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ANPRA_MOUSE
ID   ANPRA_MOUSE             Reviewed;        1057 AA.
AC   P18293;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 2.
DT   03-AUG-2022, entry version 196.
DE   RecName: Full=Atrial natriuretic peptide receptor 1;
DE            EC=4.6.1.2;
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; Synonyms=Npra;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=1973687; DOI=10.1016/s0021-9258(19)38352-8;
RA   Pandey K.N., Singh S.;
RT   "Molecular cloning and expression of murine guanylate cyclase/atrial
RT   natriuretic factor receptor cDNA.";
RL   J. Biol. Chem. 265:12342-12348(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7838126;
RA   Schoenfeld J.R., Sehl P., Quan C., Burnier J.P., Lowe D.G.;
RT   "Agonist selectivity for three species of natriuretic peptide receptor-A.";
RL   Mol. Pharmacol. 47:172-180(1995).
RN   [3]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=9405681; DOI=10.1073/pnas.94.26.14730;
RA   Oliver P.M., Fox J.E., Kim R., Rockman H.A., Kim H.S., Reddick R.L.,
RA   Pandey K.N., Milgram S.L., Smithies O., Maeda N.;
RT   "Hypertension, cardiac hypertrophy, and sudden death in mice lacking
RT   natriuretic peptide receptor A.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:14730-14735(1997).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Kidney, Liver, Lung, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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.
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   -!- 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   -!- DISRUPTION PHENOTYPE: Mice display systemic hypertension associated
CC       with cardiac hypertrophy and ventricular enlargement.
CC       {ECO:0000269|PubMed:9405681}.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC       family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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DR   EMBL; J05504; AAA37670.1; -; mRNA.
DR   EMBL; L31932; AAA66945.1; -; mRNA.
DR   CCDS; CCDS17529.1; -.
DR   PIR; A36568; OYMSAR.
DR   PIR; I57963; I57963.
DR   RefSeq; NP_032753.5; NM_008727.5.
DR   AlphaFoldDB; P18293; -.
DR   SMR; P18293; -.
DR   BioGRID; 201830; 4.
DR   ComplexPortal; CPX-34; ANPR-A receptor complex.
DR   STRING; 10090.ENSMUSP00000029540; -.
DR   GlyGen; P18293; 6 sites.
DR   iPTMnet; P18293; -.
DR   PhosphoSitePlus; P18293; -.
DR   CPTAC; non-CPTAC-3386; -.
DR   PaxDb; P18293; -.
DR   PRIDE; P18293; -.
DR   ProteomicsDB; 281996; -.
DR   Antibodypedia; 20386; 307 antibodies from 32 providers.
DR   DNASU; 18160; -.
DR   Ensembl; ENSMUST00000029540; ENSMUSP00000029540; ENSMUSG00000027931.
DR   GeneID; 18160; -.
DR   KEGG; mmu:18160; -.
DR   UCSC; uc008qcg.1; mouse.
DR   CTD; 4881; -.
DR   MGI; MGI:97371; Npr1.
DR   VEuPathDB; HostDB:ENSMUSG00000027931; -.
DR   eggNOG; KOG1023; Eukaryota.
DR   GeneTree; ENSGT00940000156223; -.
DR   HOGENOM; CLU_001072_1_3_1; -.
DR   InParanoid; P18293; -.
DR   OMA; KCAYEKS; -.
DR   OrthoDB; 229634at2759; -.
DR   PhylomeDB; P18293; -.
DR   TreeFam; TF106338; -.
DR   BRENDA; 4.6.1.2; 3474.
DR   Reactome; R-MMU-5578768; Physiological factors.
DR   BioGRID-ORCS; 18160; 1 hit in 75 CRISPR screens.
DR   ChiTaRS; Npr1; mouse.
DR   PRO; PR:P18293; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; P18293; protein.
DR   Bgee; ENSMUSG00000027931; Expressed in yolk sac and 75 other tissues.
DR   ExpressionAtlas; P18293; baseline and differential.
DR   Genevisible; P18293; MM.
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; ISO:MGI.
DR   GO; GO:0043235; C:receptor complex; ISO:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004383; F:guanylate cyclase activity; IDA:MGI.
DR   GO; GO:0042562; F:hormone binding; ISO:MGI.
DR   GO; GO:0016941; F:natriuretic peptide receptor activity; ISS:UniProtKB.
DR   GO; GO:0017046; F:peptide hormone binding; ISO:MGI.
DR   GO; GO:0001653; F:peptide receptor activity; IBA:GO_Central.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; ISO:MGI.
DR   GO; GO:0006182; P:cGMP biosynthetic process; ISO:MGI.
DR   GO; GO:0019934; P:cGMP-mediated signaling; ISO:MGI.
DR   GO; GO:0042417; P:dopamine metabolic process; ISO:MGI.
DR   GO; GO:0035556; P:intracellular signal transduction; ISO:MGI.
DR   GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; ISO:MGI.
