ACHG_HUMAN
ID ACHG_HUMAN Reviewed; 517 AA.
AC P07510; B3KWM8; Q14DU4; Q53RG2;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Acetylcholine receptor subunit gamma;
DE Flags: Precursor;
GN Name=CHRNG; Synonyms=ACHRG;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3967651; DOI=10.1111/j.1432-1033.1985.tb08614.x;
RA Shibahara S., Kubo T., Perski H.J., Takahashi H., Noda M., Numa S.;
RT "Cloning and sequence analysis of human genomic DNA encoding gamma subunit
RT precursor of muscle acetylcholine receptor.";
RL Eur. J. Biochem. 146:15-22(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Muscle fibroblast;
RX PubMed=7688301; DOI=10.1111/j.1432-1033.1993.tb18027.x;
RA Beeson D.M.W., Brydson M., Betty M., Jeremiah S., Povey S., Vincent A.,
RA Newsom-Davis J.;
RT "Primary structure of the human muscle acetylcholine receptor. cDNA cloning
RT of the gamma and epsilon subunits.";
RL Eur. J. Biochem. 215:229-238(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP VARIANT EVMPS CYS-239, AND VARIANT LMPS CYS-239.
RX PubMed=16826520; DOI=10.1086/506257;
RA Hoffmann K., Mueller J.S., Stricker S., Megarbane A., Rajab A.,
RA Lindner T.H., Cohen M., Chouery E., Adaimy L., Ghanem I., Delague V.,
RA Boltshauser E., Talim B., Horvath R., Robinson P.N., Lochmueller H.,
RA Huebner C., Mundlos S.;
RT "Escobar syndrome is a prenatal myasthenia caused by disruption of the
RT acetylcholine receptor fetal gamma subunit.";
RL Am. J. Hum. Genet. 79:303-312(2006).
RN [7]
RP VARIANT EVMPS GLY-107, AND VARIANT LMPS GLY-107.
RX PubMed=16826531; DOI=10.1086/506256;
RA Morgan N.V., Brueton L.A., Cox P., Greally M.T., Tolmie J., Pasha S.,
RA Aligianis I.A., van Bokhoven H., Marton T., Al-Gazali L., Morton J.E.V.,
RA Oley C., Johnson C.A., Trembath R.C., Brunner H.G., Maher E.R.;
RT "Mutations in the embryonal subunit of the acetylcholine receptor (CHRNG)
RT cause lethal and Escobar variants of multiple pterygium syndrome.";
RL Am. J. Hum. Genet. 79:390-395(2006).
CC -!- FUNCTION: After binding acetylcholine, the AChR responds by an
CC extensive change in conformation that affects all subunits and leads to
CC opening of an ion-conducting channel across the plasma membrane.
CC -!- SUBUNIT: Pentamer of two alpha chains, and one each of the beta, delta,
CC and gamma (in immature muscle) or epsilon (in mature muscle) chains.
