ANPRC_HUMAN
ID ANPRC_HUMAN Reviewed; 541 AA.
AC P17342; A2RRD1; B4DT84; E7EPG9;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Atrial natriuretic peptide receptor 3;
DE AltName: Full=Atrial natriuretic peptide clearance receptor;
DE AltName: Full=Atrial natriuretic peptide receptor type C;
DE Short=ANP-C;
DE Short=ANPR-C;
DE Short=NPR-C;
DE Flags: Precursor;
GN Name=NPR3; Synonyms=ANPRC, C5orf23, NPRC;
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] (ISOFORM 2).
RC TISSUE=Kidney;
RX PubMed=2162522; DOI=10.1093/nar/18.11.3412;
RA Lowe D.G., Camerato T.R., Goeddel D.V.;
RT "cDNA sequence of the human atrial natriuretic peptide clearance
RT receptor.";
RL Nucleic Acids Res. 18:3412-3412(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2169733; DOI=10.1016/0006-291x(90)91216-f;
RA Porter J.G., Arfsten A., Fuller F., Miller J.A., Gregory L.C.,
RA Lewicki J.A.;
RT "Isolation and functional expression of the human atrial natriuretic
RT peptide clearance receptor cDNA.";
RL Biochem. Biophys. Res. Commun. 171:796-803(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Lens epithelium;
RA Rae J.L., Shepard A.R.;
RT "Human lens epithelial mRNA for atrial natriuretic peptide clearance
RT receptor.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Pericardium;
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].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 PARTIAL PROTEIN SEQUENCE (ISOFORMS 1 AND 2), DISULFIDE BONDS, GLYCOSYLATION
RP AT ASN-86; ASN-293 AND ASN-394, AND STRUCTURE OF CARBOHYDRATES.
RX PubMed=7727388; DOI=10.1021/bi00203a036;
RA Stults J.T., O'Connell K.L., Garcia C., Wong S., Engel A.M., Garbers D.L.,
RA Lowe D.G.;
RT "The disulfide linkages and glycosylation sites of the human natriuretic
RT peptide receptor-C homodimer.";
RL Biochemistry 33:11372-11381(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 X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 44-485 IN COMPLEX WITH NATRIURETIC
RP PEPTIDE, GLYCOSYLATION AT ASN-293 AND ASN-394, DISULFIDE BONDS, AND
RP SUBUNIT.
RX PubMed=11533490; DOI=10.1126/science.1062246;
RA He X.-L., Chow D.-C., Martick M.M., Garcia K.C.;
RT "Allosteric activation of a spring-loaded natriuretic peptide receptor
RT dimer by hormone.";
RL Science 293:1657-1662(2001).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-480 IN COMPLEX WITH NATRIURETIC
RP PEPTIDE AND CHLORIDE IONS, GLYCOSYLATION AT ASN-86; ASN-293 AND ASN-394,
RP AND DISULFIDE BONDS.
RX PubMed=16870210; DOI=10.1016/j.jmb.2006.06.060;
RA He X.-L., Dukkipati A., Garcia K.C.;
RT "Structural determinants of natriuretic peptide receptor specificity and
RT degeneracy.";
RL J. Mol. Biol. 361:698-714(2006).
RN [12]
RP INVOLVEMENT IN BOMOS, VARIANTS BOMOS PRO-148 AND VAL-363, AND SUBCELLULAR
RP LOCATION.
RX PubMed=30032985; DOI=10.1016/j.ajhg.2018.06.007;
RA Boudin E., de Jong T.R., Prickett T.C.R., Lapauw B., Toye K., Van Hoof V.,
RA Luyckx I., Verstraeten A., Heymans H.S.A., Dulfer E., Van Laer L.,
RA Berry I.R., Dobbie A., Blair E., Loeys B., Espiner E.A., Wit J.M.,
RA Van Hul W., Houpt P., Mortier G.R.;
RT "Bi-allelic Loss-of-Function Mutations in the NPR-C Receptor Result in
RT Enhanced Growth and Connective Tissue Abnormalities.";
RL Am. J. Hum. Genet. 103:288-295(2018).
CC -!- FUNCTION: Receptor for the natriuretic peptide hormones, binding with
CC similar affinities atrial natriuretic peptide NPPA/ANP, brain
CC natriuretic peptide NPPB/BNP, and C-type natriuretic peptide NPPC/CNP.
CC May function as a clearance receptor for NPPA, NPPB and NPPC,
CC regulating their local concentrations and effects. May regulate
CC diuresis, blood pressure and skeletal development. Does not have
CC guanylate cyclase activity. {ECO:0000250|UniProtKB:P70180}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (PubMed:11533490). Dimers can also
CC be formed through the C-terminal cysteine of isoform 2
CC (PubMed:11533490). Interacts with OSTN (By similarity).