DR   GO; GO:0010753; P:positive regulation of cGMP-mediated signaling; ISO:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; ISO:MGI.
DR   GO; GO:0008217; P:regulation of blood pressure; IDA:ComplexPortal.
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..28
FT   CHAIN           29..1057
FT                   /note="Atrial natriuretic peptide receptor 1"
FT                   /id="PRO_0000012361"
FT   TOPO_DOM        29..469
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        470..490
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        491..1057
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          524..801
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          872..1002
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT   BINDING         81
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250"
FT   BINDING         113
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250"
FT   BINDING         114
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         515
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P16066"
FT   MOD_RES         525
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P16066"
FT   MOD_RES         528
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P16066"
FT   MOD_RES         530
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P16066"
FT   MOD_RES         534
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P16066"
FT   MOD_RES         538
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P18910"
FT   MOD_RES         541
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P18910"
FT   CARBOHYD        41
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        208
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        334
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        375
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        382
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        423
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        88..114
FT                   /evidence="ECO:0000250"
FT   DISULFID        192..241
FT                   /evidence="ECO:0000250"
FT   DISULFID        451..460
FT                   /evidence="ECO:0000250"
FT   CONFLICT        3
FT                   /note="G -> R (in Ref. 1; AAA37670)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        39
FT                   /note="L -> V (in Ref. 1; AAA37670)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        122
FT                   /note="G -> D (in Ref. 1; AAA37670)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        130
FT                   /note="V -> L (in Ref. 1; AAA37670)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        285
FT                   /note="R -> E (in Ref. 1; AAA37670)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        301
FT                   /note="A -> R (in Ref. 1; AAA37670)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        404..405
FT                   /note="FS -> SP (in Ref. 1; AAA37670)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        590
FT                   /note="H -> Q (in Ref. 1; AAA37670)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        652
FT                   /note="G -> C (in Ref. 1; AAA37670)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        833
FT                   /note="A -> P (in Ref. 1; AAA37670)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        958
FT                   /note="R -> G (in Ref. 1; AAA37670)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1044
FT                   /note="T -> S (in Ref. 1; AAA37670)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1050
FT                   /note="E -> D (in Ref. 1; AAA37670)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1055..1057
FT                   /note="TRG -> SRA (in Ref. 1; AAA37670)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1057 AA;  119109 MW;  53A544FB2C8EF253 CRC64;
     MPGSRRVRPR LRALLLLPPL LLLRSGHASD LTVAVVLPLT NTSYPWSWAR VGPAVELALG
     RVKARPDLLP GWTVRMVLGS SENAAGVCSD TAAPLAAVDL KWEHSPAVFL GPGCVYSAAP
     VGRFTAHWRV PLLTAGAPAL GIGVKDEYAL TTRTGPSHVK LGDFVTALHR RLGWEHQALV
     LYADRLGDDR PCFFIVEGLY MRVRERLNIT VNHQEFVEGD PDHYTKLLRT VQRKGRVIYI
     CSSPDAFRNL MLLALDAGLT GEDYVFFHLD VFGQSLQGAQ GPVPRKPWER DDGQDRRARQ
     AFQAAKIITY KEPDNPEYLE FLKQLKLLAD KKFNFTMEDG LKNIIPASFH DGLLLYVQAV
     TETLAQGGTV TDGENITQRM WNRSFQGVTG YLKIDRNGDR DTDFSLWDMD PETGAFRVVL
     NFNGTSQELM AVSEHRLYWP LGYPPPDIPK CGFDNEDPAC NQDHFSTLEV LALVGSLSLV
     SFLIVSFFIY RKMQLEKELV SELWRVRWED LQPSSLERHL RSAGSRLTLS GRGSNYGSLL
     TTEGQFQVFA KTAYYKGNLV AVKRVNRKRI ELTRKVLFEL KHMRDVQNEH LTRFVGACTD
     PPNICILTEY CPRGSLQDIL ENESITLDWM FRYSLTNDIV KGMLFLHNGA IGSHGNLKSS
     NCVVDGRFVL KITDYGLESF RDPEPEQGHT LFAKKLWTAP ELLRMASPPA RGSQAGDVYS
     FGIILQEIAL RSGVFYVEGL DLSPKEIIER VTRGEQPPFR PSMDLQSHLE ELGQLMQRCW
     AEDPQERPPF QQIRLALRKF NKENSSNILD NLLSRMEQYA NNLEELVEER TQAYLEEKRK
     AEALLYQILP HSVAEQLKRG ETVQAEAFDS VTIYFSDIVG FTALSAESTP MQVVTLLNDL
     YTCFDAVIDN FDVYKVETIG DAYMVVSGLP VRNGQLHARE VARMALALLD AVRSFRIRHR
     PQEQLRLRIG IHTGPVCAGV VGLKMPRYCL FGDTVNTASR MESNGEALRI HLSSETKAVL
     EEFDGFELEL RGDVEMKGKG KVRTYWLLGE RGCSTRG
 
 
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