ID C0A010_CYPCA Unreviewed; 1107 AA.
AC C0A010;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Guanylate cyclase {ECO:0000256|ARBA:ARBA00012202, ECO:0000256|RuleBase:RU003431};
DE EC=4.6.1.2 {ECO:0000256|ARBA:ARBA00012202, ECO:0000256|RuleBase:RU003431};
GN Name=GC-RR1 {ECO:0000313|EMBL:BAH28862.1};
OS Cyprinus carpio (Common carp).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Cyprinus.
OX NCBI_TaxID=7962 {ECO:0000313|EMBL:BAH28862.1};
RN [1] {ECO:0000313|EMBL:BAH28862.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=19556550; DOI=10.1073/pnas.0812781106;
RA Takemoto N., Tachibanaki S., Kawamura S.;
RT "High cGMP synthetic activity in carp cones.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:11788-11793(2009).
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: Photoreceptor outer segment membrane
CC {ECO:0000256|ARBA:ARBA00004451}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004451}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000256|RuleBase:RU000405}.
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DR EMBL; AB469894; BAH28862.1; -; mRNA.
DR AlphaFoldDB; C0A010; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004383; F:guanylate cyclase activity; IEA:UniProtKB-EC.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR CDD; cd07302; CHD; 1.
DR CDD; cd06371; PBP1_sensory_GC_DEF-like; 1.
DR CDD; cd14043; PK_GC-2D; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 6.10.250.780; -; 1.
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; 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 PANTHER; PTHR11920:SF477; GUANYLATE CYCLASE D; 1.
DR PANTHER; PTHR11920; GUANYLYL CYCLASE; 1.
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 PRINTS; PR00109; TYRKINASE.
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; 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 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, ECO:0000256|SAM:Phobius};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Vision {ECO:0000256|ARBA:ARBA00023305}.
FT TRANSMEM 33..50
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 471..495
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 539..812
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 885..1015
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT COILED 822..860
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1107 AA; 124702 MW; F2647E9CF4EFD772 CRC64;
MQHIHLLFGG ALWELSSYPC CPILRSRQSL STLPFYSITL WIILGVLTFP CCVQCLIFKV
GVLGPWNCDP YYAKSLPAIA SKLAVGRINE DFSLDLGCTM DFVILQEACE TSKALTSFVQ
YENMVDAFVG PTNPGYCNAA ALMGKNWDKS IFSWACINYE LDRVQGYPTF ARTLPSPTRV
LFSVLKYFSL ANIAIVSSNE DIWIDTAAKL ASALRNQGLP VGIVVSMGNN DTMLEKTLLS
IRNAGEIKVI IMCMHSALIG GEQQTSFLMK AYDMGLTKGQ YVFIPYDTLL YSLPYTNTTY
FPLQNNTKLR KAYDAVLTIT IESDLMSFNE AYNMAKRLGE LMVSQEPEQV SPLFGTIYNS
LYLLAKSMHN ARRAGKWFSG SNLASFTRNI TFSGFNQNIR MDAQGNGQTD YVILDTDGWG
SELYRCFYVN LMLDKVLFAG TYIHFPAGSP PPSDSSCWFD PSAICTGGVD ILYVIIAFVI
VLIMVLGSIG LSLFIRRRIQ QIQLIKGPNR ILLTLEDLTF INPQLSNKKI TLEDLCDSKS
YIEEKSTGEL SHSVNSMATA THETSNVAVY EGDWVWLKKF KEGDFKEVKQ STTKIFTKMK
DLRNENVNPF LGFFTDCETF AIVTEHCSRG SLHDLLRNED VKLDWMFKSS LVLDLIKGMK
YLHHREFPHG HLKSRNCVVD GRFVLKITDY GYNEILETQK APKETPPPED LFWTAPEFLR
DPESPRKGTY KGDVYSFAII LQEVVVRGAP YCMLGLSPEE IIRKVKKPPP MCRPTVAPDQ
APLECIQLMK QCWSEQPDRR PPFDQIFDQF KLINKGKKTN IIDSMLRMLE QYSSNLEDLI
RERTEELEVE KQRTEKLLAE MLPPSVAEAL KTGASVEPEY FDQVTIYFSD IVGFTTISSL
SDPIEVVDLL NDLYTLFDAV LGSHDVYKVE TIGDAYMVAS GLPKRNGNKH AAEIANMSLN
ILSSVGTFKM RHMPDVPVRI RIGIHSGSCV AGVVGLTMPR YCLFGDTVNT ASRMESTGLP
YRIHVNISTV NILRSLNDGY QIEVRGKTEL KGKGIEETYW LVGKSNFTKP LPKPPEIKPG
DNWQDMVTEE IKSLFRKANR QVDKPKI
//