ID W5M3H3_LEPOC Unreviewed; 1043 AA.
AC W5M3H3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 60.
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};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000002931.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000002931.1}
RP IDENTIFICATION.
RG Ensembl;
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: 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; AHAT01020470; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01020471; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01020472; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5M3H3; -.
DR STRING; 7918.ENSLOCP00000002931; -.
DR Ensembl; ENSLOCT00000002937.1; ENSLOCP00000002931.1; ENSLOCG00000002488.1.
DR eggNOG; KOG1023; Eukaryota.
DR GeneTree; ENSGT00940000156223; -.
DR HOGENOM; CLU_001072_1_3_1; -.
DR InParanoid; W5M3H3; -.
DR OMA; FGPFTKM; -.
DR Proteomes; UP000018468; Linkage group LG4.
DR Bgee; ENSLOCG00000002488; Expressed in testis and 2 other cell types or tissues.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004016; F:adenylate cyclase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004383; F:guanylate cyclase activity; IBA:GO_Central.
DR GO; GO:0016941; F:natriuretic peptide receptor activity; IBA:GO_Central.
DR GO; GO:0017046; F:peptide hormone binding; IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0006182; P:cGMP biosynthetic process; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; IBA:GO_Central.
DR CDD; cd07302; CHD; 1.
DR CDD; cd06352; PBP1_NPR_GC-like; 1.
DR CDD; cd12087; TM_EGFR-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; 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:SF464; 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:UP000018468};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 451..472
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 505..785
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 856..986
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
SQ SEQUENCE 1043 AA; 118107 MW; 854A5F550F76CA98 CRC64;
LDFKLLISMP NTSSQFHVGR IGAGALIAID EINRNSILLK VYLLGHRLVY EYVDDECDAI
RGPGKIVSLQ HNQNYSAFIG PSCSKVCSHV GRLAGYWNIA VVSPICADSE FLDKKEFPTM
TRVFGPFTKM GSFFVKICEK FNWRRIGIIY DTSPTWTIPA GGIRLYYTVQ GLVNSDTGSF
HHFSSIGQRA MRNEIELSHQ LSVKHINIRH NSSLLAKCMQ IKYLNDILIN AHNQGLINGE
YVFFCFEPYE QKQRCKAGGG AVSGCKLQRR DAYDSIAREA YQALFLLTLY KPDNERYMNF
SAEVIRRSKE DFGYQYEPGE KVSVLPAIAH DSVWLYAHAL NETISENGDP YNGTAISRKM
WNRTITGIQG EVTIDDNGDR ESSYMMYHVQ NKSNGTFQVI ANYFGTRKNY EQVPGLSIVW
PGGRSTPPLD TPVCGFTEEM CEDDSKARTT IIAVGLIGGL LAVVIVGLSL LYRKYKLQEK
ASLMLWKVNF SEVSMMETKH NSSVYKKLEI FLRGYTYKAI SESENTQSDF LFTKAAMYKE
NICSIRFLHV KSINLNNELI NELRQCRDLN HPNVCSFIGA CLESPHHCLL TEYCPKGSLQ
DILKNDSIKL DWMFKYSLML DIVKGMDYIH KSYLRSHGHL SSSNCVVDSR FVLKITDFGL
SNLRRPNTAG IQNSKEHWQC LLWRAPELLR GNMPTNGTQK GDVYSFGIIA QEIVYRNGVF
FIPSCVLKAN EIIEKVKEGG SNSFRPYTDT TECPGPLAML MKSCWRERPS ERPDFTSLKA
TVKKLDRGSD NILDNLLSRM EQYASNLEDI VNERTAQLLE EKKKAESLLT QMLPRSVAIQ
LISGKTVQAE TYDCVTIYFS DIVGFTAMSA GITPMQVVDL LNDLYTYFDN IIDNHDVYKV
ETIGDAYMVV SGLPIRNGDE HAKEIARMSL SIVDAMKKFE NRHVPGQQLK VRIGLHSGPC
VAGVVGLKMP RYCLFGDTVN TASRMESYGL PLKVHVSSSA KDLLDKFRTF RFELRGDIHM
KGKGLVRTFW LLGEETKRHW NDI
//