CC -!- INTERACTION:
CC P07510; Q15323: KRT31; NbExp=4; IntAct=EBI-9008836, EBI-948001;
CC P07510; P60409: KRTAP10-7; NbExp=4; IntAct=EBI-9008836, EBI-10172290;
CC P07510; P60410: KRTAP10-8; NbExp=4; IntAct=EBI-9008836, EBI-10171774;
CC P07510; P60411: KRTAP10-9; NbExp=4; IntAct=EBI-9008836, EBI-10172052;
CC P07510; Q7Z3S9: NOTCH2NLA; NbExp=5; IntAct=EBI-9008836, EBI-945833;
CC P07510-2; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-11979451, EBI-10173507;
CC P07510-2; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-11979451, EBI-3867333;
CC P07510-2; Q15323: KRT31; NbExp=6; IntAct=EBI-11979451, EBI-948001;
CC P07510-2; O76011: KRT34; NbExp=3; IntAct=EBI-11979451, EBI-1047093;
CC P07510-2; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-11979451, EBI-11959885;
CC P07510-2; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-11979451, EBI-11749135;
CC P07510-2; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-11979451, EBI-10172290;
CC P07510-2; P60410: KRTAP10-8; NbExp=6; IntAct=EBI-11979451, EBI-10171774;
CC P07510-2; P60411: KRTAP10-9; NbExp=6; IntAct=EBI-11979451, EBI-10172052;
CC P07510-2; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-11979451, EBI-11953334;
CC P07510-2; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-11979451, EBI-3958099;
CC P07510-2; Q9BYQ3: KRTAP9-3; NbExp=3; IntAct=EBI-11979451, EBI-1043191;
CC P07510-2; Q99750: MDFI; NbExp=6; IntAct=EBI-11979451, EBI-724076;
CC P07510-2; P50222: MEOX2; NbExp=3; IntAct=EBI-11979451, EBI-748397;
CC P07510-2; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-11979451, EBI-945833;
CC P07510-2; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-11979451, EBI-22310682;
CC P07510-2; O43765: SGTA; NbExp=3; IntAct=EBI-11979451, EBI-347996;
CC P07510-2; Q13596: SNX1; NbExp=3; IntAct=EBI-11979451, EBI-2822329;
CC P07510-2; O43597: SPRY2; NbExp=3; IntAct=EBI-11979451, EBI-742487;
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane
CC protein. Cell membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P07510-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P07510-2; Sequence=VSP_055775;
CC -!- DISEASE: Multiple pterygium syndrome, lethal type (LMPS) [MIM:253290]:
CC Multiple pterygia are found infrequently in children with
CC arthrogryposis and in fetuses with fetal akinesia syndrome. In lethal
CC multiple pterygium syndrome there is intrauterine growth retardation,
CC multiple pterygia, and flexion contractures causing severe
CC arthrogryposis and fetal akinesia. Subcutaneous edema can be severe,
CC causing fetal hydrops with cystic hygroma and lung hypoplasia.
CC Oligohydramnios and facial anomalies are frequent.
CC {ECO:0000269|PubMed:16826520, ECO:0000269|PubMed:16826531}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Multiple pterygium syndrome, Escobar variant (EVMPS)
CC [MIM:265000]: Non-lethal form of arthrogryposis multiplex congenita. It
CC is an autosomal recessive condition characterized by excessive webbing
CC (pterygia), congenital contractures (arthrogryposis), and scoliosis.
CC Variable other features include intrauterine death, congenital
CC respiratory distress, short stature, faciocranial dysmorphism, ptosis,
CC low-set ears, arachnodactyly and cryptorchism in males. Congenital
CC contractures are common and may be caused by reduced fetal movements at
CC sensitive times of development. Possible causes of decreased fetal
CC mobility include space constraints such as oligohydramnion, drugs,
CC metabolic conditions or neuromuscular disorders including myasthenia
CC gravis. {ECO:0000269|PubMed:16826520, ECO:0000269|PubMed:16826531}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC Acetylcholine receptor (TC 1.A.9.1) subfamily. Gamma/CHRNG sub-
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAY24103.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA25861.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X01715; CAA25861.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X01716; CAA25861.1; JOINED; Genomic_DNA.
DR EMBL; X01717; CAA25861.1; JOINED; Genomic_DNA.
DR EMBL; X01718; CAA25861.1; JOINED; Genomic_DNA.
DR EMBL; X01719; CAA25861.1; JOINED; Genomic_DNA.
DR EMBL; X01720; CAA25861.1; JOINED; Genomic_DNA.
DR EMBL; X01721; CAA25861.1; JOINED; Genomic_DNA.
DR EMBL; X04759; CAA25861.1; JOINED; Genomic_DNA.
DR EMBL; AK125362; BAG54190.1; -; mRNA.
DR EMBL; AC092165; AAY24103.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC111802; AAI11803.1; -; mRNA.