CC {ECO:0000250|UniProtKB:P70180, ECO:0000269|PubMed:11533490}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:30032985};
CC Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=NPR-C5;
CC IsoId=P17342-1; Sequence=Displayed;
CC Name=2; Synonyms=NPR-C6;
CC IsoId=P17342-2; Sequence=VSP_001812;
CC Name=3;
CC IsoId=P17342-3; Sequence=VSP_045901, VSP_045902, VSP_001812;
CC -!- DISEASE: Boudin-Mortier syndrome (BOMOS) [MIM:619543]: An autosomal
CC recessive disorder characterized by tall stature, long digits, and
CC extra epiphyses in the hands and feet. In addition, some patients show
CC joint hypermobility and dilation of the aortic root.
CC {ECO:0000269|PubMed:30032985}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: Has low affinity for peptide hormones in the absence of
CC bound chloride.
CC -!- SIMILARITY: Belongs to the ANF receptor family. {ECO:0000305}.
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DR EMBL; X52282; CAA36523.1; -; mRNA.
DR EMBL; M59305; AAA51734.1; -; mRNA.
DR EMBL; AF025998; AAB88801.1; -; mRNA.
DR EMBL; AK300094; BAG61896.1; -; mRNA.
DR EMBL; AC008766; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC026703; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471118; EAX10799.1; -; Genomic_DNA.
DR EMBL; BC131540; AAI31541.1; -; mRNA.
DR CCDS; CCDS47196.1; -. [P17342-2]
DR CCDS; CCDS56356.1; -. [P17342-3]
DR CCDS; CCDS56357.1; -. [P17342-1]
DR PIR; S10150; OYHUCR.
DR RefSeq; NP_000899.1; NM_000908.3. [P17342-2]
DR RefSeq; NP_001191304.1; NM_001204375.1. [P17342-1]
DR RefSeq; NP_001191305.1; NM_001204376.1. [P17342-3]
DR PDB; 1JDN; X-ray; 2.90 A; A=44-485.
DR PDB; 1JDP; X-ray; 2.00 A; A/B=44-485.
DR PDB; 1YK0; X-ray; 2.40 A; A/B=1-480.
DR PDB; 1YK1; X-ray; 2.90 A; A/B=2-480.
DR PDBsum; 1JDN; -.
DR PDBsum; 1JDP; -.
DR PDBsum; 1YK0; -.
DR PDBsum; 1YK1; -.
DR AlphaFoldDB; P17342; -.
DR SMR; P17342; -.
DR BioGRID; 110943; 9.
DR IntAct; P17342; 1.
DR STRING; 9606.ENSP00000265074; -.
DR BindingDB; P17342; -.
DR ChEMBL; CHEMBL2247; -.
DR DrugBank; DB04899; Nesiritide.
DR GuidetoPHARMACOLOGY; 1749; -.
DR GlyGen; P17342; 4 sites.
DR iPTMnet; P17342; -.
DR PhosphoSitePlus; P17342; -.
DR BioMuta; NPR3; -.
DR DMDM; 27735161; -.
DR EPD; P17342; -.
DR jPOST; P17342; -.
DR MassIVE; P17342; -.
DR MaxQB; P17342; -.
DR PaxDb; P17342; -.
DR PeptideAtlas; P17342; -.
DR PRIDE; P17342; -.
DR ProteomicsDB; 17357; -.
DR ProteomicsDB; 53468; -. [P17342-1]
DR ProteomicsDB; 53469; -. [P17342-2]
DR Antibodypedia; 5387; 481 antibodies from 35 providers.
DR DNASU; 4883; -.
DR Ensembl; ENST00000265074.13; ENSP00000265074.8; ENSG00000113389.16. [P17342-1]
DR Ensembl; ENST00000326958.5; ENSP00000318340.2; ENSG00000113389.16. [P17342-3]
DR Ensembl; ENST00000415167.2; ENSP00000398028.2; ENSG00000113389.16. [P17342-2]
DR GeneID; 4883; -.
DR KEGG; hsa:4883; -.
DR MANE-Select; ENST00000265074.13; ENSP00000265074.8; NM_001204375.2; NP_001191304.1.
DR UCSC; uc003jhv.4; human. [P17342-1]
DR CTD; 4883; -.
DR DisGeNET; 4883; -.
DR GeneCards; NPR3; -.
DR HGNC; HGNC:7945; NPR3.
DR HPA; ENSG00000113389; Tissue enhanced (kidney).
DR MIM; 108962; gene.
DR MIM; 619543; phenotype.
