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Database: UniProt
Entry: C0A011_CYPCA
LinkDB: C0A011_CYPCA
Original site: C0A011_CYPCA 
ID   C0A011_CYPCA            Unreviewed;      1076 AA.
AC   C0A011;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 79.
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-RR2 {ECO:0000313|EMBL:BAH28863.1};
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:BAH28863.1};
RN   [1] {ECO:0000313|EMBL:BAH28863.1}
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   -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC       family. {ECO:0000256|RuleBase:RU000405}.
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DR   EMBL; AB469895; BAH28863.1; -; mRNA.
DR   AlphaFoldDB; C0A011; -.
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   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; -; 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; 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; GUANYLYL CYCLASE; 1.
DR   PANTHER; PTHR11920:SF349; RETINAL GUANYLYL CYCLASE 2; 1.
DR   Pfam; PF01094; ANF_receptor; 1.
DR   Pfam; PF00211; Guanylate_cyc; 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};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000405};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
SQ   SEQUENCE   1076 AA;  121157 MW;  A288130A95CA6E9C CRC64;
     MQRPSSAFHS LRPARATRGL QIPDQSTHKY TYLCLWPLLS TVSFLCLFPA TFAATVRVGV
     VGPWSCDPLF TKAQPGVAAQ LAVDHINRDP YLSQGITFDY VILEEDCETS QAFARFLGFY
     TRASGFIGPV NPGYCEAASL LGKSWNKAVF SWSCIGHELD DARSHPTFAR TMPLPSLVLL
     RFMHHFRWAH VGIITSAEDA WFEAGLKLAS ALRSHGMPVS IVASVRNDHT SVRKTLARVK
     KVADLRLVIL VMHSVLIGGG TQKLLLETAY DMQMTDGSLV FLSYDTLFYS LPYHHVTQPA
     LRHNSKLLRA YDAVLTITIE SPQEQSFYQA FERAQEQGEL PRNLRPQQVS PLFGTIYSSI
     VFMAHAVQSV RASGQWMSGG NIAQNARNLL SKGFSLQANF SDFGTLDYVV LDTDGFSWEL
     QPTHHIEMQT DMVRFLGWPI HFPPAGPPKT DSSCWFTHGL ICRGGVNLLH MVLIFLSGFL
     FIFFSIGCSY CIRRKISKIR MVRGPNKILL TLNDVTFINP SLSNKKLSLD DSKASDSRMS
     ISERSLKSPL SIQSPATYEN SNVVIYEGDW AWLKRLPYGN FRSITPHTSD VFELMKDMRH
     ENVNPFLGFF HDCGVFAIVT EYCSRGSLED LLLNDDVKLD WMFKSSLILD LIKGMKYLHH
     RNICHGRLKS RNCVVDGRFV LKITDYGYNE VLEAQRFPYV EPPAETLLWT APEILRGPYP
     GLYGSHPGDV YSFSIIMQEV VMRGPPYCML ENSFDEIVQK IRKPPPMCRP IVSPDHAPME
     CIQLMKQCWN EQPEKRPTFD EIFDQFKNVN KGKKTNIIDS MLRMLEQYSS NLEELIRERT
     EELEIEKQKT EKLLTQMLPT SVAEALKRGT TVEPEYFDSV SLYFSDIVGF TTISANSEPI
     EVVDLLNDLY TTFDAVIGDH DVYKVETIGD AYMVASGVPM PNGNRHAAEI ANMALDILSA
     VGTFKMRHMP DVPVRIRIGL HTGSCVAGVV GLTMPRYCLF GDTVTTASRM ESTGLPYRIH
     VHSSTVKVLM ELKSGYKVEL RARTELKGKG VEETYWLTGR DGFTKPLPVP PVLKSG
//
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