ID G5BV55_HETGA Unreviewed; 1074 AA.
AC G5BV55;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 68.
DE RecName: Full=Guanylate cyclase {ECO:0000256|RuleBase:RU003431};
DE EC=4.6.1.2 {ECO:0000256|RuleBase:RU003431};
GN ORFNames=GW7_19639 {ECO:0000313|EMBL:EHB13169.1};
OS Heterocephalus glaber (Naked mole rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Heterocephalus.
OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB13169.1, ECO:0000313|Proteomes:UP000006813};
RN [1] {ECO:0000313|EMBL:EHB13169.1, ECO:0000313|Proteomes:UP000006813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993625; DOI=10.1038/nature10533;
RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT "Genome sequencing reveals insights into physiology and longevity of the
RT naked mole rat.";
RL Nature 479:223-227(2011).
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}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000256|RuleBase:RU000405}.
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DR EMBL; JH172079; EHB13169.1; -; Genomic_DNA.
DR AlphaFoldDB; G5BV55; -.
DR STRING; 10181.G5BV55; -.
DR eggNOG; KOG1023; Eukaryota.
DR InParanoid; G5BV55; -.
DR OMA; VNFWKAN; -.
DR Proteomes; UP000006813; Unassembled WGS sequence.
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 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:SF347; HEAT-STABLE ENTEROTOXIN RECEPTOR; 1.
DR Pfam; PF01094; ANF_receptor; 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 Receptor {ECO:0000313|EMBL:EHB13169.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006813};
KW Signal {ECO:0000256|ARBA:ARBA00022729, 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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1074
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003474762"
FT TRANSMEM 432..455
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 490..750
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 825..955
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
SQ SEQUENCE 1074 AA; 123081 MW; A99984F5C5F15300 CRC64;
MKSPLLGLAL WALLLQLFQP LLAYWASQMS QKCHSGSYEI SVLMMNNSAF GEALDDLKAA
VNLGLEIVRE HLQKAGVNVT VNATFIYSEG LIYKSGDCRS STCEGLDLLR AITREKQMGC
ALMGPSCTYA TYQMYLDTEL NFPMISAGSF GLSCDYKETL TRMMSPARKL LYFLVDFWRV
NNLPFKTFSW NTSYVFKNGT ESEYCFWYIN ALEAGVSYFS QVLSFKDTVR GTDELQNILK
SRNRRSNVIV MCGTPQTLES LDLTGAEDIV IILVDLFNNY YFEDNVIAPD YMKNVLVLTL
PPGNSTINSS LSKRFSQGRT DFALAYLDGT LLFGHVLKTF LENGEIITTS KFAHAFRNLT
FEGSTGPVTL DGCGDIDNVM VLLYTSVDTK KYKVLLTYDT HINQTTSMDT SPTFIWKNHK
LPNDIPGRGP QILMIAVFAL AGVLVLLLLI ALLVLRKYKK DNELRQKKWS HIPPENIFPL
ETNETNHVSL KIDDDKRRDT IQRLRQCKYD QKRVILKDLK HCDGNFTEKQ KIELNKLLQS
DYYNLTKFYG TVKLDTRIFG VVEYCERGSL REVLNDTISY PDGTFMDWEF KISVLYDIAK
GMSYLHSSKI EVHGRLKSTN CVVDSRMVVK ITDFGCNSIL PPKKDLWTAP EHLRQAKSSQ
KGDVYSFGII AQEIVLRRET FYTLSCRDQK EKIFRVENYD ELKPFRPDLF LETAEEKELE
VYLLVKNCWE EDPEKRPDFK KIENTLAKIF GLFHDQKNES YMDTLIRRLQ LYSRNLEHLV
EERTQLYKAE RDRADRLNFM LLPRLVVQSL KEKGIVEPEL YEEVTIYFSD IVGFTTICKY
STPMEVVDML NDLYKSFDQI VDRHDVYKVE TIGDAYVVAS GLPMRNGNRH AIDISKMALD
ILSFIGTFEL EHLPGLPVWI RIGVHSGPCA AGVVGIKMPR YCLFGDTVNT ASRMESTGLP
LRIHMSSSTI AILKRTQCQF LYEVRGETYL KGRGTETTYW LTGMKDQEYN LPTPPTVENQ
QRLQAEFSDM ITSSLQKRQA AGIKRRKPTQ IASYKKGSLE YLQLNTTDQD NTYF
//