DR CCDS; CCDS33400.1; -. [P07510-1]
DR PIR; A23261; A23261.
DR RefSeq; NP_005190.4; NM_005199.4. [P07510-1]
DR AlphaFoldDB; P07510; -.
DR SMR; P07510; -.
DR BioGRID; 107568; 22.
DR ComplexPortal; CPX-2179; Muscle-type nicotinic acetylcholine receptor complex, alpha1-beta1-delta-gamma.
DR IntAct; P07510; 21.
DR STRING; 9606.ENSP00000374145; -.
DR BindingDB; P07510; -.
DR ChEMBL; CHEMBL1907588; -.
DR DrugCentral; P07510; -.
DR TCDB; 1.A.9.1.1; the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.
DR GlyGen; P07510; 2 sites.
DR iPTMnet; P07510; -.
DR PhosphoSitePlus; P07510; -.
DR BioMuta; CHRNG; -.
DR DMDM; 126302510; -.
DR jPOST; P07510; -.
DR PaxDb; P07510; -.
DR PeptideAtlas; P07510; -.
DR PRIDE; P07510; -.
DR ProteomicsDB; 52012; -. [P07510-1]
DR ABCD; P07510; 2 sequenced antibodies.
DR Antibodypedia; 20220; 134 antibodies from 26 providers.
DR DNASU; 1146; -.
DR Ensembl; ENST00000389492.3; ENSP00000374143.3; ENSG00000196811.13. [P07510-2]
DR Ensembl; ENST00000651502.1; ENSP00000498757.1; ENSG00000196811.13. [P07510-1]
DR GeneID; 1146; -.
DR KEGG; hsa:1146; -.
DR MANE-Select; ENST00000651502.1; ENSP00000498757.1; NM_005199.5; NP_005190.4.
DR UCSC; uc002vsx.1; human. [P07510-1]
DR CTD; 1146; -.
DR DisGeNET; 1146; -.
DR GeneCards; CHRNG; -.
DR HGNC; HGNC:1967; CHRNG.
DR HPA; ENSG00000196811; Tissue enriched (skeletal).
DR MalaCards; CHRNG; -.
DR MIM; 100730; gene.
DR MIM; 253290; phenotype.
DR MIM; 265000; phenotype.
DR neXtProt; NX_P07510; -.
DR OpenTargets; ENSG00000196811; -.
DR Orphanet; 2990; Autosomal recessive multiple pterygium syndrome.
DR Orphanet; 33108; Lethal multiple pterygium syndrome.
DR PharmGKB; PA26499; -.
DR VEuPathDB; HostDB:ENSG00000196811; -.
DR eggNOG; KOG3645; Eukaryota.
DR GeneTree; ENSGT00940000160041; -.
DR HOGENOM; CLU_018074_1_4_1; -.
DR InParanoid; P07510; -.
DR OMA; CVDACNL; -.
DR OrthoDB; 588360at2759; -.
DR PhylomeDB; P07510; -.
DR TreeFam; TF315605; -.
DR PathwayCommons; P07510; -.
DR Reactome; R-HSA-629587; Highly sodium permeable postsynaptic acetylcholine nicotinic receptors.
DR SignaLink; P07510; -.
DR BioGRID-ORCS; 1146; 23 hits in 1069 CRISPR screens.
DR GeneWiki; CHRNG; -.
DR GenomeRNAi; 1146; -.
DR Pharos; P07510; Tclin.
DR PRO; PR:P07510; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P07510; protein.
DR Bgee; ENSG00000196811; Expressed in gastrocnemius and 49 other tissues.
DR ExpressionAtlas; P07510; baseline and differential.
DR Genevisible; P07510; HS.
DR GO; GO:0005892; C:acetylcholine-gated channel complex; IC:ComplexPortal.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0015464; F:acetylcholine receptor activity; TAS:ProtInc.
DR GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; IBA:GO_Central.
DR GO; GO:0015267; F:channel activity; TAS:ProtInc.
