ACTHR_HUMAN
ID ACTHR_HUMAN Reviewed; 297 AA.
AC Q01718; A8K016; Q3MI45; Q504X6;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Adrenocorticotropic hormone receptor;
DE Short=ACTH receptor;
DE Short=ACTH-R;
DE AltName: Full=Adrenocorticotropin receptor;
DE AltName: Full=Melanocortin receptor 2;
DE Short=MC2-R;
GN Name=MC2R; Synonyms=ACTHR;
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].
RC TISSUE=Skin;
RX PubMed=1325670; DOI=10.1126/science.1325670;
RA Mountjoy K.G., Robbins L.S., Mortrud M., Cone R.D.;
RT "The cloning of a family of genes that encode the melanocortin receptors.";
RL Science 257:1248-1251(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S.,
RA Tsutsumi S., Aburatani H., Asai K., Akiyama Y.;
RT "Genome-wide discovery and analysis of human seven transmembrane helix
RT receptor genes.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kopatz S.A., Aronstam R.S., Sharma S.V.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Adrenal gland;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-293.
RX PubMed=8463333; DOI=10.1016/s0021-9258(18)53088-x;
RA Gantz I., Konda Y., Tashiro T., Shimoto Y., Miwa H., Munzert G.,
RA Watson S.J., Delvalle J., Yamada T.;
RT "Molecular cloning of a novel melanocortin receptor.";
RL J. Biol. Chem. 268:8246-8250(1993).
RN [8]
RP INTERACTION WITH MRAP.
RX PubMed=15654338; DOI=10.1038/ng1501;
RA Metherell L.A., Chapple J.P., Cooray S., David A., Becker C.,
RA Rueschendorf F., Naville D., Begeot M., Khoo B., Nuernberg P., Huebner A.,
RA Cheetham M.E., Clark A.J.L.;
RT "Mutations in MRAP, encoding a new interacting partner of the ACTH
RT receptor, cause familial glucocorticoid deficiency type 2.";
RL Nat. Genet. 37:166-170(2005).
RN [9]
RP FUNCTION, AND INTERACTION WITH MRAP AND MRAP2.
RX PubMed=19329486; DOI=10.1073/pnas.0809918106;
RA Chan L.F., Webb T.R., Chung T.T., Meimaridou E., Cooray S.N., Guasti L.,
RA Chapple J.P., Egertova M., Elphick M.R., Cheetham M.E., Metherell L.A.,
RA Clark A.J.;
RT "MRAP and MRAP2 are bidirectional regulators of the melanocortin receptor
RT family.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:6146-6151(2009).
RN [10]
RP FUNCTION, AND INTERACTION WITH MRAP AND MRAP2.
RX PubMed=20371771; DOI=10.1126/scisignal.2000593;
RA Sebag J.A., Hinkle P.M.;
RT "Regulation of G protein-coupled receptor signaling: specific dominant-
RT negative effects of melanocortin 2 receptor accessory protein 2.";
RL Sci. Signal. 3:RA28-RA28(2010).
RN [11]
RP REVIEW ON GCCD1 VARIANTS.
RA Clark A.J.L., Weber A.;
RT "Molecular insights into inherited ACTH resistance syndromes.";
RL Trends Endocrinol. Metab. 5:209-214(1994).
RN [12]
RP VARIANT GCCD1 ILE-74.
RX PubMed=8094489; DOI=10.1016/0140-6736(93)90208-x;
RA Clark A.J.L., McLoughlin L., Grossman A.;
RT "Familial glucocorticoid deficiency associated with point mutation in the
RT adrenocorticotropin receptor.";
RL Lancet 341:461-462(1993).
RN [13]
RP VARIANT GCCD1 ARG-120.
RX PubMed=8227361; DOI=10.1172/jci116853;
RA Tsigos C., Arai K., Hung W., Chrousos G.P.;
RT "Hereditary isolated glucocorticoid deficiency is associated with
RT abnormalities of the adrenocorticotropin receptor gene.";
RL J. Clin. Invest. 92:2458-2461(1993).
RN [14]
RP VARIANTS GCCD1 ASN-107 AND PHE-251.