DR neXtProt; NX_P17342; -.
DR OpenTargets; ENSG00000113389; -.
DR PharmGKB; PA31737; -.
DR VEuPathDB; HostDB:ENSG00000113389; -.
DR eggNOG; KOG1023; Eukaryota.
DR GeneTree; ENSGT00440000033872; -.
DR HOGENOM; CLU_013995_1_0_1; -.
DR InParanoid; P17342; -.
DR OMA; ENNIGKH; -.
DR PhylomeDB; P17342; -.
DR TreeFam; TF106339; -.
DR PathwayCommons; P17342; -.
DR SignaLink; P17342; -.
DR BioGRID-ORCS; 4883; 4 hits in 1068 CRISPR screens.
DR EvolutionaryTrace; P17342; -.
DR GeneWiki; NPR3; -.
DR GenomeRNAi; 4883; -.
DR Pharos; P17342; Tchem.
DR PRO; PR:P17342; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P17342; protein.
DR Bgee; ENSG00000113389; Expressed in adrenal tissue and 171 other tissues.
DR ExpressionAtlas; P17342; baseline and differential.
DR Genevisible; P17342; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IC:BHF-UCL.
DR GO; GO:0032991; C:protein-containing complex; IDA:CAFA.
DR GO; GO:0031404; F:chloride ion binding; IDA:CAFA.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; ISS:BHF-UCL.
DR GO; GO:0042562; F:hormone binding; IPI:CAFA.
DR GO; GO:0016941; F:natriuretic peptide receptor activity; IDA:UniProtKB.
DR GO; GO:0042277; F:peptide binding; IPI:CAFA.
DR GO; GO:0017046; F:peptide hormone binding; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0007194; P:negative regulation of adenylate cyclase activity; IEA:Ensembl.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0002158; P:osteoclast proliferation; ISS:UniProtKB.
DR GO; GO:0030157; P:pancreatic juice secretion; IEA:Ensembl.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:Ensembl.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; ISS:BHF-UCL.
DR GO; GO:0035810; P:positive regulation of urine volume; ISS:UniProtKB.
DR GO; GO:0008217; P:regulation of blood pressure; ISS:UniProtKB.
DR GO; GO:0033688; P:regulation of osteoblast proliferation; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0001501; P:skeletal system development; ISS:UniProtKB.
DR GO; GO:0042311; P:vasodilation; IEA:Ensembl.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR001170; ANPR/GUC.
DR InterPro; IPR028082; Peripla_BP_I.
DR Pfam; PF01094; ANF_receptor; 1.
DR PRINTS; PR00255; NATPEPTIDER.
DR SUPFAM; SSF53822; SSF53822; 1.
DR PROSITE; PS00458; ANF_RECEPTORS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Chloride;
KW Direct protein sequencing; Disease variant; Disulfide bond; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..541
FT /note="Atrial natriuretic peptide receptor 3"
FT /id="PRO_0000012370"
FT TOPO_DOM 27..481
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 482..504
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 505..541
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 106
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT BINDING 135
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT BINDING 136
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:16870210,
FT ECO:0000269|PubMed:7727388"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:11533490,
FT ECO:0000269|PubMed:16870210, ECO:0000269|PubMed:7727388"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:11533490,
FT ECO:0000269|PubMed:16870210, ECO:0000269|PubMed:7727388"
FT DISULFID 108..136
FT /evidence="ECO:0000269|PubMed:11533490,
FT ECO:0000269|PubMed:16870210, ECO:0000269|PubMed:7727388"
FT DISULFID 213..261
FT /evidence="ECO:0000269|PubMed:11533490,
FT ECO:0000269|PubMed:16870210, ECO:0000269|PubMed:7727388"
FT DISULFID 473
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:11533490,
FT ECO:0000269|PubMed:16870210, ECO:0000269|PubMed:7727388"
FT VAR_SEQ 1..40
FT /note="MPSLLVLTFSPCVLLGWALLAGGTGGGGVGGGGGGAGIGG -> MEPSALGP
