ID V4BA20_LOTGI Unreviewed; 968 AA.
AC V4BA20;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 63.
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=LOTGIDRAFT_138137 {ECO:0000313|EMBL:ESP02582.1};
OS Lottia gigantea (Giant owl limpet).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Patellogastropoda; Lottioidea; Lottiidae; Lottia.
OX NCBI_TaxID=225164 {ECO:0000313|EMBL:ESP02582.1, ECO:0000313|Proteomes:UP000030746};
RN [1] {ECO:0000313|EMBL:ESP02582.1, ECO:0000313|Proteomes:UP000030746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(2013).
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: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane 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; KB200170; ESP02582.1; -; Genomic_DNA.
DR RefSeq; XP_009046722.1; XM_009048474.1.
DR AlphaFoldDB; V4BA20; -.
DR EnsemblMetazoa; LotgiT138137; LotgiP138137; LotgiG138137.
DR GeneID; 20234006; -.
DR KEGG; lgi:LOTGIDRAFT_138137; -.
DR CTD; 20234006; -.
DR HOGENOM; CLU_001072_1_3_1; -.
DR OMA; NDSIAME; -.
DR OrthoDB; 3683909at2759; -.
DR Proteomes; UP000030746; 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; 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:SF494; 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 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:UP000030746};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 394..418
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 470..728
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 795..925
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT COILED 732..763
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 968 AA; 110298 MW; 32ECEE2563ED1168 CRC64;
MALEYVKEKY NDTIDFKYVY RDGGRICGPA KAAHAASEVY YSENVTVFIG PACSLAVEQM
AYMATIWNIP VITPSGTSGI LADKEAFPIL IRIAFGMQEF AALYLKLFKL YSWRHVALLY
ESDVSFNKII GGTFYEAFRT SRLSLVHFQI SKDMTFEESR HVLRKANENA RVFVLLATTK
TIRKLMLAAH SLQYTNGDHV FIATYPVYEK MNIWYKNDEN DSIAMEAAQS LLLVNLEQKF
DSEYIQFNDE LVSRSYIDYG FDYGDIEPNI LLPRFYDAVL IYAEILNETL VEGGDPLDGL
AIVTKMKNRT FHGKSGRISI NANGDRYTDL VLYDMTLPDM GAFEIVGFYD GKLQEYTPNY
YKKIQWPGDK GPPPDIPECG FRDDTCPQQG LSKVFVISLS SCFGALAVMT FIIGILCYRR
WRGNARQDLW WWKIQLEELI FDKRTQNGSS ISFMGRGISV HHGLCLIYLQ RASLKSEINN
FSDVHVGIAL YKGITVQVRE LNVSDIPITN QLLNEFKEIR DINQNNIVKV FGACFHPISS
FLVIEHCSKG TLQDVVGNTE IKLDAHFKFS LAIDIAQGMT FIHQSSIHHH GNLSSMVCLI
DNRFSVKITD VGLRYLYSYI KKDKLSQEYI NGKCNYFTKE GDVYSFGIIL QEILTRDSPF
SLETSELGAK DVLMKVKENS GEPFRPKVDH VSPNTSDMLT LMKKCWQEDP HSRPIFSSIV
KELKHMTSGN LLDNLLRRME LYANNLEKMV DEKTLELNEE KKRSEELLYQ ILPRSVAERL
KRGLRVEPEA FDCITIYFSD ICGFTTISAR SKPMEVVNLL NDLYSCFDDI LEGFDVYKVE
TIGDAYMVAS GLPQRNGHKH AEEIARMSLA LLKAIDSFRM RHLPDEKLKL RIGLHSGPVC
AGVVGVKMPR YCLFGDTVNT ASRMESHGEG LKIHMSESTN KILQQNNFFE IVKRGDIEIK
VMNTSEYC
//