RX PubMed=8636348; DOI=10.1210/jcem.81.4.8636348;
RA Naville D., Barjhoux L., Jaillard C., Faury D., Despert F., Esteva B.,
RA Durand P., Saez J.M., Begeot M.;
RT "Demonstration by transfection studies that mutations in the
RT adrenocorticotropin receptor gene are one cause of the hereditary syndrome
RT of glucocorticoid deficiency.";
RL J. Clin. Endocrinol. Metab. 81:1442-1448(1996).
RN [15]
RP VARIANTS GCCD1 ASN-103 AND TRP-137.
RX PubMed=10971458; DOI=10.1046/j.1365-2265.2000.01040.x;
RA Ishii T., Ogata T., Sasaki G., Sato S., Kinoshita E.I., Matsuo N.;
RT "Novel mutations of the ACTH receptor gene in a female adult patient with
RT adrenal unresponsiveness to ACTH.";
RL Clin. Endocrinol. (Oxf.) 53:389-392(2000).
RN [16]
RP VARIANTS GCCD1 ILE-74; TRP-137 AND CYS-254.
RX PubMed=12213892; DOI=10.1210/jc.2002-020501;
RA Fluck C.E., Martens J.W.M., Conte F.A., Miller W.L.;
RT "Clinical, genetic, and functional characterization of adrenocorticotropin
RT receptor mutations using a novel receptor assay.";
RL J. Clin. Endocrinol. Metab. 87:4318-4323(2002).
RN [17]
RP VARIANT PRO-137.
RX PubMed=20108423;
RA Mueller O.T., Coovadia A.;
RT "Novel human pathological mutations. Gene symbol: MC2R. Disease:
RT Glucocorticoid deficiency.";
RL Hum. Genet. 127:112-112(2010).
CC -!- FUNCTION: Receptor for corticotropin (ACTH). This receptor is mediated
CC by G proteins (G(s)) which activate adenylate cyclase (cAMP).
CC {ECO:0000269|PubMed:19329486, ECO:0000269|PubMed:20371771}.
CC -!- SUBUNIT: Interacts with MRAP; increasing ligand-sensitivity and
CC generation of cAMP. Interacts with MRAP2; competing with MRAP for
CC binding to MC2R and impairing the binding of corticotropin (ACTH).
CC {ECO:0000269|PubMed:15654338, ECO:0000269|PubMed:19329486,
CC ECO:0000269|PubMed:20371771}.
CC -!- INTERACTION:
CC Q01718; Q8TCY5: MRAP; NbExp=3; IntAct=EBI-9537171, EBI-9538727;
CC Q01718; Q8TCY5-1: MRAP; NbExp=3; IntAct=EBI-9537171, EBI-21991233;
CC Q01718; Q96G30: MRAP2; NbExp=2; IntAct=EBI-9537171, EBI-9537218;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Melanocytes and corticoadrenal tissue.
CC -!- DISEASE: Glucocorticoid deficiency 1 (GCCD1) [MIM:202200]: A form of
CC glucocorticoid deficiency, a rare autosomal recessive disorder
CC characterized by resistance to ACTH action on the adrenal cortex,
CC adrenal insufficiency and an inability of the adrenal cortex to produce
CC cortisol. It usually presents in the neonatal period or in early
CC childhood with episodes of hypoglycemia and other symptoms related to
CC cortisol deficiency, including failure to thrive, recurrent illnesses
CC or infections, convulsions, and shock. In a small number of patients
CC hypoglycemia can be sufficiently severe and persistent that it leads to
CC serious long-term neurological damage or death. The diagnosis is
CC readily confirmed with a low plasma cortisol measurement in the
CC presence of an elevated ACTH level, and normal aldosterone and plasma
CC renin measurements. {ECO:0000269|PubMed:10971458,
CC ECO:0000269|PubMed:12213892, ECO:0000269|PubMed:8094489,
CC ECO:0000269|PubMed:8227361, ECO:0000269|PubMed:8636348}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; X65633; CAA46587.1; -; Genomic_DNA.
DR EMBL; AB065915; BAC06130.1; -; Genomic_DNA.
DR EMBL; AK289381; BAF82070.1; -; mRNA.
DR EMBL; AK315319; BAG37722.1; -; mRNA.
