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Database: UniProt
Entry: H2MGW7_ORYLA
LinkDB: H2MGW7_ORYLA
Original site: H2MGW7_ORYLA 
ID   H2MGW7_ORYLA            Unreviewed;      1043 AA.
AC   H2MGW7;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, 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=gucy2ca {ECO:0000313|Ensembl:ENSORLP00000017861.2};
OS   Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC   Oryzias.
OX   NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000017861.2, ECO:0000313|Proteomes:UP000001038};
RN   [1] {ECO:0000313|Ensembl:ENSORLP00000017861.2, ECO:0000313|Proteomes:UP000001038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000017861.2,
RC   ECO:0000313|Proteomes:UP000001038};
RX   PubMed=17554307; DOI=10.1038/nature05846;
RA   Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA   Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA   Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA   Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA   Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA   Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT   "The medaka draft genome and insights into vertebrate genome evolution.";
RL   Nature 447:714-719(2007).
RN   [2] {ECO:0000313|Ensembl:ENSORLP00000017861.2}
RP   IDENTIFICATION.
RC   STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000017861.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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|ARBA:ARBA00036920};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13666;
CC         Evidence={ECO:0000256|ARBA:ARBA00036920};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC       Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC       Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004115}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004115}.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC       family. {ECO:0000256|RuleBase:RU000405}.
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DR   AlphaFoldDB; H2MGW7; -.
DR   Ensembl; ENSORLT00000017862.2; ENSORLP00000017861.2; ENSORLG00000014236.2.
DR   eggNOG; KOG1023; Eukaryota.
DR   GeneTree; ENSGT00940000155955; -.
DR   HOGENOM; CLU_001072_1_3_1; -.
DR   TreeFam; TF106338; -.
DR   Proteomes; UP000001038; Chromosome 8.
DR   Bgee; ENSORLG00000014236; Expressed in intestine and 6 other cell types or tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma 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   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; 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:SF347; GUANYLYL CYCLASE C; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
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   3: Inferred from homology;
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, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001038};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..1043
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017273581"
FT   TRANSMEM        399..424
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          425..708
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          783..913
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
SQ   SEQUENCE   1043 AA;  119720 MW;  648158E23CF33C98 CRC64;
     MYGLQSLLFL GTLTMLVSND MLDDCLESNP RYTMNVVLLE DNTYEWSRPF VQEAVEGAIK
     KDAEENRKAG LNFTLTANYN WFNTNLYNRQ GCGSSTCEGV AILKKLHVEV GCVMLGPSCT
     FATFQLVDME IGLSLSIPVI SAGSFGLSCD YKPKLTRILP PARKVSDSLV YFFNEKNMLK
     PIWEKAYVYK KSNNVTEDCF WYNNALEAPS AHFASSKKRE MLRGEEELKK ALTSKYRFSN
     IFILCGSVDD IVSIKGLAKQ FHEDTIFILI DLYNPEYYIN TTSLAPMRDV LVVTLPPRNY
     VNESNSTFNN TINDYVAGYH DSALLFGEVL RRKMLSQHVP LSDTPFGNIS FEGMAGNYVL
     DEYGDRDVNF TFIYTSAQTS KDVNHLYLCL LADLSTQDII VIVLGVSVVV VTAIALIFYS
     VWIFSKPLRL CPLGFHLTTF NIYDLFTEQI DEDKRKDSTF FSHRGRYDKK PVVLKELKHP
     DEDFTEEQKI ELNTLLRIDY YNLTKFYGTV KFEYGVFGVF ELCQRGSLRY ILNDRISYPD
     ETFMDMEFKI SVMYDIAKGM SYLHTSNIPV HGRLKSTNCE VDNRMVVKIT DFGCHTILKP
     AKDLWTAPEH LRKDGVSQKG DVYSYAIIAH EIVTRKPPFY TQYCSDSAEK MYRVQYPRNN
     NFFRPELNFE GASDRETEVY MLIKNCWDED PERRPDFKKI ELTLGKIFSN LHNQATETYM
     DNLIRRLQMY SRTLENLVEE RTALYKAERD RADHLNFMLL PGPVVRSLKE TGRVEPELFE
     EVTIYFSDIV GFTTLCHYST PMEVVDMLNN IYKNFDSILD HHDVYKVETI GDAYMVASGL
     PNRNGDRHAV DIAHMALDIL SFVGTFELQH LPGIPLWIRI GVHSGPCAAG VVGNKMPRYC
     LFGDTVNTAS RMESTGLPLR IHVSQSTIKI LQRTPCKFEF EQRGETYLKG KGKEMTYWLT
     GVTGGNYNLP TPPTAENFQR LQQDLADMII SSLEKREGGK ETIEKRKTLS TRIRWKDRNN
     SFQKESPPEY FHLAVTENPS TYL
//
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