ANPRA_HUMAN
ID ANPRA_HUMAN Reviewed; 1061 AA.
AC P16066; B0ZBF0; Q5SR08; Q6P4Q3;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 219.
DE RecName: Full=Atrial natriuretic peptide receptor 1 {ECO:0000305};
DE EC=4.6.1.2 {ECO:0000269|PubMed:1672777};
DE AltName: Full=Atrial natriuretic peptide receptor type A;
DE Short=ANP-A;
DE Short=ANPR-A;
DE Short=NPR-A;
DE AltName: Full=Guanylate cyclase A;
DE Short=GC-A;
DE Flags: Precursor;
GN Name=NPR1 {ECO:0000312|HGNC:HGNC:7943}; Synonyms=ANPRA;
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 [MRNA].
RC TISSUE=Kidney;
RX PubMed=2569967; DOI=10.1002/j.1460-2075.1989.tb03518.x;
RA Lowe D.G., Chang M.S., Hellmiss R., Chen E., Singh S., Garbers D.L.,
RA Goeddel D.V.;
RT "Human atrial natriuretic peptide receptor defines a new paradigm for
RT second messenger signal transduction.";
RL EMBO J. 8:1377-1384(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Blood;
RX PubMed=9618281; DOI=10.1006/bbrc.1998.8693;
RA Takahashi Y., Nakayama T., Soma M., Izumi Y., Kanmatsuse K.;
RT "Organization of the human natriuretic peptide receptor A gene.";
RL Biochem. Biophys. Res. Commun. 246:736-739(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Maeda N., Knowles J.W.;
RT "Identification of functional polymorphisms in noncoding regions of the
RT human natriuretic peptide receptor A gene.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 634-1048.
RC TISSUE=Retina;
RX PubMed=7954658; DOI=10.1007/bf02088585;
RA Pardhasaradhi K., Kutty R.K., Gentleman S., Krishna G.;
RT "Expression of mRNA for atrial natriuretic peptide receptor guanylate
RT cyclase (ANPRA) in human retina.";
RL Cell. Mol. Neurobiol. 14:1-7(1994).
RN [9]
RP LIGAND-BINDING.
RX PubMed=1660465; DOI=10.1016/s0021-9258(18)54463-x;
RA Bennett B.D., Bennett G.L., Vitangcol R.V., Jewett J.R., Burnier J.,
RA Henzel W., Lowe D.G.;
RT "Extracellular domain-IgG fusion proteins for three human natriuretic
RT peptide receptors. Hormone pharmacology and application to solid phase
RT screening of synthetic peptide antisera.";
RL J. Biol. Chem. 266:23060-23067(1991).
RN [10]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=1672777; DOI=10.1126/science.1672777;
RA Koller K.J., Lowe D.G., Bennett G.L., Minamino N., Kangawa K., Matsuo H.,
RA Goeddel D.V.;
RT "Selective activation of the B natriuretic peptide receptor by C-type
RT natriuretic peptide (CNP).";
RL Science 252:120-123(1991).
RN [11]
RP PHOSPHORYLATION AT SER-519; SER-529; THR-532; SER-534 AND SER-538.
RX PubMed=20977274; DOI=10.1021/bi101700e;
RA Yoder A.R., Stone M.D., Griffin T.J., Potter L.R.;
RT "Mass spectrometric identification of phosphorylation sites in guanylyl
RT cyclase A and B.";
RL Biochemistry 49:10137-10145(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP VARIANTS [LARGE SCALE ANALYSIS] VAL-182; CYS-270; MET-755; GLN-939 AND
RP LYS-967.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Receptor for the atrial natriuretic peptide NPPA/ANP and the
CC brain natriuretic peptide NPPB/BNP which are potent vasoactive hormones
CC playing a key role in cardiovascular homeostasis. Has guanylate cyclase
CC activity upon binding of the ligand. {ECO:0000269|PubMed:1672777}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP = 3',5'-cyclic GMP + diphosphate; Xref=Rhea:RHEA:13665,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57746; EC=4.6.1.2;
CC Evidence={ECO:0000269|PubMed:1672777};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13666;
CC Evidence={ECO:0000305|PubMed:1672777};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- PTM: Phosphorylation of the protein kinase-like domain is required for
CC full activation by ANP. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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DR EMBL; X15357; CAA33417.1; -; mRNA.
DR EMBL; AB010491; BAA31199.1; -; Genomic_DNA.
DR EMBL; AF190631; AAF01340.1; -; Genomic_DNA.
DR EMBL; EU326310; ACA05918.1; -; Genomic_DNA.
DR EMBL; AL713889; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW53284.1; -; Genomic_DNA.
DR EMBL; BC063304; AAH63304.1; -; mRNA.
DR EMBL; S72628; AAD14112.1; -; mRNA.
DR CCDS; CCDS1051.1; -.
DR PIR; S04459; OYHUAR.
DR RefSeq; NP_000897.3; NM_000906.3.
