tissue specific splicing." Frazier A.L., Robbins L.S., Stork P.J., Sprengel R., Segaloff D.L., Cone R.D. Mol. Endocrinol. 4:1264-1276(1990) [PubMed: 2293030] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Thyroid.
[4]	"Structure of the human luteinizing hormone-choriogonadotropin receptor gene: unusual promoter and 5' non-coding regions." Atger M., Misrahi M., Sar S., Leflem L., Dessen P., Milgrom E. Mol. Cell. Endocrinol. 111:113-123(1995) [PubMed: 7556872] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LEU-GLN-18 INS.
[5]	"Genomic distribution and gonadal mRNA expression of two human luteinizing hormone receptor exon 1 sequences in random populations." Tsai-Morris C.-H., Geng Y., Buczko E., Dehejia A., Dufau M.L. Hum. Hered. 49:48-51(1999) [PubMed: 9858858] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-54, VARIANT LEU-GLN-18 INS.
[6]	"Structural predictions for the ligand-binding region of glycoprotein hormone receptors and the nature of hormone-receptor interactions." Jiang X., Dreano M., Buckler D.R., Cheng S., Ythier A., Wu H., Hendrickson W.A., el Tayar N. Structure 3:1341-1353(1995) [PubMed: 8747461] [Abstract] Cited for: 3D-STRUCTURE MODELING OF 51-232.
[7]	"Evidence that palmitoylation of carboxyl terminus cysteine residues of the human luteinizing hormone receptor regulates postendocytic processing." Munshi U.M., Clouser C.L., Peegel H., Menon K.M. Mol. Endocrinol. 19:749-758(2005) [PubMed: 15539429] [Abstract] Cited for: PALMITOYLATION AT CYS-643 AND CYS-644, MUTAGENESIS OF CYS-643 AND CYS-644.
[8]	"A constitutively activating mutation of the luteinizing hormone receptor in familial male precocious puberty." Shenker A., Laue L., Kosugi S., Merendino J.J. Jr., Minegishi T., Cutler G.B. Jr. Nature 365:652-654(1993) [PubMed: 7692306] [Abstract] Cited for: VARIANT FMPP GLY-578.
[9]	"Cosegregation of missense mutations of the luteinizing hormone receptor gene with familial male-limited precocious puberty." Kremer H., Mariman E., Otten B.J., Moll G.W. Jr., Stoelinga G.B.A., Wit J.M., Jansen M., Drop S.L., Faas B., Ropers H.-H., Brunner H.G. Hum. Mol. Genet. 2:1779-1783(1993) [PubMed: 8281137] [Abstract] Cited for: VARIANTS FMPP ILE-571 AND GLY-578.
[10]	"Characterization of heterogeneous mutations causing constitutive activation of the luteinizing hormone receptor in familial male precocious puberty." Kosugi S., van Dop C., Geffner M.E., Rabl W., Carel J.-C., Chaussain J.-L., Mori T., Merendino J.J. Jr., Shenker A. Hum. Mol. Genet. 4:183-188(1995) [PubMed: 7757065] [Abstract] Cited for: VARIANT FMPP ILE-577.
[11]	"A new constitutively activating point mutation in the luteinizing hormone/choriogonadotropin receptor gene in cases of male-limited precocious puberty." Yano K., Saji M., Hidaka A., Moriya N., Okuno A., Kohn L.D., Cutler G.B. Jr. J. Clin. Endocrinol. Metab. 80:1162-1168(1995) [PubMed: 7714085] [Abstract] Cited for: VARIANT FMPP VAL-572.
[12]	"A novel mutation of the luteinizing hormone receptor gene causing male gonadotropin-independent precocious puberty." Latronico A.C., Anasti J., Arnhold I.J., Mendonca B.B., Domenice S., Albano M.C., Zachman K., Wajchenberg B.L., Tsigos C. J. Clin. Endocrinol. Metab. 80:2490-2494(1995) [PubMed: 7629248] [Abstract] Cited for: VARIANT FMPP VAL-568.
[13]	"Male pseudohermaphroditism due to a homozygous missense mutation of the luteinizing hormone receptor gene." Kremer H., Kraaij R., Toledo S.P.A., Post M., Fridman J.B., Hayashida C.Y., van Reen M., Milgrom E., Ropers H.-H., Mariman E., Themmen A.P.N., Brunner H.G. Nat. Genet. 9:160-164(1995) [PubMed: 7719343] [Abstract] Cited for: VARIANT LCH PRO-593.
[14]	"A missense (T577I) mutation in the luteinizing hormone receptor gene associated with familial male-limited precocious puberty." Cocco S., Meloni A., Marini M.G., Cao A., Moi P. Hum. Mutat. 7:164-166(1996) [PubMed: 8829636] [Abstract] Cited for: VARIANT FMPP ILE-577.
