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Database: UniProt
Entry: A0A1U8CPT3_MESAU
LinkDB: A0A1U8CPT3_MESAU
Original site: A0A1U8CPT3_MESAU 
ID   A0A1U8CPT3_MESAU        Unreviewed;      1108 AA.
AC   A0A1U8CPT3;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 35.
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=Gucy2f {ECO:0000313|RefSeq:XP_012977758.1};
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_012977758.1};
RN   [1] {ECO:0000313|RefSeq:XP_012977758.1}
RP   IDENTIFICATION.
RG   RefSeq;
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|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   RefSeq; XP_012977758.1; XM_013122304.1.
DR   AlphaFoldDB; A0A1U8CPT3; -.
DR   STRING; 10036.ENSMAUP00000018336; -.
DR   GeneID; 101840848; -.
DR   KEGG; maua:101840848; -.
DR   CTD; 2986; -.
DR   eggNOG; KOG1023; Eukaryota.
DR   OrthoDB; 3683909at2759; -.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0120200; C:rod photoreceptor outer segment; IEA:Ensembl.
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:0050908; P:detection of light stimulus involved in visual perception; IEA:Ensembl.
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   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; 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; 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; PF07701; HNOBA; 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}; 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   Reference proteome {ECO:0000313|Proteomes:UP000189706};
KW   Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
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        468..490
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          532..812
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          884..1014
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   COILED          821..848
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1108 AA;  124692 MW;  EE3FEA157382FF20 CRC64;
     MFLGPWPFSR LLSWFAISSN LSRHHGLASC RFLQYVCLLA LLSLIRWVQA VPYKIGVIGP
     WTCDPFFSKA LPKVAARLAI ERISRDVSFD RSYSFEYVIL DEDCQTSKAL SSFISHQQMA
     SGFIGPANPG YCEAASLLGN SWDKGIFSWA CVNHELDNKH SYPTFSRTLP SPIRVLVTVM
     KYFQWAHAGV ISSDEDIWLH TANRVSSALQ SHGLPVGVVL TTGQDSQSIQ KALQHIRQAD
     RIRIIILCMH SALIGGETQT HFLELAHELK MTDGTYVFVP YDVLLYSLPY KHTPYQVLRN
     NQKLREAYDA VLTITVESHE KTFYEAYTEA TASGEIPEKL DSHQVSPLFG TIYNSIYFIA
     QAMNNAMKEN GQASATSLVQ HSRNMRFYGF NQLIRTDSNG NGISEYVILD TNGKEWELRS
     TYTVDMETEL LRFRGTPIHF PGGRPTSADA KCWFAEGKIC QGGIDPALAM MVCLALLIAL
     LSINGFAYFI RRRINKIQLI KGPNRILLTL EDVTFINPHF GSKRGSRASV SFQIISEVQS
     GRSPRLSFSS GSLTPATYEN SNIAIYEGDW VWLKKFPPGD FGDIKSIKSR ASDVFEMMKD
     LRHENVNPLL GFFCDSGMFA IVTEFCSRRS LEDILTNDDV KLDWMFKSSL LLDLIKGMKY
     LHHREFIHGR LKSRNCVVDG RFVLKVTDYG FNDILEMLSL SEEEPSEEEL LWTAPELLKA
     PRGIRLGSFA GDVYSFAIIM QEVMVRGPPF CMMDLPAKEI IDRLQKPPPV YRPVVSPEYA
     PLECLQLMKQ CWAEAAEQRP TFDEIFNQFK TFNKGKKTNI IDSMLRMLEQ YSSNLEDLIR
     ERTEELEIEK QKTEKLLTQM LPPSVAESLK KGCTVEPEGF DLVTLYFSDI VGFTTISAMS
     EPIEVVDLLN DLYTLFDAII GSHDVYKVET IGDAYMVASG LPKRNGSRHA AEIANMSLDI
     LSSVGTFKMR HMPEVPVRIR IGLHSGPVVA GVVGLTMPRY CLFGDTVNTA SRMESTGLPY
     RIHVSLSTVT ILQTLSEGYE VELRGRTELK GKGTEETFWL IGKKGFTKPL PVPPPVGKDG
     QVGHGLQPAE IAAFQRKKAE RQLVRNKP
//
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