Reviewed, UniProtKB/Swiss-Prot P07510 (ACHG_HUMAN)

Names and origin

Protein names

Recommended name:
    Acetylcholine receptor subunit gamma

Gene names

Name:	CHRNG
Synonyms:	ACHRG

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	517 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	After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Subunit structure	Pentamer of two alpha chains, and one each of the beta, delta, and gamma (in immature muscle) or epsilon (in mature muscle) chains.
Subcellular location	Cell junction › synapse › postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
Involvement in disease	Defects in CHRNG are a cause of lethal type multiple pterygium syndrome [MIM:253290]. Multiple pterygia are found infrequently in children with arthrogryposis and in fetuses with fetal akinesia syndrome. Inheritance can be autosomal dominant, autosomal recessive, or X linked, but autosomal recessive inheritance appears to be most common. Clinical expression is very variable, and, in the severest form, lethal multiple pterygium syndrome there is intrauterine growth retardation, multiple pterygia (e.g., chin to sternum, cervical, axillary, humero-ulnar, crural, popliteal, and ankles), and flexion contractures causing severe arthrogryposis and fetal akinesia. Subcutaneous edema can be severe, causing fetal hydrops with cystic hygroma and lung hypoplasia. Oligohydramnios and facial anomalies-in particular, cleft palate-are frequent. Defects in CHRNG are a cause of Escobar syndrome [MIM:265000]; also known as Escobar variant of multiple pterygium syndrome or nonlethal type multiple pterygium syndrome. Escobar syndrome is a nonlethal form of arthrogryposis multiplex congenita. It is an autosomal recessive condition characterized by excessive webbing (pterygia), congenital contractures (arthrogryposis), and scoliosis. Variable other features include intrauterine death, congenital respiratory distress, short stature, faciocranial dysmorphism, ptosis, low-set ears, arachnodactyly and cryptorchism in males. Congenital contractures are common and may be caused by reduced fetal movements at sensitive times of development. Possible causes of decreased fetal mobility include space constraints such as oligohydramnion, drugs, metabolic conditions or neuromuscular disorders including myasthenia gravis.
Sequence similarities	Belongs to the ligand-gated ionic channel (TC 1.A.9) family. [View classification]
Sequence caution	The sequence AAY24103.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAA25861.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Ion transport Transport
Cellular component	Cell junction Cell membrane Membrane Postsynaptic cell membrane Synapse
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Signal Transmembrane
Molecular function	Ionic channel Receptor
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	ion transport Inferred from electronic annotation. Source: UniProtKB-KW muscle contraction Traceable author statement. Source: ProtInc signal transduction Ref.1 Traceable author statement. Source: ProtInc
Cellular component	cell junction Inferred from electronic annotation. Source: UniProtKB-KW integral to plasma membrane Ref.1 Traceable author statement. Source: ProtInc postsynaptic membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	acetylcholine receptor activity Ref.1 Traceable author statement. Source: ProtInc nicotinic acetylcholine-activated cation-selective channel activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22	Potential
	Chain	23 – 517	495	Acetylcholine receptor subunit gamma		PRO_0000000334
Regions
	Topological domain	23 – 240	218	Extracellular Potential
	Transmembrane	241 – 265	25	Potential
	Transmembrane	275 – 293	19	Potential
	Transmembrane	309 – 330	22	Potential
	Topological domain	331 – 474	144	Cytoplasmic Potential
	Transmembrane	475 – 495	21	Potential
Amino acid modifications
	Modified residue	285	1	Phosphothreonine Ref.5
	Glycosylation	52	1	N-linked (GlcNAc...) Potential
	Glycosylation	163	1	N-linked (GlcNAc...) Potential
	Disulfide bond	150 ↔ 164		By similarity
Natural variations
	Natural variant	107	1	V → G in Escobar syndrome and multiple pterygium syndrome; lethal type. Ref.7		VAR_030753
	Natural variant	149	1	A → T: dbSNP rs2289080.		VAR_030754
	Natural variant	239	1	R → C in Escobar syndrome and multiple pterygium syndrome; lethal type. Ref.6		VAR_030755

