GUC2D_CANLF
ID GUC2D_CANLF Reviewed; 1109 AA.
AC O19179;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Retinal guanylyl cyclase 1;
DE Short=RETGC-1;
DE EC=4.6.1.2 {ECO:0000250|UniProtKB:P55203};
DE AltName: Full=Guanylate cyclase 2D, retinal;
DE AltName: Full=Guanylate cyclase E {ECO:0000303|PubMed:9651484};
DE Short=GC-E {ECO:0000303|PubMed:9651484};
DE AltName: Full=Rod outer segment membrane guanylate cyclase;
DE Short=ROS-GC;
DE Flags: Precursor;
GN Name=GUCY2D; Synonyms=GUC2D;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Beagle X Briard; TISSUE=Leukocyte, and Retina;
RX PubMed=9651484; DOI=10.1016/s0005-2736(98)00047-9;
RA Veske A., Nilsson S.E.G., Gal A.;
RT "Organization of the canine gene encoding the E isoform of retinal
RT guanylate cyclase (cGC-E) and exclusion of its involvement in the inherited
RT retinal dystrophy of the Swedish Briard and Briard-beagle dogs.";
RL Biochim. Biophys. Acta 1372:69-77(1998).
CC -!- FUNCTION: Catalyzes the synthesis of cyclic GMP (cGMP) in rods and
CC cones of photoreceptors. Plays an essential role in phototransduction,
CC by mediating cGMP replenishment. May also participate in the
CC trafficking of membrane-associated proteins to the photoreceptor outer
CC segment membrane. {ECO:0000250|UniProtKB:P52785}.
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:0000250|UniProtKB:P55203};
CC -!- ACTIVITY REGULATION: Activated by GUCA1A when free calcium ions
CC concentration is low, and inhibited by GUCA1A when free calcium ions
CC concentration is high (By similarity). Negatively regulated by RD3; RD3
CC inhibits the basal and GUCA1A-stimulated guanylate cyclase activity (By
CC similarity). {ECO:0000250|UniProtKB:P52785,
CC ECO:0000250|UniProtKB:Q02846}.
CC -!- SUBUNIT: Homodimer; requires homodimerization for guanylyl cyclase
CC activity (By similarity). Interacts (via C-terminus) with RD3 (via C-
CC terminus); promotes the exit of GUCY2D from the endoplasmic reticulum
CC and its trafficking to the photoreceptor outer segments (By
CC similarity). Interaction with RD3 negatively regulates GUCY2D guanylate
CC cyclase activity (By similarity). {ECO:0000250|UniProtKB:P51840,
CC ECO:0000250|UniProtKB:Q02846}.
CC -!- SUBCELLULAR LOCATION: Photoreceptor outer segment membrane
CC {ECO:0000250|UniProtKB:Q02846}; Single-pass type I membrane protein
CC {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q02846}; Single-pass type I membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in retina. Low expression in cerebrum
CC (occipital lobe). {ECO:0000269|PubMed:9651484}.
CC -!- PTM: There are 9 conserved cysteine residues in sensory guanylate
CC cyclases, 6 in the extracellular domain, which may be involved in
CC intra- or interchain disulfide bonds.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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DR EMBL; Y15484; CAA75656.1; -; Genomic_DNA.
DR EMBL; Y15483; CAA75655.1; -; mRNA.
DR RefSeq; NP_001003207.1; NM_001003207.1.
DR AlphaFoldDB; O19179; -.
DR SMR; O19179; -.
DR STRING; 9615.ENSCAFP00000024862; -.
DR PaxDb; O19179; -.
DR GeneID; 403863; -.
DR KEGG; cfa:403863; -.
DR CTD; 3000; -.
DR eggNOG; KOG1023; Eukaryota.
DR InParanoid; O19179; -.
DR OrthoDB; 229634at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0001750; C:photoreceptor outer segment; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0001653; F:peptide receptor activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0006182; P:cGMP biosynthetic process; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
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; IPR011645; HNOB_dom_associated.
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; PF07701; HNOBA; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00044; CYCc; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
DR SUPFAM; SSF55073; SSF55073; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 2: Evidence at transcript level;
KW Cell projection; cGMP biosynthesis; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; GTP-binding; Lyase; Membrane; Nucleotide-binding;
KW Reference proteome; Sensory transduction; Signal; Transmembrane;
KW Transmembrane helix; Vision.
FT SIGNAL 1..55
FT /evidence="ECO:0000250|UniProtKB:P55203"
FT CHAIN 56..1109
FT /note="Retinal guanylyl cyclase 1"
FT /id="PRO_0000012380"
FT TOPO_DOM 56..466
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 467..491
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 492..1109
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 492..810
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 884..1014
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 453
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 461
FT /note="Interchain"
FT /evidence="ECO:0000305"
SQ 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
