ID V4ALG5_LOTGI Unreviewed; 1026 AA.
AC V4ALG5;
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_153062 {ECO:0000313|EMBL:ESO97952.1};
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:ESO97952.1, ECO:0000313|Proteomes:UP000030746};
RN [1] {ECO:0000313|EMBL:ESO97952.1, 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; KB201304; ESO97952.1; -; Genomic_DNA.
DR RefSeq; XP_009051792.1; XM_009053544.1.
DR AlphaFoldDB; V4ALG5; -.
DR EnsemblMetazoa; LotgiT153062; LotgiP153062; LotgiG153062.
DR GeneID; 20235855; -.
DR KEGG; lgi:LOTGIDRAFT_153062; -.
DR CTD; 20235855; -.
DR HOGENOM; CLU_001072_1_3_1; -.
DR OMA; MEIANMS; -.
DR OrthoDB; 2877804at2759; -.
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; 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:SF509; GUANYLATE CYCLASE; 1.
DR PANTHER; PTHR11920; GUANYLYL CYCLASE; 1.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF00211; Guanylate_cyc; 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};
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 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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1026
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004717302"
FT TRANSMEM 449..471
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 490..773
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 845..975
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
SQ SEQUENCE 1026 AA; 115786 MW; C498BE792763567B CRC64;
MGFYLFVFCA LCVGATYVTS VTEIKIGTLL ISEHHAPYTM ERVGPALDVA FDEINSNILN
ESYKLVQVKV AYDNICNARY ATGVASKLYY EEKIVALIGP ACSYALDGVA RLAGFWNIPI
VTGLGDGGMF KNKTDYPTLT RFSYCQCRMR KVFGSVFKQF NWTDIVVIYD VNDGHTDILG
NTLKEGLQKG GIFPFMIPYY GKENNNFSSI LQEASVHARI IVLIVPGESL RQFLLAAFGL
GYTTGDYVFF DVELFSFPGQ YWGNHDWRRG DDKDTEAKTA FESLLRVSWQ EPSGMGWMNF
SCNVKDIALS KYNYSFGDEK VNFFVGSFHD AAVRLGLAIN ETLSTGGNLS DGYTITRLMW
TKTLPGVTGP VIIDNNGDRD TDFAILDMDP IDGNFKVVAN YWGANPGYNA VDHRSYHWPG
RDTPPPNTPR CGFTGTNPVC KSPDTSEKFI WTIISVFVFI ITCLIVGFFV YRRYKWEQDL
TNMAWRVQYE DIRFKLLDGV SSRTSMARIS DTFCADVVHE SSVTLGIYKG RTVAVQKVDK
EKIVLTRDVL LELKQVRDLH HENLSSFIGA CIEPGHNYVL TEYCNKGSLQ DVLGNDTLKL
DMMFRLSMLR DIAMGMAFIH KSDLKIHGFL NSSNCLVDGK FVLKITEFGL PTFFRDKRYS
QSKENMEMLL WVAPEVLRQA PFMQSTQKSD VYSFGIIMEE MILRSIPFDT YRALLDVQDI
VDKVKDDCAP YFRPKVSESQ APKGYIELMK KCWSEIPDER PTYDGIAKQL KELQGDKNIS
LVEALVLRLE EYASNLENLV AERTTQLIAE KKKSETLLYQ ILPKPVADQL KQGKSVVPET
YDCVTIYFSD IVGFTALSSE SSPMEIVNFL NDLYVMFDSV VDYYDAYKVE TIGDAYMVVS
GLPIRNGEQH AVEISRMSLA LLDGIKSFTI RHRPQDMLKL RIGIHSGPCA SGVVGLKMPR
YCLFGDTVNT TSRMESTGEA LKIHISEKTK SILDRMGNFI TEYRGSIAMK GKGEQTTYWL
VGEKSF
//
