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Retinal guanylyl cyclase 1 (RETGC-1) (EC 4.6.1.2) (Guanylate cyclase 2D, retinal) (Guanylate cyclase E) (GC-E) (Rod outer segment membrane guanylate cyclase) (ROS-GC)

 GUC2D_CANLF             Reviewed;        1109 AA.
O19179;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
22-NOV-2017, entry version 119.
RecName: Full=Retinal guanylyl cyclase 1;
Short=RETGC-1;
EC=4.6.1.2;
AltName: Full=Guanylate cyclase 2D, retinal;
AltName: Full=Guanylate cyclase E;
Short=GC-E;
AltName: Full=Rod outer segment membrane guanylate cyclase;
Short=ROS-GC;
Flags: Precursor;
Name=GUCY2D; Synonyms=GUC2D;
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
STRAIN=Beagle X Briard; TISSUE=Leukocyte, and Retina;
PubMed=9651484; DOI=10.1016/S0005-2736(98)00047-9;
Veske A., Nilsson S.E.G., Gal A.;
"Organization of the canine gene encoding the E isoform of retinal
guanylate cyclase (cGC-E) and exclusion of its involvement in the
inherited retinal dystrophy of the Swedish Briard and Briard-beagle
dogs.";
Biochim. Biophys. Acta 1372:69-77(1998).
-!- CATALYTIC ACTIVITY: GTP = 3',5'-cyclic GMP + diphosphate.
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- TISSUE SPECIFICITY: Expressed in retina. Low expression in
cerebrum (occipital lobe). {ECO:0000269|PubMed:9651484}.
-!- PTM: There are 9 conserved cysteine residues in sensory guanylate
cyclases, 6 in the extracellular domain, which may be involved in
intra- or interchain disulfide bonds.
-!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl
cyclase family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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EMBL; Y15484; CAA75656.1; -; Genomic_DNA.
EMBL; Y15483; CAA75655.1; -; mRNA.
RefSeq; NP_001003207.1; NM_001003207.1.
UniGene; Cfa.3724; -.
ProteinModelPortal; O19179; -.
SMR; O19179; -.
STRING; 9615.ENSCAFP00000024862; -.
PaxDb; O19179; -.
GeneID; 403863; -.
KEGG; cfa:403863; -.
CTD; 3000; -.
eggNOG; KOG1023; Eukaryota.
eggNOG; COG2114; LUCA.
HOGENOM; HOG000293307; -.
HOVERGEN; HBG098487; -.
InParanoid; O19179; -.
KO; K12321; -.
Proteomes; UP000002254; Unplaced.
GO; GO:0008074; C:guanylate cyclase complex, soluble; IBA:GO_Central.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:InterPro.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0004383; F:guanylate cyclase activity; IBA:GO_Central.
GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
GO; GO:0006182; P:cGMP biosynthetic process; IBA:GO_Central.
GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
GO; GO:0007165; P:signal transduction; IBA:GO_Central.
GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
Gene3D; 3.30.70.1230; -; 1.
InterPro; IPR001054; A/G_cyclase.
InterPro; IPR018297; A/G_cyclase_CS.
InterPro; IPR001828; ANF_lig-bd_rcpt.
InterPro; IPR011645; HNOB_dom_associated.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR029787; Nucleotide_cyclase.
InterPro; IPR028082; Peripla_BP_I.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
Pfam; PF01094; ANF_receptor; 1.
Pfam; PF00211; Guanylate_cyc; 1.
Pfam; PF07701; HNOBA; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
SMART; SM00044; CYCc; 1.
SUPFAM; SSF53822; SSF53822; 1.
SUPFAM; SSF55073; SSF55073; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
2: Evidence at transcript level;
cGMP biosynthesis; Complete proteome; Disulfide bond; Glycoprotein;
GTP-binding; Lyase; Membrane; Nucleotide-binding; Reference proteome;
Sensory transduction; Signal; Transmembrane; Transmembrane helix;
Vision.
SIGNAL 1 55 {ECO:0000250}.
CHAIN 56 1109 Retinal guanylyl cyclase 1.
/FTId=PRO_0000012380.
TOPO_DOM 56 466 Extracellular. {ECO:0000255}.
TRANSMEM 467 491 Helical. {ECO:0000255}.
TOPO_DOM 492 1109 Cytoplasmic. {ECO:0000255}.
DOMAIN 492 810 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 884 1014 Guanylate cyclase. {ECO:0000255|PROSITE-
ProRule:PRU00099}.
CARBOHYD 301 301 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 453 453 Interchain. {ECO:0000305}.
DISULFID 461 461 Interchain. {ECO:0000305}.
SEQUENCE 1109 AA; 119899 MW; A8C641498DCC6E90 CRC64;
MSACALLAGG LPDPRLCAPA RWARSPPGVP GAPPWPQPRL RLLLLLLLLP PSALSAVFTV
GVLGPWACDP IFARARPDLA ARLAAARLNR DAALEDGPRF EVTLLPEPCR TPGSLGAVSS
ALGRVSGLVG PVNPAACRPA ELLAQEAGVA LVPWSCPGTR AGGTTAPAGT PAADALYALL
RAFRWARVAL ITAPQDLWVE AGRALSAALR ARGLPVALVT TMEPSDLSGA REALRRVQDG
PRVRAVIMVM HSVLLGGEEQ RCLLQAAEEL GLADGSLVFL PFDTLHYALS PGPEALAVLA
NSSQLRRAHD AVLILTRHCP PGGSVMDNLR RAQEHQELPS DLDLQQVSPF FGTIYDAVLL
LAGGVARARA AAGGGWVSGA TVAHHIPDAQ VPGFCGTLGG AQEPPFVLLD TDAAGDRLFA
TYMLDPTRGS LLSAGTPVHF PRGGGTPGSD PSCWFEPGVI CNGGVEPGLV FLGFLLVVGM
GLTGAFLAHY LRHRLLHIQM VSGPNKIILT LDDVTFLHPH GGSTRKVVQG SRSSLAARST
SDIRSVPSQP LDNSNIGLFE GDWVWLKKFP GDQHIAIRPA TKTAFSKLRE LRHENVVLYL
GLFLGSGGAG GSAAGEGVLA VVSEHCARGS LHDLLAQRDI KLDWMFKSSL LLDLIKGMRY
LHHRGVAHGR LKSRNCVVDG RFVLKVTDHG HARLMEAQRV LLEPPSAEDQ LWTAPELLRD
PALERRGTLP GDVFSLGIIM QEVVCRSAPY AMLELTPEEV VERVRSPPPL CRPSVSMDQA
PVECIQLMKQ CWAEHPDLRP SLGHIFDQFK SINKGRKTNI IDSMLRMLEQ YSSNLEDLIR
ERTEELELEK QKTDRLLTQM LPPSVAEALK MGTPVEPEYF EEVTLYFSDI VGFTTISAMS
EPIEVVDLLN DLYTLFDAII GSHDVYKVET IGDAYMVASG LPQRNGQRHA AEIANMALDI
LSAVGSFRMR HMPEVPVRIR IGLHSGPCVA GVVGLTMPRY CLFGDTVNTA SRMESTGLPY
RIHVNMSTVR ILHALDEGFQ TEVRGRTELK GKGAEDTYWL VGRRGFNKPI PKPPDLQPGA
SNHGISLQEI PLDRRWKLEK ARPGQFSGK


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