DR AlphaFoldDB; P16066; -.
DR SMR; P16066; -.
DR BioGRID; 110941; 12.
DR ComplexPortal; CPX-35; ANPR-A receptor complex.
DR DIP; DIP-46246N; -.
DR IntAct; P16066; 5.
DR MINT; P16066; -.
DR STRING; 9606.ENSP00000357669; -.
DR BindingDB; P16066; -.
DR ChEMBL; CHEMBL1988; -.
DR DrugBank; DB01612; Amyl Nitrite.
DR DrugBank; DB01613; Erythrityl tetranitrate.
DR DrugBank; DB00883; Isosorbide dinitrate.
DR DrugBank; DB04899; Nesiritide.
DR DrugBank; DB00727; Nitroglycerin.
DR DrugBank; DB00325; Nitroprusside.
DR DrugBank; DB05034; Ularitide.
DR DrugCentral; P16066; -.
DR GuidetoPHARMACOLOGY; 1747; -.
DR TCDB; 8.A.85.1.6; the guanylate cyclase (gc) family.
DR GlyGen; P16066; 7 sites.
DR iPTMnet; P16066; -.
DR PhosphoSitePlus; P16066; -.
DR BioMuta; NPR1; -.
DR DMDM; 113912; -.
DR EPD; P16066; -.
DR jPOST; P16066; -.
DR MassIVE; P16066; -.
DR MaxQB; P16066; -.
DR PaxDb; P16066; -.
DR PeptideAtlas; P16066; -.
DR PRIDE; P16066; -.
DR ProteomicsDB; 53265; -.
DR ABCD; P16066; 1 sequenced antibody.
DR Antibodypedia; 20386; 307 antibodies from 32 providers.
DR DNASU; 4881; -.
DR Ensembl; ENST00000368680.4; ENSP00000357669.3; ENSG00000169418.10.
DR GeneID; 4881; -.
DR KEGG; hsa:4881; -.
DR MANE-Select; ENST00000368680.4; ENSP00000357669.3; NM_000906.4; NP_000897.3.
DR UCSC; uc001fcs.5; human.
DR CTD; 4881; -.
DR DisGeNET; 4881; -.
DR GeneCards; NPR1; -.
DR HGNC; HGNC:7943; NPR1.
DR HPA; ENSG00000169418; Tissue enhanced (adipose).
DR MIM; 108960; gene.
DR neXtProt; NX_P16066; -.
DR OpenTargets; ENSG00000169418; -.
DR PharmGKB; PA31736; -.
DR VEuPathDB; HostDB:ENSG00000169418; -.
DR eggNOG; KOG1023; Eukaryota.
DR GeneTree; ENSGT00940000156223; -.
DR HOGENOM; CLU_001072_1_3_1; -.
DR InParanoid; P16066; -.
DR OMA; KCAYEKS; -.
DR OrthoDB; 229634at2759; -.
DR PhylomeDB; P16066; -.
DR TreeFam; TF106338; -.
DR BRENDA; 4.6.1.2; 2681.
DR PathwayCommons; P16066; -.
DR Reactome; R-HSA-5578768; Physiological factors.
DR SignaLink; P16066; -.
DR SIGNOR; P16066; -.
DR BioGRID-ORCS; 4881; 17 hits in 1104 CRISPR screens.
DR ChiTaRS; NPR1; human.
DR GeneWiki; NPR1; -.
DR GenomeRNAi; 4881; -.
DR Pharos; P16066; Tclin.
DR PRO; PR:P16066; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P16066; protein.
DR Bgee; ENSG00000169418; Expressed in descending thoracic aorta and 174 other tissues.
DR ExpressionAtlas; P16066; baseline and differential.
DR Genevisible; P16066; HS.
DR GO; GO:1990620; C:ANPR-A receptor complex; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; NAS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004383; F:guanylate cyclase activity; IDA:UniProtKB.
DR GO; GO:0042562; F:hormone binding; IPI:UniProtKB.
DR GO; GO:0016941; F:natriuretic peptide receptor activity; IDA:UniProtKB.
DR GO; GO:0017046; F:peptide hormone binding; IPI:UniProtKB.
DR GO; GO:0001653; F:peptide receptor activity; IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0097746; P:blood vessel diameter maintenance; NAS:UniProtKB.
DR GO; GO:0007589; P:body fluid secretion; TAS:UniProtKB.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; NAS:UniProtKB.
DR GO; GO:0006182; P:cGMP biosynthetic process; IDA:GO_Central.
DR GO; GO:0019934; P:cGMP-mediated signaling; IEA:Ensembl.
DR GO; GO:0042417; P:dopamine metabolic process; IEA:Ensembl.
DR GO; GO:0016525; P:negative regulation of angiogenesis; TAS:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; NAS:UniProtKB.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0010753; P:positive regulation of cGMP-mediated signaling; IEA:Ensembl.
DR GO; GO:0035815; P:positive regulation of renal sodium excretion; TAS:UniProtKB.