Sequences

	Sequence		Length	Mass (Da)
	P07510-1 [UniParc]. Last modified February 20, 2007. Version 2. Checksum: 7C78F533D4997D7A	FASTA	517	57,883
	10 20 30 40 50 60 MHGGQGPLLL LLLLAVCLGA QGRNQEERLL ADLMQNYDPN LRPAERDSDV VNVSLKLTLT 70 80 90 100 110 120 NLISLNEREE ALTTNVWIEM QWCDYRLRWD PRDYEGLWVL RVPSTMVWRP DIVLENNVDG 130 140 150 160 170 180 VFEVALYCNV LVSPDGCIYW LPPAIFRSAC SISVTYFPFD WQNCSLIFQS QTYSTNEIDL 190 200 210 220 230 240 QLSQEDGQTI EWIFIDPEAF TENGEWAIQH RPAKMLLDPA APAQEAGHQK VVFYLLIQRK 250 260 270 280 290 300 PLFYVINIIA PCVLISSVAI LIHFLPAKAG GQKCTVAINV LLAQTVFLFL VAKKVPETSQ 310 320 330 340 350 360 AVPLISKYLT FLLVVTILIV VNAVVVLNVS LRSPHTHSMA RGVRKVFLRL LPQLLRMHVR 370 380 390 400 410 420 PLAPAAVQDT QSRLQNGSSG WSITTGEEVA LCLPRSELLF QQWQRQGLVA AALEKLEKGP 430 440 450 460 470 480 ELGLSQFCGS LKQAAPAIQA CVEACNLIAC ARHQQSHFDN GNEEWFLVGR VLDRVCFLAM 490 500 510 LSLFICGTAG IFLMAHYNRV PALPFPGDPR PYLPSPD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequence analysis of human genomic DNA encoding gamma subunit precursor of muscle acetylcholine receptor." Shibahara S., Kubo T., Perski H.J., Takahashi H., Noda M., Numa S. Eur. J. Biochem. 146:15-22(1985) [PubMed: 3967651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Primary structure of the human muscle acetylcholine receptor. cDNA cloning of the gamma and epsilon subunits." Beeson D.M.W., Brydson M., Betty M., Jeremiah S., Povey S., Vincent A., Newsom-Davis J. Eur. J. Biochem. 215:229-238(1993) [PubMed: 7688301] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Muscle fibroblast.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Tongue.
[4]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-285, MASS SPECTROMETRY.
[6]	"Escobar syndrome is a prenatal myasthenia caused by disruption of the acetylcholine receptor fetal gamma subunit." Hoffmann K., Mueller J.S., Stricker S., Megarbane A., Rajab A., Lindner T.H., Cohen M., Chouery E., Adaimy L., Ghanem I., Delague V., Boltshauser E., Talim B., Horvath R., Robinson P.N., Lochmueller H., Huebner C., Mundlos S. Am. J. Hum. Genet. 79:303-312(2006) [PubMed: 16826520] [Abstract] Cited for: VARIANT ESCOBAR SYNDROME/MULTIPLE PTERYGIUM SYNDROME CYS-239.
[7]	"Mutations in the embryonal subunit of the acetylcholine receptor (CHRNG) cause lethal and Escobar variants of multiple pterygium syndrome." Morgan N.V., Brueton L.A., Cox P., Greally M.T., Tolmie J., Pasha S., Aligianis I.A., van Bokhoven H., Marton T., Al-Gazali L., Morton J.E.V., Oley C., Johnson C.A., Trembath R.C., Brunner H.G., Maher E.R. Am. J. Hum. Genet. 79:390-395(2006) [PubMed: 16826531] [Abstract] Cited for: VARIANT ESCOBAR SYNDROME/MULTIPLE PTERYGIUM SYNDROME GLY-107.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBLGenBankDDBJ	X01715 , X01716, X01717, X01718, X01719, X01720, X01721, X04759 Genomic DNA. Translation: CAA25861.1. Sequence problems. AK125362 mRNA. Translation: BAG54190.1. AC092165 Genomic DNA. Translation: AAY24103.1. Sequence problems.
IPI	IPI00746413.
PIR	A23261.
RefSeq	NP_005190.4.
UniGene	Hs.248101
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	P07510.
PTM databases
PhosphoSite	P07510.
Proteomic databases
PRIDE	P07510.
Genome annotation databases
Ensembl	ENST00000389492; ENSP00000374143; ENSG00000196811; Homo sapiens. [Genome view] ENST00000389494; ENSP00000374145; ENSG00000196811; Homo sapiens. [Genome view]
GeneID	1146.
KEGG	hsa:1146.
UCSC	uc002vsx.1. human.
Organism-specific databases
CTD	1146.
GeneCards	GC02P233112.
HGNC	HGNC:1967. CHRNG.
MIM	100730. gene. 253290. phenotype. 265000. phenotype.
Orphanet	2990. Autosomal recessive multiple pterygium syndrome. 79449. Escobar syndrome. 33108. Multiple pterygium syndrome, lethal form.
PharmGKB	PA26499.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	P07510.
OMA	PQLLRMH.
Gene expression databases
ArrayExpress	P07510.
Bgee	P07510.
CleanEx	HS_CHRNG.
Genevestigator	P07510.
GermOnline	ENSG00000196811. Homo sapiens.
Family and domain databases
InterPro	IPR006029. Neu_channel_TM. IPR006202. Neur_chan_lig_bd. IPR006201. Neur_channel. IPR018000. Neurotransmitter_ion_chnl_CS. IPR002394. Nicotinic_acetylcholine_rcpt_N. [Graphical view]
Gene3D	G3DSA:2.70.170.10. Neur_chan_lig_bd. 1 hit.
PANTHER	PTHR18945. Neur_channel. 1 hit.
Pfam	PF02931. Neur_chan_LBD. 1 hit. PF02932. Neur_chan_memb. 1 hit. [Graphical view]
PRINTS	PR00254. NICOTINICR. PR00252. NRIONCHANNEL.
PROSITE	PS00236. NEUROTR_ION_CHANNEL. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	4768.
SOURCE	Search...

Entry information

Entry name

ACHG_HUMAN

Accession

Primary (citable) accession number: P07510
Secondary accession number(s): B3KWM8, Q53RG2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	February 20, 2007
Last modified:	November 3, 2009
This is version 95 of the entry and version 2 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.