[15]	"A new point mutation in the luteinising hormone receptor gene in familial and sporadic male limited precocious puberty: genotype does not always correlate with phenotype." Evans B.A.J., Bowen D.J., Smith P.J., Clayton P.E., Gregory J.W. J. Med. Genet. 33:143-147(1996) [PubMed: 8929952] [Abstract] Cited for: VARIANT FMPP THR-398.
[16]	"Testicular and ovarian resistance to luteinizing hormone caused by inactivating mutations of the luteinizing hormone-receptor gene." Latronico A.C., Anasti J., Arnhold I.J.P., Rapaport R., Mendonca B.B., Bloise W., Castro M., Tsigos C., Chrousos G.P. N. Engl. J. Med. 334:507-512(1996) [PubMed: 8559204] [Abstract] Cited for: VARIANT LCH TYR-616.
[17]	"Comparison of immunocytochemical and molecular features with the phenotype in a case of incomplete male pseudohermaphroditism associated with a mutation of the luteinizing hormone receptor." Misrahi M., Meduri G., Pissard S., Bouvattier C., Beau I., Loosfelt H., Jolivet A., Rappaport R., Milgrom E., Bougneres P. J. Clin. Endocrinol. Metab. 82:2159-2165(1997) [PubMed: 9215288] [Abstract] Cited for: VARIANT LCH ARG-131.
[18]	"Polymorphisms in the coding exons of the human luteinizing hormone receptor gene." Wu S.-M., Jose M., Hallermeier K., Rennert O.M., Chan W.-Y. Hum. Mutat. 11:333-334(1998) [PubMed: 10215412] [Abstract] Cited for: VARIANTS LEU-GLN-18 INS; SER-284 AND ASN-306.
[19]	"A mutation in the first transmembrane domain of the lutropin receptor causes male precocious puberty." Gromoll J., Partsch C.-J., Simoni M., Nordhoff V., Sippell W.G., Nieschlag E., Saxena B.B. J. Clin. Endocrinol. Metab. 83:476-480(1998) [PubMed: 9467560] [Abstract] Cited for: VARIANT FMPP VAL-373.
[20]	"A novel mutation of the human luteinizing hormone receptor in 46XY and 46XX sisters." Stavrou S.S., Zhu Y.S., Cai L.Q., Katz M.D., Herrera C., Defillo-Ricart M., Imperato-Mcginley J. J. Clin. Endocrinol. Metab. 83:2091-2098(1998) [PubMed: 9626144] [Abstract] Cited for: VARIANT LCH LYS-354.
[21]	"A unique constitutively activating mutation in third transmembrane helix of luteinizing hormone receptor causes sporadic male gonadotropin-independent precocious puberty." Latronico A.C., Abell A.N., Arnhold I.J., Liu X., Lins T.S., Brito V.N., Billerbeck A.E., Segaloff D.L., Mendonca B.B. J. Clin. Endocrinol. Metab. 83:2435-2440(1998) [PubMed: 9661624] [Abstract] Cited for: VARIANT FMPP ARG-457.
[22]	"Evidences for an allelic variant of the human LC/CG receptor rather than a gene duplication: functional comparison of wild-type and variant receptors." Rodien P., Cetani F., Costagliola S., Tonacchera M., Duprez L., Minegishi T., Govaerts C., Vassart G. J. Clin. Endocrinol. Metab. 83:4431-4434(1998) [PubMed: 9851790] [Abstract] Cited for: VARIANT LEU-GLN-18 INS.
[23]	"A homozygous microdeletion in helix 7 of the luteinizing hormone receptor associated with familial testicular and ovarian resistance is due to both decreased cell surface expression and impaired effector activation by the cell surface receptor." Latronico A.C., Chai Y., Arnhold I.J.P., Liu X., Mendonca B.B., Segaloff D.L. Mol. Endocrinol. 12:442-450(1998) [PubMed: 9514160] [Abstract] Cited for: VARIANT LCH 608-LEU-VAL-609 DEL.
[24]	"A homozygous mutation in the luteinizing hormone receptor causes partial Leydig cell hypoplasia: correlation between receptor activity and phenotype." Martens J.W., Verhoef-Post M., Abelin N., Ezabella M., Toledo S.P., Brunner H.G., Themmen A.P. Mol. Endocrinol. 12:775-784(1998) [PubMed: 9626653] [Abstract] Cited for: VARIANT LCH LYS-625.
[25]	"Leydig-cell tumors caused by an activating mutation of the gene encoding the luteinizing hormone receptor." Liu G., Duranteau L., Carel J.-C., Monroe J., Doyle D.A., Shenker A. N. Engl. J. Med. 341:1731-1736(1999) [PubMed: 10580072] [Abstract] Cited for: VARIANT LEYDIG CELL TUMOR HIS-578.
[26]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] ASN-564.
+	Additional computationally mapped references.

