ID W5JE51_ANODA Unreviewed; 1208 AA.
AC W5JE51;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 67.
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 ORFNames=AND_007261 {ECO:0000313|EMBL:ETN61094.1};
OS Anopheles darlingi (Mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=43151 {ECO:0000313|EMBL:ETN61094.1};
RN [1] {ECO:0000313|EMBL:ETN61094.1, ECO:0000313|Proteomes:UP000000673}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20920257; DOI=10.1186/1471-2164-11-529;
RA Mendes N.D., Freitas A.T., Vasconcelos A.T., Sagot M.F.;
RT "Combination of measures distinguishes pre-miRNAs from other stem-loops in
RT the genome of the newly sequenced Anopheles darlingi.";
RL BMC Genomics 11:529-529(2010).
RN [2] {ECO:0000313|EMBL:ETN61094.1}
RP NUCLEOTIDE SEQUENCE.
RA Almeida L.G., Nicolas M.F., Souza R.C., Vasconcelos A.T.R.;
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ETN61094.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23761445;
RA Marinotti O., Cerqueira G.C., de Almeida L.G., Ferro M.I., Loreto E.L.,
RA Zaha A., Teixeira S.M., Wespiser A.R., Almeida E Silva A.,
RA Schlindwein A.D., Pacheco A.C., Silva A.L., Graveley B.R., Walenz B.P.,
RA Lima Bde A., Ribeiro C.A., Nunes-Silva C.G., de Carvalho C.R., Soares C.M.,
RA de Menezes C.B., Matiolli C., Caffrey D., Araujo D.A., de Oliveira D.M.,
RA Golenbock D., Grisard E.C., Fantinatti-Garboggini F., de Carvalho F.M.,
RA Barcellos F.G., Prosdocimi F., May G., Azevedo Junior G.M., Guimaraes G.M.,
RA Goldman G.H., Padilha I.Q., Batista Jda S., Ferro J.A., Ribeiro J.M.,
RA Fietto J.L., Dabbas K.M., Cerdeira L., Agnez-Lima L.F., Brocchi M.,
RA de Carvalho M.O., Teixeira Mde M., Diniz Maia Mde M., Goldman M.H.,
RA Cruz Schneider M.P., Felipe M.S., Hungria M., Nicolas M.F., Pereira M.,
RA Montes M.A., Cantao M.E., Vincentz M., Rafael M.S., Silverman N.,
RA Stoco P.H., Souza R.C., Vicentini R., Gazzinelli R.T., Neves Rde O.,
RA Silva R., Astolfi-Filho S., Maciel T.E., Urmenyi T.P., Tadei W.P.,
RA Camargo E.P., de Vasconcelos A.T.;
RT "The genome of Anopheles darlingi, the main neotropical malaria vector.";
RL Nucleic Acids Res. 41:7387-7400(2013).
RN [4] {ECO:0000313|EnsemblMetazoa:ADAC007261-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) 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:ARBA00001436,
CC ECO:0000256|RuleBase:RU003431};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC protein {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; ADMH02001784; ETN61094.1; -; Genomic_DNA.
DR AlphaFoldDB; W5JE51; -.
DR STRING; 43151.W5JE51; -.
DR EnsemblMetazoa; ADAC007261-RA; ADAC007261-PA; ADAC007261.
DR VEuPathDB; VectorBase:ADAC007261; -.
DR VEuPathDB; VectorBase:ADAR2_004796; -.
DR eggNOG; KOG1023; Eukaryota.
DR HOGENOM; CLU_001072_1_3_1; -.
DR OMA; GNSPDCH; -.
DR OrthoDB; 3683909at2759; -.
DR Proteomes; UP000000673; Unassembled WGS sequence.
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 CDD; cd06352; PBP1_NPR_GC-like; 1.
DR Gene3D; 3.40.50.2300; -; 3.
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; IPR001170; ANPR/GUC.
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:SF274; GUANYLATE CYCLASE; 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; PR00255; NATPEPTIDER.
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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000405};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:ETN61094.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000673};
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..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1208
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010155319"
FT TRANSMEM 581..604
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 646..927
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1000..1130
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT COILED 937..968
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1208 AA; 135145 MW; C6C126D02030168D CRC64;
MAYVDRWFVV VLVLLLQCTL LQTALCGPSE THRDRRAGRS LEDTELGMLL SSLCGTNCDG
EGSDYSLEED ESGILVPAAL VSGAGKMNGT SGTASAVAAT ATATNRIQKR SLNKLEVAPV
PKDANYTVYY VGVLMASHLD SPFDLERCGP AIDLALDIVN HSLKKAHNVQ LLKVQAAYAS
CSGSKSPGLA ADMHFKYSVI AFIGPACAFA LEPVAQLADY WNTPIITGMG DQPPSEGELS
VTSGILGRLS NRWKNDSSGI FKDKSRYQTL TRTSYCQCRL KLVFSSIFRQ FGWRHIALII
DRSDLFSLTV GKNLEYGLKD EELLKFVREL DGNEEEDIEA YLTDAAMYAR VIILSVRGSL
VRRFMLSALA LDMTKGDFTF LDVEIFQSSY WGDHYWELGD EDDFKARKAY EALLRVSLLQ
PTSPTYQEFA DKVRIRAKQT YNYTFVEDEE VNFFIGAFFD GVYLLGMALN DTLNEGGDIR
DGTAITRKMW GRDFEGITGH VRIDDNGDRD ADYSILDLDP ITGRFEVVAH YYGITREYSP
VKGQKIHWPG GGEGPPPDIP KCGFLGTGPA CVEKDDHKRI IILYGLVGFG IISAFAAAVT
YVLCKQMKLN SELNNMAWRV RPDEVLLEVG KMFGSKMGLQ KLNYENFSLQ QFGLNSGRVS
IASGNSQLPA QLFTTIGIYK GERVAIKKVA KKKVYITSTL LWEIKQARDV SHENTVRFVG
ACIDLPRPTI LILTEYCPKG SLKDVLENEA IQLDWNFRMS LIHDMVKGMA YLHNSDVGVH
GKLRSCNCLI DGRFVLKISD FGLRTLTTPS EFVRDQTYYN KLLWVAPELL HATVIPGTPA
TQKGDVYSFA IILEEIVVRG GPYETARQFM DPQAIIDRVA LHESPPFRPF VGQRDCPPDL
LDLMEKCWSD SPDDRPTFSG IRSSVRLIMK GFCENLMDDL LRRMEQYANN LESLVEEKTE
ELSMEKRRTE ELLYQVLPRP VAQQLLAGEM VQPEQFECVT IYFSDIVGFT ALCAQSRPME
VVDFLNDLYS TFDRIIGFYD VYKVETIGDA YMVVSGLPER NGRDHAREIG LMALAILDAV
KSFTIKHKPD YQLKIRIGIH SGPVCAGVVG QKMPHYCLFG DTVNTASRME STGHPLKIHV
SDAAKQILDK FGTFRMELRG DVELKGKGIV TTYWLLECSE PDPRPPTPMR NYNENEVPFP
ILFPAIGK
//