DR EMBL; CH471113; EAX01503.1; -; Genomic_DNA.
DR EMBL; BC069074; AAH69074.1; -; mRNA.
DR EMBL; BC094710; AAH94710.1; -; mRNA.
DR EMBL; BC104169; AAI04170.1; -; mRNA.
DR EMBL; BC104170; AAI04171.1; -; mRNA.
DR EMBL; AY225229; AAO67714.1; -; Genomic_DNA.
DR CCDS; CCDS11869.1; -.
DR PIR; C43265; C43265.
DR RefSeq; NP_000520.1; NM_000529.2.
DR RefSeq; NP_001278840.1; NM_001291911.1.
DR RefSeq; XP_016881270.1; XM_017025781.1.
DR AlphaFoldDB; Q01718; -.
DR SMR; Q01718; -.
DR BioGRID; 110328; 3.
DR DIP; DIP-29949N; -.
DR IntAct; Q01718; 2.
DR MINT; Q01718; -.
DR STRING; 9606.ENSP00000333821; -.
DR BindingDB; Q01718; -.
DR ChEMBL; CHEMBL1965; -.
DR DrugBank; DB11653; Bremelanotide.
DR DrugBank; DB01285; Corticotropin.
DR DrugBank; DB09334; Seractide acetate.
DR DrugBank; DB01284; Tetracosactide.
DR DrugCentral; Q01718; -.
DR GuidetoPHARMACOLOGY; 283; -.
DR TCDB; 9.A.14.2.4; the g-protein-coupled receptor (gpcr) family.
DR GlyGen; Q01718; 2 sites.
DR iPTMnet; Q01718; -.
DR PhosphoSitePlus; Q01718; -.
DR BioMuta; MC2R; -.
DR DMDM; 399002; -.
DR PaxDb; Q01718; -.
DR PeptideAtlas; Q01718; -.
DR PRIDE; Q01718; -.
DR Antibodypedia; 21964; 286 antibodies from 32 providers.
DR DNASU; 4158; -.
DR Ensembl; ENST00000327606.4; ENSP00000333821.2; ENSG00000185231.5.
DR GeneID; 4158; -.
DR KEGG; hsa:4158; -.
DR MANE-Select; ENST00000327606.4; ENSP00000333821.2; NM_000529.2; NP_000520.1.
DR UCSC; uc002ksp.2; human.
DR CTD; 4158; -.
DR DisGeNET; 4158; -.
DR GeneCards; MC2R; -.
DR HGNC; HGNC:6930; MC2R.
DR HPA; ENSG00000185231; Tissue enriched (adrenal).
DR MalaCards; MC2R; -.
DR MIM; 202200; phenotype.
DR MIM; 607397; gene.
DR neXtProt; NX_Q01718; -.
DR OpenTargets; ENSG00000185231; -.
DR Orphanet; 361; Familial glucocorticoid deficiency.
DR PharmGKB; PA30674; -.
DR VEuPathDB; HostDB:ENSG00000185231; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234510; -.
DR HOGENOM; CLU_009579_13_0_1; -.
DR InParanoid; Q01718; -.
DR OMA; AVIWTFC; -.
DR OrthoDB; 988552at2759; -.
DR PhylomeDB; Q01718; -.
DR TreeFam; TF332646; -.
DR PathwayCommons; Q01718; -.
DR Reactome; R-HSA-375276; Peptide ligand-binding receptors.
DR Reactome; R-HSA-418555; G alpha (s) signalling events.
DR Reactome; R-HSA-5579031; Defective ACTH causes obesity and POMCD.
DR Reactome; R-HSA-9660821; ADORA2B mediated anti-inflammatory cytokines production.
DR SignaLink; Q01718; -.
DR SIGNOR; Q01718; -.
DR BioGRID-ORCS; 4158; 11 hits in 1069 CRISPR screens.
DR GeneWiki; ACTH_receptor; -.
DR GenomeRNAi; 4158; -.
DR Pharos; Q01718; Tclin.
DR PRO; PR:Q01718; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q01718; protein.
DR Bgee; ENSG00000185231; Expressed in adrenal tissue and 30 other tissues.
DR ExpressionAtlas; Q01718; baseline and differential.