Web resources

Human luteinizing hormone receptor mutation db

GRIS

Glycoprotein-hormone Receptors Information System

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

Cross-references

Sequence databases

EMBLGenBankDDBJ

M63108 mRNA. Translation: AAA59515.1.
S57793 mRNA. Translation: AAB19917.2.
M73746 mRNA. Translation: AAA70231.1.
X84753 , X84754, X84755, X84756, X84757, X84758, X84759, X84760, X84761, X84762, X84763 Genomic DNA. Translation: CAA59234.1.
AF082076 Genomic DNA. Translation: AAC98291.1.
AF024642 Genomic DNA. Translation: AAB88417.1.

IPI

IPI00299615.
IPI00414187.

PIR

QRHUUT. A36243.

RefSeq

NP_000224.2.

UniGene

Hs.468490

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LUT	model	-	A	51-232	[»]
1XUL	model	-	C	51-232	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P22888.

Protein family/group databases

GPCRDB

Search...

PTM databases

PhosphoSite

P22888.

Proteomic databases

PRIDE

P22888.

Genome annotation databases

Ensembl

ENST00000294954; ENSP00000294954; ENSG00000138039; Homo sapiens. [Genome view]
ENST00000344775; ENSP00000344301; ENSG00000138039; Homo sapiens. [Genome view]
ENST00000401907; ENSP00000385406; ENSG00000138039; Homo sapiens. [Genome view]
ENST00000403273; ENSP00000385847; ENSG00000138039; Homo sapiens. [Genome view]
ENST00000405626; ENSP00000386033; ENSG00000138039; Homo sapiens. [Genome view]
ENST00000406114; ENSP00000385288; ENSG00000138039; Homo sapiens. [Genome view]
ENST00000420913; ENSP00000412255; ENSG00000138039; Homo sapiens. [Genome view]
ENST00000428232; ENSP00000403748; ENSG00000138039; Homo sapiens. [Genome view]

GeneID

3973.

KEGG

hsa:3973.

Organism-specific databases

CTD

3973.

GeneCards

GC02M048825.

HGNC

HGNC:6585. LHCGR.

HPA

CAB009814.

MIM

152790. gene+phenotype.
176410. phenotype.

Orphanet

755. Leydig cell hypoplasia.
3000. Testotoxicosis.

PharmGKB

PA30357.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P22888.

HOVERGEN

P22888.

Enzyme and pathway databases

Pathway_Interaction_DB

arf6arrestinpathway. Arf6 mediated densensitization of LHCGR.
arf6cyclingpathway. Arf6 signaling events.
arf6_traffickingpathway. Arf6 trafficking events.

Reactome

REACT_14797. Signaling by GPCR.

Gene expression databases

ArrayExpress

P22888.

Bgee

P22888.

CleanEx

HS_LHCGR.

Genevestigator

P22888.

GermOnline

ENSG00000138039. Homo sapiens.

Family and domain databases

InterPro

IPR000276. 7TM_GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_supfam.
IPR002131. Gphrmn_rcpt.
IPR000372. Leu-rich_rpt_Cys-rich-dom_N.
IPR002273. LSH_rcpt.
[Graphical view]

Pfam

PF00001. 7tm_1. 1 hit.
[Graphical view]

PRINTS

PR00373. GLYCHORMONER.
PR00237. GPCRRHODOPSN.
PR01144. LSHRECEPTOR.

SMART

SM00013. LRRNT. 1 hit.
[Graphical view]

PROSITE

PS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00050. Cetrorelix.
DB00097. Choriogonadotropin alfa.
DB00014. Goserelin.
DB00044. Lutropin alfa.
DB00032. Menotropins.

SOURCE

Search...

Entry information

Entry name

LSHR_HUMAN

Accession

Primary (citable) accession number: P22888
Secondary accession number(s): Q14751, Q15996, Q9UEW9

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	February 12, 2003
Last modified:	October 13, 2009
This is version 127 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.