DR GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
DR GO; GO:0095500; P:acetylcholine receptor signaling pathway; IC:ComplexPortal.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006936; P:muscle contraction; TAS:ProtInc.
DR GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 1.20.58.390; -; 2.
DR Gene3D; 2.70.170.10; -; 1.
DR InterPro; IPR006202; Neur_chan_lig-bd.
DR InterPro; IPR036734; Neur_chan_lig-bd_sf.
DR InterPro; IPR006201; Neur_channel.
DR InterPro; IPR036719; Neuro-gated_channel_TM_sf.
DR InterPro; IPR038050; Neuro_actylchol_rec.
DR InterPro; IPR006029; Neurotrans-gated_channel_TM.
DR InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
DR InterPro; IPR002394; Nicotinic_acetylcholine_rcpt.
DR PANTHER; PTHR18945; PTHR18945; 1.
DR Pfam; PF02931; Neur_chan_LBD; 1.
DR Pfam; PF02932; Neur_chan_memb; 1.
DR PRINTS; PR00254; NICOTINICR.
DR PRINTS; PR00252; NRIONCHANNEL.
DR SUPFAM; SSF63712; SSF63712; 1.
DR SUPFAM; SSF90112; SSF90112; 1.
DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disease variant; Disulfide bond;
KW Glycoprotein; Ion channel; Ion transport; Ligand-gated ion channel;
KW Membrane; Postsynaptic cell membrane; Receptor; Reference proteome; Signal;
KW Synapse; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..517
FT /note="Acetylcholine receptor subunit gamma"
FT /id="PRO_0000000334"
FT TOPO_DOM 23..240
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..293
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 331..474
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 475..495
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 150..164
FT /evidence="ECO:0000250"
FT VAR_SEQ 117..169
FT /note="NVDGVFEVALYCNVLVSPDGCIYWLPPAIFRSACSISVTYFPFDWQNCSLIF
FT Q -> K (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055775"
FT VARIANT 107
FT /note="V -> G (in EVMPS and LMPS; dbSNP:rs267606726)"
FT /evidence="ECO:0000269|PubMed:16826531"
FT /id="VAR_030753"
FT VARIANT 149
FT /note="A -> T (in dbSNP:rs2289080)"
FT /id="VAR_030754"
FT VARIANT 239
FT /note="R -> C (in EVMPS and LMPS; dbSNP:rs121912670)"
FT /evidence="ECO:0000269|PubMed:16826520"
FT /id="VAR_030755"
FT CONFLICT 189
FT /note="T -> S (in Ref. 5; AAI11803)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 517 AA; 57883 MW; 7C78F533D4997D7A CRC64;
MHGGQGPLLL LLLLAVCLGA QGRNQEERLL ADLMQNYDPN LRPAERDSDV VNVSLKLTLT
NLISLNEREE ALTTNVWIEM QWCDYRLRWD PRDYEGLWVL RVPSTMVWRP DIVLENNVDG
VFEVALYCNV LVSPDGCIYW LPPAIFRSAC SISVTYFPFD WQNCSLIFQS QTYSTNEIDL
QLSQEDGQTI EWIFIDPEAF TENGEWAIQH RPAKMLLDPA APAQEAGHQK VVFYLLIQRK
PLFYVINIIA PCVLISSVAI LIHFLPAKAG GQKCTVAINV LLAQTVFLFL VAKKVPETSQ
AVPLISKYLT FLLVVTILIV VNAVVVLNVS LRSPHTHSMA RGVRKVFLRL LPQLLRMHVR
PLAPAAVQDT QSRLQNGSSG WSITTGEEVA LCLPRSELLF QQWQRQGLVA AALEKLEKGP
ELGLSQFCGS LKQAAPAIQA CVEACNLIAC ARHQQSHFDN GNEEWFLVGR VLDRVCFLAM
LSLFICGTAG IFLMAHYNRV PALPFPGDPR PYLPSPD
