ID G1SR19_RABIT Unreviewed; 1044 AA.
AC G1SR19;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Guanylate cyclase {ECO:0000256|RuleBase:RU003431};
DE EC=4.6.1.2 {ECO:0000256|RuleBase:RU003431};
GN Name=NPR2 {ECO:0000313|Ensembl:ENSOCUP00000005582.3};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000005582.3, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000005582.3, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000005582.3,
RC ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000005582.3}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000005582.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Receptor for the C-type natriuretic peptide NPPC/CNP hormone.
CC Has guanylate cyclase activity upon binding of its ligand. May play a
CC role in the regulation of skeletal growth.
CC {ECO:0000256|ARBA:ARBA00043880}.
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:0000256|RuleBase:RU003431};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000256|RuleBase:RU000405}.
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DR EMBL; AAGW02033518; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02033519; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1SR19; -.
DR SMR; G1SR19; -.
DR STRING; 9986.ENSOCUP00000005582; -.
DR PaxDb; 9986-ENSOCUP00000005582; -.
DR Ensembl; ENSOCUT00000006456.3; ENSOCUP00000005582.3; ENSOCUG00000006453.3.
DR eggNOG; KOG1023; Eukaryota.
DR GeneTree; ENSGT00940000156985; -.
DR HOGENOM; CLU_001072_1_3_1; -.
DR InParanoid; G1SR19; -.
DR TreeFam; TF106338; -.
DR Proteomes; UP000001811; Chromosome 1.
DR Bgee; ENSOCUG00000006453; Expressed in aorta and 18 other cell types or tissues.
DR GO; GO:0005929; C:cilium; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0043005; C:neuron projection; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004383; F:guanylate cyclase activity; IEA:UniProtKB-EC.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0016941; F:natriuretic peptide receptor activity; IEA:Ensembl.
DR GO; GO:0017046; F:peptide hormone binding; IEA:Ensembl.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0060466; P:activation of meiosis involved in egg activation; IEA:Ensembl.
DR GO; GO:0060385; P:axonogenesis involved in innervation; IEA:Ensembl.
DR GO; GO:0008015; P:blood circulation; IEA:Ensembl.
DR GO; GO:0001974; P:blood vessel remodeling; IEA:Ensembl.
DR GO; GO:0061939; P:c-di-GMP signaling; IEA:Ensembl.
DR GO; GO:0071321; P:cellular response to cGMP; IEA:Ensembl.
DR GO; GO:0097011; P:cellular response to granulocyte macrophage colony-stimulating factor stimulus; IEA:Ensembl.
DR GO; GO:1901653; P:cellular response to peptide; IEA:Ensembl.
DR GO; GO:0007268; P:chemical synaptic transmission; IEA:Ensembl.
DR GO; GO:0002062; P:chondrocyte differentiation; IEA:Ensembl.
DR GO; GO:0035988; P:chondrocyte proliferation; IEA:Ensembl.
DR GO; GO:0051276; P:chromosome organization; IEA:Ensembl.
DR GO; GO:0048668; P:collateral sprouting; IEA:Ensembl.
DR GO; GO:0001549; P:cumulus cell differentiation; IEA:Ensembl.
DR GO; GO:0048546; P:digestive tract morphogenesis; IEA:Ensembl.
DR GO; GO:0001958; P:endochondral ossification; IEA:Ensembl.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0097194; P:execution phase of apoptosis; IEA:Ensembl.
DR GO; GO:0030540; P:female genitalia development; IEA:Ensembl.
DR GO; GO:0035483; P:gastric emptying; IEA:Ensembl.
DR GO; GO:0035112; P:genitalia morphogenesis; IEA:Ensembl.
DR GO; GO:0003417; P:growth plate cartilage development; IEA:Ensembl.
DR GO; GO:0035108; P:limb morphogenesis; IEA:Ensembl.
DR GO; GO:0001945; P:lymph vessel development; IEA:Ensembl.
DR GO; GO:0000165; P:MAPK cascade; IEA:Ensembl.
DR GO; GO:1903537; P:meiotic cell cycle process involved in oocyte maturation; IEA:Ensembl.
DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR GO; GO:0051447; P:negative regulation of meiotic cell cycle; IEA:Ensembl.
DR GO; GO:1900194; P:negative regulation of oocyte maturation; IEA:Ensembl.
DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0019228; P:neuronal action potential; IEA:Ensembl.