DR GO; GO:0035810; P:positive regulation of urine volume; TAS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; IDA:UniProtKB.
DR GO; GO:0008217; P:regulation of blood pressure; NAS:UniProtKB.
DR GO; GO:0043114; P:regulation of vascular permeability; TAS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd07302; CHD; 1.
DR Gene3D; 3.30.70.1230; -; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR018297; A/G_cyclase_CS.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR001170; ANPR/GUC.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00255; NATPEPTIDER.
DR SMART; SM00044; CYCc; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
DR SUPFAM; SSF55073; SSF55073; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00458; ANF_RECEPTORS; 1.
DR PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW cGMP biosynthesis; Chloride; Disulfide bond; Glycoprotein; GTP-binding;
KW Lyase; Membrane; Nucleotide-binding; Phosphoprotein; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Vasoactive.
FT SIGNAL 1..32
FT CHAIN 33..1061
FT /note="Atrial natriuretic peptide receptor 1"
FT /id="PRO_0000012360"
FT TOPO_DOM 33..473
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 474..494
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 495..1061
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 528..805
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 876..1006
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 85
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250"
FT MOD_RES 519
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20977274"
FT MOD_RES 529
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20977274"
FT MOD_RES 532
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:20977274"
FT MOD_RES 534
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20977274"
FT MOD_RES 538
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20977274"
FT MOD_RES 542
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18910"
FT MOD_RES 545
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P18910"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 386
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 92..118
FT /evidence="ECO:0000250"
FT DISULFID 196..245
FT /evidence="ECO:0000250"
FT DISULFID 455..464
FT /evidence="ECO:0000250"
FT VARIANT 182
FT /note="A -> V (in dbSNP:rs56019647)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042214"
FT VARIANT 270
FT /note="F -> C (in a breast pleomorphic lobular carcinoma
FT sample; somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042215"
FT VARIANT 755
FT /note="V -> M (in dbSNP:rs55837780)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042216"
FT VARIANT 939
FT /note="R -> Q (in dbSNP:rs35240348)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042217"
FT VARIANT 967
FT /note="E -> K (in dbSNP:rs35479618)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042218"
FT CONFLICT 344
FT /note="G -> V (in Ref. 7; AAH63304)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1061 AA; 118919 MW; E6B5BD0FCA32F70D CRC64;
MPGPRRPAGS RLRLLLLLLL PPLLLLLRGS HAGNLTVAVV LPLANTSYPW SWARVGPAVE
LALAQVKARP DLLPGWTVRT VLGSSENALG VCSDTAAPLA AVDLKWEHNP AVFLGPGCVY
AAAPVGRFTA HWRVPLLTAG APALGFGVKD EYALTTRAGP SYAKLGDFVA ALHRRLGWER
QALMLYAYRP GDEEHCFFLV EGLFMRVRDR LNITVDHLEF AEDDLSHYTR LLRTMPRKGR
VIYICSSPDA FRTLMLLALE AGLCGEDYVF FHLDIFGQSL QGGQGPAPRR PWERGDGQDV
SARQAFQAAK IITYKDPDNP EYLEFLKQLK HLAYEQFNFT MEDGLVNTIP ASFHDGLLLY
IQAVTETLAH GGTVTDGENI TQRMWNRSFQ GVTGYLKIDS SGDRETDFSL WDMDPENGAF
RVVLNYNGTS QELVAVSGRK LNWPLGYPPP DIPKCGFDNE DPACNQDHLS TLEVLALVGS
LSLLGILIVS FFIYRKMQLE KELASELWRV RWEDVEPSSL ERHLRSAGSR LTLSGRGSNY
GSLLTTEGQF QVFAKTAYYK GNLVAVKRVN RKRIELTRKV LFELKHMRDV QNEHLTRFVG
ACTDPPNICI LTEYCPRGSL QDILENESIT LDWMFRYSLT NDIVKGMLFL HNGAICSHGN
LKSSNCVVDG RFVLKITDYG LESFRDLDPE QGHTVYAKKL WTAPELLRMA SPPVRGSQAG
DVYSFGIILQ EIALRSGVFH VEGLDLSPKE IIERVTRGEQ PPFRPSLALQ SHLEELGLLM
QRCWAEDPQE RPPFQQIRLT LRKFNRENSS NILDNLLSRM EQYANNLEEL VEERTQAYLE
EKRKAEALLY QILPHSVAEQ LKRGETVQAE AFDSVTIYFS DIVGFTALSA ESTPMQVVTL
LNDLYTCFDA VIDNFDVYKV ETIGDAYMVV SGLPVRNGRL HACEVARMAL ALLDAVRSFR
IRHRPQEQLR LRIGIHTGPV CAGVVGLKMP RYCLFGDTVN TASRMESNGE ALKIHLSSET
KAVLEEFGGF ELELRGDVEM KGKGKVRTYW LLGERGSSTR G