FT WSLFPDLAPRDQEGQVLAPRRCFRRECGQNEK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045901"
FT VAR_SEQ 41..256
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045902"
FT VAR_SEQ 476..477
FT /note="SG -> C (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:2162522, ECO:0000303|Ref.3"
FT /id="VSP_001812"
FT VARIANT 148
FT /note="S -> P (in BOMOS; loss of localization at the plasma
FT membrane)"
FT /evidence="ECO:0000269|PubMed:30032985"
FT /id="VAR_086244"
FT VARIANT 363
FT /note="D -> V (in BOMOS; loss of localization at the plasma
FT membrane)"
FT /evidence="ECO:0000269|PubMed:30032985"
FT /id="VAR_086245"
FT CONFLICT 522
FT /note="N -> D (in Ref. 4; BAG61896)"
FT /evidence="ECO:0000305"
FT STRAND 52..59
FT /evidence="ECO:0007829|PDB:1JDP"
FT HELIX 69..83
FT /evidence="ECO:0007829|PDB:1JDP"
FT STRAND 98..105
FT /evidence="ECO:0007829|PDB:1JDP"
FT HELIX 111..122
FT /evidence="ECO:0007829|PDB:1JDP"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:1JDP"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:1JDP"
FT HELIX 137..150
FT /evidence="ECO:0007829|PDB:1JDP"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:1JDP"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:1JDP"
FT TURN 167..173
FT /evidence="ECO:0007829|PDB:1JDP"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:1JDP"
FT HELIX 181..195
FT /evidence="ECO:0007829|PDB:1JDP"
FT STRAND 199..205
FT /evidence="ECO:0007829|PDB:1JDP"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:1JDP"
FT HELIX 212..227
FT /evidence="ECO:0007829|PDB:1JDP"
FT STRAND 230..236
FT /evidence="ECO:0007829|PDB:1JDP"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:1YK0"
FT HELIX 244..254
FT /evidence="ECO:0007829|PDB:1JDP"
FT STRAND 256..262
FT /evidence="ECO:0007829|PDB:1JDP"
FT HELIX 264..276
FT /evidence="ECO:0007829|PDB:1JDP"
FT TURN 280..283
FT /evidence="ECO:0007829|PDB:1JDP"
FT STRAND 285..289
FT /evidence="ECO:0007829|PDB:1JDP"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:1JDN"
FT TURN 297..299
FT /evidence="ECO:0007829|PDB:1JDP"
FT HELIX 309..315
FT /evidence="ECO:0007829|PDB:1JDP"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:1JDP"
FT STRAND 319..324
FT /evidence="ECO:0007829|PDB:1JDP"
FT HELIX 330..344
FT /evidence="ECO:0007829|PDB:1JDP"
FT TURN 345..347
FT /evidence="ECO:0007829|PDB:1JDP"
FT HELIX 356..377
FT /evidence="ECO:0007829|PDB:1JDP"
FT HELIX 385..392
FT /evidence="ECO:0007829|PDB:1JDP"
FT STRAND 393..399
FT /evidence="ECO:0007829|PDB:1JDP"
FT STRAND 402..406
FT /evidence="ECO:0007829|PDB:1JDP"
FT STRAND 410..412
FT /evidence="ECO:0007829|PDB:1JDP"
FT STRAND 415..423
FT /evidence="ECO:0007829|PDB:1JDP"
FT TURN 424..427
FT /evidence="ECO:0007829|PDB:1JDP"
FT STRAND 428..436
FT /evidence="ECO:0007829|PDB:1JDP"
FT TURN 437..440
FT /evidence="ECO:0007829|PDB:1JDP"
FT STRAND 441..444
FT /evidence="ECO:0007829|PDB:1JDP"
FT STRAND 451..453
FT /evidence="ECO:0007829|PDB:1JDN"
FT HELIX 454..456
FT /evidence="ECO:0007829|PDB:1JDN"
SQ SEQUENCE 541 AA; 59808 MW; 8A66415F7F7D62B7 CRC64;
MPSLLVLTFS PCVLLGWALL AGGTGGGGVG GGGGGAGIGG GRQEREALPP QKIEVLVLLP
QDDSYLFSLT RVRPAIEYAL RSVEGNGTGR RLLPPGTRFQ VAYEDSDCGN RALFSLVDRV
AAARGAKPDL ILGPVCEYAA APVARLASHW DLPMLSAGAL AAGFQHKDSE YSHLTRVAPA
YAKMGEMMLA LFRHHHWSRA ALVYSDDKLE RNCYFTLEGV HEVFQEEGLH TSIYSFDETK
DLDLEDIVRN IQASERVVIM CASSDTIRSI MLVAHRHGMT SGDYAFFNIE LFNSSSYGDG
SWKRGDKHDF EAKQAYSSLQ TVTLLRTVKP EFEKFSMEVK SSVEKQGLNM EDYVNMFVEG
FHDAILLYVL ALHEVLRAGY SKKDGGKIIQ QTWNRTFEGI AGQVSIDANG DRYGDFSVIA
MTDVEAGTQE VIGDYFGKEG RFEMRPNVKY PWGPLKLRID ENRIVEHTNS SPCKSSGGLE
ESAVTGIVVG ALLGAGLLMA FYFFRKKYRI TIERRTQQEE SNLGKHRELR EDSIRSHFSV
A