DR GO; GO:0036342; P:post-anal tail morphogenesis; IEA:Ensembl.
DR GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; IEA:Ensembl.
DR GO; GO:0071774; P:response to fibroblast growth factor; IEA:Ensembl.
DR GO; GO:0034699; P:response to luteinizing hormone; IEA:Ensembl.
DR GO; GO:1902074; P:response to salt; IEA:Ensembl.
DR GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
DR GO; GO:0048745; P:smooth muscle tissue development; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR GO; GO:0001964; P:startle response; IEA:Ensembl.
DR GO; GO:0007033; P:vacuole organization; IEA:Ensembl.
DR GO; GO:0061042; P:vascular wound healing; IEA:Ensembl.
DR GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
DR GO; GO:0021647; P:vestibulocochlear nerve maturation; IEA:Ensembl.
DR GO; GO:0050872; P:white fat cell differentiation; IEA:Ensembl.
DR CDD; cd07302; CHD; 1.
DR CDD; cd14042; PK_GC-A_B; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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 PANTHER; PTHR11920:SF508; ATRIAL NATRIURETIC PEPTIDE RECEPTOR 2; 1.
DR PANTHER; PTHR11920; GUANYLYL CYCLASE; 1.
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; SSF55073; Nucleotide cyclase; 1.
DR SUPFAM; SSF53822; Periplasmic binding protein-like I; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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 3: Inferred from homology;
KW cGMP biosynthesis {ECO:0000256|ARBA:ARBA00023293,
KW ECO:0000256|RuleBase:RU003431}; Coiled coil {ECO:0000256|SAM:Coils};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000405};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Osteogenesis {ECO:0000256|ARBA:ARBA00022855};
KW Reference proteome {ECO:0000313|Proteomes:UP000001811};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1044
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5023890895"
FT DOMAIN 510..783
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 858..988
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT COILED 795..822
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1044 AA; 116449 MW; 441EA343992492AF CRC64;
MALPSLLLLV AALAGGVRPP GARNLTLAVV LPEHNLSYAW AWPRVGPAVA LAVEALGRAL
PVDLRFVSSE LDGACSEYLA PLRAVDLKLY HDPDLLLGPG CVYPAASVAR FASHWRLPLL
TAGAVASGFA AKSEHYRTLV RTGPSAPKLG EFVVTLHEHF NWTSRAALLY LDARTDDRPH
YFTIEGVFEA LQGNNLSVQH QVYAREPGGP EQATHFIRAN GRIVYICGPL EMLHEILLQA
QRENLTNGDY VFFYLDVFGE SLRAGPTRST GRPWQDNRTQ EQAQALREAF QTVLVITYRE
PPNPEYQEFQ NRLLIRARED FGVELAPSLM NLIAGCFYDG ILLYAEVLNE TLQEGGTRED
GLRIDVAWVG TSQGQGWGQA LRQLEGPRER GAGPWAQLSA SSQPAAHYSG AEKQIWWTER
PIAWVKGAPP LDNPPCAFDL DDPSCDKTPL STLAIVALGT GITFIMFGVS SFLIFRKLML
EKELASMLWR IRWEELQFGN SERCHKGAGS RLTLSLRGSS YGSLMTAHGK YQIFANTGHF
KGNVVAIKHV NKKRIELTRQ VLFELKHMRD VQFNHLTRFI GACIDPPNIC IVTEYCPRGS
LQDILENDSI NLDWMFRYSL INDLVKGMAF LHNSIISSHG SLKSSNCVVD SRFVLKITDY
GLASFRSTAE PDDSHALYAK KLWTAPELLS GNSLPTTGMQ KADVYSFGII LQEIALRSGP
FYLEGLDLSP KEIVQKVRNG QRPYFRPSID RTQLNEELVL LMERCWAQDP AERPDFGQIK
GFIRRFNKEG GTSILDNLLL RMEQYANNLE KLVEERTQAY LEEKRKAEAL LYQILPHSVA
EQLKRGETVQ AEAFDSVTIY FSDIVGFTAL SAESTPMQVV TLLNDLYTCF DAIIDNFDVY
KVETIGDAYM VVSGLPGRNG QRHAPEIARM ALALLDAVSS FRIRHRPHDQ LRLRIGVHTG
PVCAGVVGLK MPRYCLFGDT VNTASRMESN GQALKIHVSS TTKDALDELG CFQLELRGDV
EMKGKGKMRT YWLLGERKGS PGLL
//