DR Genevisible; Q01718; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004978; F:corticotropin receptor activity; TAS:ProtInc.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0004977; F:melanocortin receptor activity; TAS:ProtInc.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; TAS:ProtInc.
DR GO; GO:0019222; P:regulation of metabolic process; IBA:GO_Central.
DR InterPro; IPR001168; ACTH_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR001671; Melcrt_ACTH_rcpt.
DR PANTHER; PTHR22750:SF3; PTHR22750:SF3; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00520; ACTROPHINR.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00534; MCRFAMILY.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disease variant; G-protein coupled receptor; Glycoprotein;
KW Lipoprotein; Membrane; Palmitate; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..297
FT /note="Adrenocorticotropic hormone receptor"
FT /id="PRO_0000069054"
FT TOPO_DOM 1..23
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 24..49
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 50..58
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 59..79
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 80..104
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 105..126
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 127..147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 148..168
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 169..180
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 181..199
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 200..217
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 218..244
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 245..256
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 257..278
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 279..297
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT LIPID 293
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 12
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 17
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 27
FT /note="P -> R (in dbSNP:rs28926178)"
FT /id="VAR_003509"
FT VARIANT 74
FT /note="S -> I (in GCCD1; complete loss of activity;
FT dbSNP:rs104894658)"
FT /evidence="ECO:0000269|PubMed:12213892,
FT ECO:0000269|PubMed:8094489"
FT /id="VAR_003510"
FT VARIANT 103
FT /note="D -> N (in GCCD1; dbSNP:rs768093045)"
FT /evidence="ECO:0000269|PubMed:10971458"
FT /id="VAR_010702"
FT VARIANT 107
FT /note="D -> N (in GCCD1; dbSNP:rs104894661)"
FT /evidence="ECO:0000269|PubMed:8636348"
FT /id="VAR_015095"
FT VARIANT 120
FT /note="S -> R (in GCCD1; dbSNP:rs104894656)"
FT /evidence="ECO:0000269|PubMed:8227361"
FT /id="VAR_003511"
FT VARIANT 128
FT /note="R -> C (in GCCD1; dbSNP:rs104894657)"
FT /id="VAR_003512"
FT VARIANT 137
FT /note="R -> P (found in a glucocorticoid deficiency patient
FT carrying also mutation I-74; dbSNP:rs1208417750)"
FT /evidence="ECO:0000269|PubMed:20108423"
FT /id="VAR_064986"
FT VARIANT 137
FT /note="R -> W (in GCCD1; partial loss of ACTIVITY;
FT dbSNP:rs104894660)"
FT /evidence="ECO:0000269|PubMed:10971458,
FT ECO:0000269|PubMed:12213892"
FT /id="VAR_010703"
FT VARIANT 146
FT /note="R -> H (in GCCD1; dbSNP:rs758709668)"
FT /id="VAR_003513"
FT VARIANT 251
FT /note="C -> F (in GCCD1; dbSNP:rs104894662)"
FT /evidence="ECO:0000269|PubMed:8636348"
FT /id="VAR_015096"
FT VARIANT 254
FT /note="Y -> C (in GCCD1; complete loss of activity;
FT dbSNP:rs28940892)"
FT /evidence="ECO:0000269|PubMed:12213892"
FT /id="VAR_015295"
FT VARIANT 278
FT /note="F -> C (in dbSNP:rs28926182)"
FT /id="VAR_049369"
SQ SEQUENCE 297 AA; 33927 MW; 66EE31961ABB8773 CRC64;
MKHIINSYEN INNTARNNSD CPRVVLPEEI FFTISIVGVL ENLIVLLAVF KNKNLQAPMY
FFICSLAISD MLGSLYKILE NILIILRNMG YLKPRGSFET TADDIIDSLF VLSLLGSIFS
LSVIAADRYI TIFHALRYHS IVTMRRTVVV LTVIWTFCTG TGITMVIFSH HVPTVITFTS
LFPLMLVFIL CLYVHMFLLA RSHTRKISTL PRANMKGAIT LTILLGVFIF CWAPFVLHVL
LMTFCPSNPY CACYMSLFQV NGMLIMCNAV IDPFIYAFRS PELRDAFKKM IFCSRYW
