ID A0A1S3NMQ6_SALSA Unreviewed; 1075 AA.
AC A0A1S3NMQ6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
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 Name=LOC106580330 {ECO:0000313|RefSeq:XP_014016703.1,
GN ECO:0000313|RefSeq:XP_014016713.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014016703.1};
RN [1] {ECO:0000313|RefSeq:XP_014016703.1, ECO:0000313|RefSeq:XP_014016713.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014016703.1,
RC ECO:0000313|RefSeq:XP_014016713.1};
RG RefSeq;
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 RefSeq; XP_014016703.1; XM_014161228.1.
DR RefSeq; XP_014016713.1; XM_014161238.1.
DR STRING; 8030.ENSSSAP00000051209; -.
DR PaxDb; 8030-ENSSSAP00000051209; -.
DR GeneID; 106580330; -.
DR KEGG; sasa:106580330; -.
DR OrthoDB; 3683909at2759; -.
DR Proteomes; UP000087266; Chromosome ssa02.
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 CDD; cd14042; PK_GC-A_B; 1.
DR Gene3D; 3.40.50.2300; -; 2.
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; 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:SF483; 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; PS51257; PROKAR_LIPOPROTEIN; 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 Receptor {ECO:0000313|RefSeq:XP_014016703.1,
KW ECO:0000313|RefSeq:XP_014016713.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
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..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1075
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010814085"
FT TRANSMEM 486..506
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 551..814
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 889..1019
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT COILED 826..857
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1075 AA; 122255 MW; 32DAAD22C96AD87F CRC64;
MRMQGEKLLL VLLLLLGACL QWVQSGKSSR HRDSHRHPRE HRDHRQHRNI TLAIILPQRN
TAYPWAWPRV GPALDRAIDT INTDPALLPG HHLGYVFENS ENEEGICSES IAPLMAVDLK
FAYDPWAFIG PGCDYTSSPV GLFTTHWDIP MVTAGAPAVG FNGINMYPSI TNTGPTHKKL
GKFGLHICKH FEWKEQVLLM FSDNKKDDRP CYFAVEGLYT ELHLNNITSV DLVFEENTGP
VNYSDLLHNI KQDGRVVFVC CSPDTFRQLM VHFRRAGLPQ EEFVFFYIDM FGRSLDSQNA
QPWARGDQDD LVAKEAFQSV KILTYREPQN PEYKDFVRDL KTDAKRMFNF TVEDSLMNII
SGGFYDGLML YTHALNETMT SPEDRPVGKT VTRRMWNRTY NGVTGLVQID ENGDRETDFA
FWDMTDTNTS VFQIVSVYNG SQKKLRALPG MDIQWPGGAA PLDVPVCGFK NDNPACLART
ITIHQMVTIV VFFIIIIILT ITVFIYRKLK LENELVAQLW RVSWEDIQMS NMEKVLRSAG
SKLTLSLRGS NYGSLLTGDG NFQVFAKTGY YKANIVAIKY INRKRIELTR NVLFELKHMR
DIQNEHLTRF IGACIDPPNI CIITEYCPRG SLQDIMENES ITLDWMFRYS LINDIVKGMA
FLHNSVIVSH GNLKSSNCVV DNRFVLKITD YGLSSFRTES NTDDAHAYYA RKLWMAPELL
RLESPPPCGT QKGDVYSFGI ILQEVALRHG AFYLEGEPLS PKEIMDRVAL GEWPCLRPAV
NPQIHSQELG QLMQRCWAEE PTERPEFNHI KLLLRKQNRE CSTNILDNLL SRMEQYANNL
EELVEERTQA YHEEKRKAEA LLYQILPHSV AEQLKRGETV QAEAFDSVTI YFSDIVGFTA
ISAESTPMQV VTLLNDLYTC FDAIIDNFDV YKVETIGDAY MVVSGLPVRN GKLHGREIAR
MALALLNAVR TFKIRHRPDQ QLKLRIGIHS GPVCAGVVGL KMPRYCLFGD TVNTSSRLES
NGEALKIHVS AATRDVLQEF NCFQLELRGD VAMKGKGKMT TYWLLGESKS NESTS
//
